PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 3472524-7 1987 The apparent Km of liver homogenate TL PST for dopamine was 27 microM. Dopamine 47-55 sulfotransferase family 1A member 3 Homo sapiens 36-42 2568905-7 1989 Apparent Km values of TL PST for dopamine and of TS PST for p-nitrophenol were 10 microM and 0.92 microM, respectively. Dopamine 33-41 sulfotransferase family 1A member 3 Homo sapiens 22-28 2568905-7 1989 Apparent Km values of TL PST for dopamine and of TS PST for p-nitrophenol were 10 microM and 0.92 microM, respectively. 4-nitrophenol 60-73 sulfotransferase family 1A member 3 Homo sapiens 22-28 2568905-8 1989 Jejunal mucosal TL PST, like TL PST in other human tissues, also catalyzed the sulfation of p-nitrophenol, but with a very high apparent Km of 1100 microM. 4-nitrophenol 92-105 sulfotransferase family 1A member 3 Homo sapiens 16-22 2568905-8 1989 Jejunal mucosal TL PST, like TL PST in other human tissues, also catalyzed the sulfation of p-nitrophenol, but with a very high apparent Km of 1100 microM. 4-nitrophenol 92-105 sulfotransferase family 1A member 3 Homo sapiens 29-35 3253448-0 1988 STM imaging of molecular collagen and phospholipid membranes. Phospholipids 38-50 sulfotransferase family 1A member 3 Homo sapiens 0-3 3253448-3 1988 We have also used STM to image artificial Langmuir DPE (dipalmitoyl phosphatidyl ethanolamine) phospholipid membranes. 1,2-dipalmitoyl-3-phosphatidylethanolamine 56-93 sulfotransferase family 1A member 3 Homo sapiens 18-21 3253448-3 1988 We have also used STM to image artificial Langmuir DPE (dipalmitoyl phosphatidyl ethanolamine) phospholipid membranes. Phospholipids 95-107 sulfotransferase family 1A member 3 Homo sapiens 18-21 3253448-6 1988 Spikes which periodically protrude from strands in our STM images of collagen appear to represent pyrrolidine ring structures in the amino acids proline and hydroxyproline. pyrrolidine 98-109 sulfotransferase family 1A member 3 Homo sapiens 55-58 3253448-6 1988 Spikes which periodically protrude from strands in our STM images of collagen appear to represent pyrrolidine ring structures in the amino acids proline and hydroxyproline. Proline 145-152 sulfotransferase family 1A member 3 Homo sapiens 55-58 3253448-6 1988 Spikes which periodically protrude from strands in our STM images of collagen appear to represent pyrrolidine ring structures in the amino acids proline and hydroxyproline. Hydroxyproline 157-171 sulfotransferase family 1A member 3 Homo sapiens 55-58 3253448-8 1988 STM imaging of phospholipid membranes show a lattice pattern with densities spaced approximately 4.5 A apart. Phospholipids 15-27 sulfotransferase family 1A member 3 Homo sapiens 0-3 34014236-1 2021 The formation of a two-phase surface molecular overlayer that transitions from isolated propene molecules to a highly ordered 1D chain structure on Cu(111) is elucidated through combined high-resolution STM imaging and DFT-based calculations. Copper 148-150 sulfotransferase family 1A member 3 Homo sapiens 203-206 6586330-2 1984 TL PST was assayed with dopamine as the substrate and TS PST was measured with phenol and with p-nitrophenol. Dopamine 24-32 sulfotransferase family 1A member 3 Homo sapiens 0-6 34014236-1 2021 The formation of a two-phase surface molecular overlayer that transitions from isolated propene molecules to a highly ordered 1D chain structure on Cu(111) is elucidated through combined high-resolution STM imaging and DFT-based calculations. propylene 88-95 sulfotransferase family 1A member 3 Homo sapiens 203-206 2873064-8 1986 In addition, both platelet TS and TL PST activities are correlated significantly with the extent of sulfate conjugation of orally administered drugs such as acetaminophen and methyldopa. Sulfates 100-107 sulfotransferase family 1A member 3 Homo sapiens 34-40 2873064-8 1986 In addition, both platelet TS and TL PST activities are correlated significantly with the extent of sulfate conjugation of orally administered drugs such as acetaminophen and methyldopa. Acetaminophen 157-170 sulfotransferase family 1A member 3 Homo sapiens 34-40 2873064-8 1986 In addition, both platelet TS and TL PST activities are correlated significantly with the extent of sulfate conjugation of orally administered drugs such as acetaminophen and methyldopa. Methyldopa 175-185 sulfotransferase family 1A member 3 Homo sapiens 34-40 17743569-0 1986 STM Evidence for Silicon (111). Silicon 17-24 sulfotransferase family 1A member 3 Homo sapiens 0-3 3859706-1 1985 Human placental estrogen sulfotransferase (ESFT) was partially purified from the term placental cytosol by (NH4)2SO4 precipitation and agarose gel chromatography. Ammonium Sulfate 107-116 sulfotransferase family 1A member 3 Homo sapiens 6-41 3859706-1 1985 Human placental estrogen sulfotransferase (ESFT) was partially purified from the term placental cytosol by (NH4)2SO4 precipitation and agarose gel chromatography. Sepharose 135-142 sulfotransferase family 1A member 3 Homo sapiens 6-41 3855967-4 1985 TS PST catalyzes the sulfate conjugation of micromolar concentrations of phenol and p-nitrophenol and TL PST catalyzes the sulfate conjugation of dopamine and other monoamines. Dopamine 146-154 sulfotransferase family 1A member 3 Homo sapiens 102-108 3855967-4 1985 TS PST catalyzes the sulfate conjugation of micromolar concentrations of phenol and p-nitrophenol and TL PST catalyzes the sulfate conjugation of dopamine and other monoamines. monoamines 165-175 sulfotransferase family 1A member 3 Homo sapiens 102-108 33694297-3 2021 Sharp Kondo resonances near Fermi level, both at the corrole ligand and the silver center, were observed by cryogenic STM, with relatively high Kondo temperature (172 K), providing the first direct spectroscopic evidence for a non-innocent Ag II -corrole 2- species. Silver 76-82 sulfotransferase family 1A member 3 Homo sapiens 118-121 33694297-3 2021 Sharp Kondo resonances near Fermi level, both at the corrole ligand and the silver center, were observed by cryogenic STM, with relatively high Kondo temperature (172 K), providing the first direct spectroscopic evidence for a non-innocent Ag II -corrole 2- species. ag ii 240-245 sulfotransferase family 1A member 3 Homo sapiens 118-121 33881100-1 2021 A combined Tof-SIMS, XPS and STM characterization has been performed to study the deposition of a sulphur-functionalized nitronyl nitroxide radical on Au(111) clearly demonstrating the chemisorption of intact molecules. nitronyl nitroxide radical 121-147 sulfotransferase family 1A member 3 Homo sapiens 29-32 34010994-12 2021 Conclusions: Techniques of STM in supine position plus CT scan under setting A can be combined by Valsalva passive ET opening. valsalva 98-106 sulfotransferase family 1A member 3 Homo sapiens 27-30 33881100-1 2021 A combined Tof-SIMS, XPS and STM characterization has been performed to study the deposition of a sulphur-functionalized nitronyl nitroxide radical on Au(111) clearly demonstrating the chemisorption of intact molecules. Gold 151-153 sulfotransferase family 1A member 3 Homo sapiens 29-32 33686490-12 2021 Peak values of IL6, Syndecan-1, sVEGFR1, and sTM all correlated to peak PGI2. Epoprostenol 72-76 sulfotransferase family 1A member 3 Homo sapiens 45-48 33792326-1 2021 We report the on-surface chemistry of diamantanethiols on metal surfaces by combining low-temperature STM studies with quantum mechanical density functional theory computations. diamantanethiols 38-54 sulfotransferase family 1A member 3 Homo sapiens 102-105 33792326-1 2021 We report the on-surface chemistry of diamantanethiols on metal surfaces by combining low-temperature STM studies with quantum mechanical density functional theory computations. Metals 58-63 sulfotransferase family 1A member 3 Homo sapiens 102-105 33146444-7 2021 LEED and STM assisted by theoretical simulations have been employed to characterize in detail these novel 2D conglomerates with relevant chiral properties for systems with C 3h symmetry. Tritium 174-176 sulfotransferase family 1A member 3 Homo sapiens 9-12 33355460-5 2021 We demonstrate, using STM break-junction technique, single-molecule heterojunction comprising Au-molecule-ITO and Au-molecule-carbon circuits. Gold 94-96 sulfotransferase family 1A member 3 Homo sapiens 22-25 33355460-5 2021 We demonstrate, using STM break-junction technique, single-molecule heterojunction comprising Au-molecule-ITO and Au-molecule-carbon circuits. Gold 114-116 sulfotransferase family 1A member 3 Homo sapiens 22-25 33355460-5 2021 We demonstrate, using STM break-junction technique, single-molecule heterojunction comprising Au-molecule-ITO and Au-molecule-carbon circuits. Carbon 126-132 sulfotransferase family 1A member 3 Homo sapiens 22-25 33346311-0 2021 Collective radical oligomerisation induced by an STM tip on a silicon surface. Silicon 62-69 sulfotransferase family 1A member 3 Homo sapiens 49-52 33179941-3 2020 Herein, we employ an STM break junction (STM-BJ) technique to investigate the acid-base chemistry of carboxylic acid-based molecules at a Au (111) model surface and propose a prototype of a single-molecule pH sensor for the first time. Carboxylic Acids 101-116 sulfotransferase family 1A member 3 Homo sapiens 21-24 33510641-0 2020 Characterization of Formononetin Sulfonation in SULT1A3 Overexpressing HKE293 Cells: Involvement of Multidrug Resistance-Associated Protein 4 in Excretion of Sulfate. formononetin sulfonation 20-44 sulfotransferase family 1A member 3 Homo sapiens 48-55 33305772-0 2020 STM induced manipulation of azulene-based molecules and nanostructures: the role of the dipole moment. azulene 28-35 sulfotransferase family 1A member 3 Homo sapiens 0-3 33216089-0 2020 Adsorption of acetylene on a rutile TiO2(110) surface: a low temperature STM study. Acetylene 14-23 sulfotransferase family 1A member 3 Homo sapiens 73-76 33216089-1 2020 Low temperature scanning tunneling microscopy (LT-STM) has been applied to investigate the adsorption of acetylene (C2H2) on the rutile TiO2(110) surface at 77 K. Through in situ exposing and ex situ annealing experiments we unambiguously demonstrate that C2H2 molecules adsorb weakly on top of the Ti5c ions. Acetylene 105-114 sulfotransferase family 1A member 3 Homo sapiens 50-53 33510641-3 2020 Here, expression-activity correlation was performed to identify the contributing of SULT1A3 to formononetin metabolism. formononetin 95-107 sulfotransferase family 1A member 3 Homo sapiens 84-91 33510641-5 2020 As a result, formononetin sulfonation was significantly correlated with SULT1A3 protein levels (r = 0.728; p < 0.05) in a bank of individual human intestine S9 fractions (n = 9). formononetin sulfonation 13-37 sulfotransferase family 1A member 3 Homo sapiens 72-79 33510641-11 2020 In conclusion, SULT1A3 was of great significance in determining sulfonation of formononetin. formononetin 79-91 sulfotransferase family 1A member 3 Homo sapiens 15-22 33179941-3 2020 Herein, we employ an STM break junction (STM-BJ) technique to investigate the acid-base chemistry of carboxylic acid-based molecules at a Au (111) model surface and propose a prototype of a single-molecule pH sensor for the first time. Carboxylic Acids 101-116 sulfotransferase family 1A member 3 Homo sapiens 41-44 33206100-8 2020 The possibility for the detection of the arrangement of the halogen impurities at the MoX2 basal plane even with the graphene layer deposited on top was demonstrated through STM measurements which will be undoubtedly useful for the fabrication of electronic schemes and elements based on the proposed heterostructures for their further application in nanoelectronics and spintronics. Graphite 117-125 sulfotransferase family 1A member 3 Homo sapiens 174-177 33485192-3 2021 To this end, we have constructed isoform-specific inhibitors of the human cytosolic sulfotransferase 1A3 (SULT1A3)-the isoform responsible for sulfonating ~80% of the serotonin in the extracellular brain fluid. Serotonin 167-176 sulfotransferase family 1A member 3 Homo sapiens 106-113 32966082-3 2020 In this letter, by means of a combined experimental (STM, XPS and LEED) and theoretical (DFT) study, we present a proof of how CO molecules succeed in permeating the graphene layer and get into the confined zone between graphene and the Ni(111) surface. Graphite 166-174 sulfotransferase family 1A member 3 Homo sapiens 53-56 32966082-3 2020 In this letter, by means of a combined experimental (STM, XPS and LEED) and theoretical (DFT) study, we present a proof of how CO molecules succeed in permeating the graphene layer and get into the confined zone between graphene and the Ni(111) surface. Graphite 220-228 sulfotransferase family 1A member 3 Homo sapiens 53-56 32824181-5 2020 In addition, CUC1 and CUC2 are also required for the activation of KLU, a cytochrome P450-encoding gene known to restrict organ production, and KLU counteracts STM in the promotion of meristem activity, providing a possible balancing mechanism for shoot meristem maintenance. klu 144-147 sulfotransferase family 1A member 3 Homo sapiens 160-163 32806015-4 2020 The rhodium wires derived from the terminal acetylene and gold-functionalized precursors show comparable, high single-molecule conductance ((6-7) x 10-3 G0) as determined by the STM break-junction measurements, suggesting formation of virtually the same covalently linked metal electrode-molecule-metal electrode junctions. Acetylene 44-53 sulfotransferase family 1A member 3 Homo sapiens 178-181 32787162-1 2020 We investigate electronic states of Se-substituted 1T-TaS2 by scanning tunneling microscopy/spectroscopy (STM/STS), where superconductivity emerges from the unique Mott-charge-density-wave (Mott-CDW) state. Selenium 36-38 sulfotransferase family 1A member 3 Homo sapiens 106-109 32953370-0 2020 Role of redox-active axial ligands of metal porphyrins adsorbed at solid-liquid interfaces in a liquid-STM setup. metal porphyrins 38-54 sulfotransferase family 1A member 3 Homo sapiens 103-106 32526807-8 2020 Mean duration on milrinone was 13.7 vs. 81.0 days in STM and LTM, respectively. Milrinone 17-26 sulfotransferase family 1A member 3 Homo sapiens 53-56 32324372-5 2020 We then study the mechanism of CD fluorescence by directly imaging individual CDs with sub-particle resolution by STM. Cadmium 31-33 sulfotransferase family 1A member 3 Homo sapiens 114-117 32340450-0 2020 Self-assembly properties of solution processable, electroactive alkoxy and alkyl-thienylene derivatives of fused benzoacridines - an STM study. alkoxy and alkyl-thienylene 64-91 sulfotransferase family 1A member 3 Homo sapiens 133-136 32340450-0 2020 Self-assembly properties of solution processable, electroactive alkoxy and alkyl-thienylene derivatives of fused benzoacridines - an STM study. benzoacridines 113-127 sulfotransferase family 1A member 3 Homo sapiens 133-136 32096309-2 2020 Experiments performed by using ultrahigh-vacuum scanning tunneling microscopy (UHV-STM), with the substitution of metal-coordination centers, metallic substrates and functional organic ligands, corroborate the template effect of the Cu-N coordination. Metals 114-119 sulfotransferase family 1A member 3 Homo sapiens 83-86 32321241-3 2020 Herein, we design a molecule with cumulene moiety (Br2C=C=C=CBr2) and employ STM tip manipulation to achieve the molecular skeleton rearrangement from cumulene to diyne moiety (Br-C C-C C-Br). Polyenes 151-159 sulfotransferase family 1A member 3 Homo sapiens 77-80 32321241-3 2020 Herein, we design a molecule with cumulene moiety (Br2C=C=C=CBr2) and employ STM tip manipulation to achieve the molecular skeleton rearrangement from cumulene to diyne moiety (Br-C C-C C-Br). Diynes 163-168 sulfotransferase family 1A member 3 Homo sapiens 77-80 32152050-7 2020 This resulted in an increase in the toxicity of dopamine, a substrate for SULT1A3. Dopamine 48-56 sulfotransferase family 1A member 3 Homo sapiens 74-81 32152050-11 2020 In neuron-like cells, SULT4A1 is able to modulate dopamine toxicity by interacting with SULT1A3, potentially decreasing the metabolism of dopamine. Dopamine 50-58 sulfotransferase family 1A member 3 Homo sapiens 88-95 32152050-11 2020 In neuron-like cells, SULT4A1 is able to modulate dopamine toxicity by interacting with SULT1A3, potentially decreasing the metabolism of dopamine. Dopamine 138-146 sulfotransferase family 1A member 3 Homo sapiens 88-95 32022018-1 2020 The two-dimensional (2D) self-assembly behavior of an asymmetric thienophenanthrene derivative (M1) has been theoretically predicted and further probed via STM. thienophenanthrene 65-83 sulfotransferase family 1A member 3 Homo sapiens 156-159 31842001-4 2020 Scanning tunneling microscope/spectroscopy (STM/STS) revealed the presence of Fe atoms near sulfur atoms and asymmetric spectra. Iron 78-80 sulfotransferase family 1A member 3 Homo sapiens 44-47 31842001-4 2020 Scanning tunneling microscope/spectroscopy (STM/STS) revealed the presence of Fe atoms near sulfur atoms and asymmetric spectra. Sulfur 92-98 sulfotransferase family 1A member 3 Homo sapiens 44-47 32207467-1 2020 Combining STM measurements on three different substrates (HOPG, MoS2, and Au[111]) together with DFT calculations allow for analysis of the origin of the self-assembly of 4-cyano-4"-n-decylbiphenyl (10CB) molecules into kinked row structures using a previously developed phenomenological model. 4-cyano-4"-n-decylbiphenyl 171-197 sulfotransferase family 1A member 3 Homo sapiens 10-13 32150680-4 2020 With the help of ultrahigh-vacuum, low-temperature scanning tunneling microscopy (UHV-LT-STM) and scanning tunneling spectroscopy (STS), we were able to directly visualize both Ru(II) and Fe(II), which act as staining reagents on the repeat units, thus providing detailed structural information for the single polymer chain. ru(ii) 177-183 sulfotransferase family 1A member 3 Homo sapiens 89-92 31492243-2 2020 By immersing the alkanedithiol SAM/Au in a corresponding metalcontaining solution (HAuCl4, AgNO3, H2PtCl6 and PdSO4), Au, Ag, Pt and Pd clusters, respectively, could be formed on top of the SAM/Au(111) electrode surface, which was confirmed by STM characterization. alkanedithiol 17-30 sulfotransferase family 1A member 3 Homo sapiens 244-247 31880944-5 2020 At negative sample bias, the screened Coulomb interaction between STM tip and the charged vacancies creates disk-like protrusion around VPd and crater-like features around VSe. vpd 136-139 sulfotransferase family 1A member 3 Homo sapiens 66-69 31859319-3 2020 Herein, we investigated the self-assembled behaviors of two DTBDT derivatives, 4,8-bis(4-octadecylthiophen-2-yl)benzo[1,2-b:4,5-b"]dithiophene (H-DTBDT) and 4,8-bis(5-bromo-4-octadecylthiophen-2-yl)benzo[1,2-b:4,5-b"]dithiophene (Br-DTBDT), to elucidate the effect of introducing a bromine atom on molecular packing structures by STM at the 1-phenyloctane/HOPG interface. dtbdt 60-65 sulfotransferase family 1A member 3 Homo sapiens 330-333 31944105-4 2020 The Si-TPP complex presents a saddle-shaped conformation that is stable under STM manipulation. tetraphenylporphyrin 4-10 sulfotransferase family 1A member 3 Homo sapiens 78-81 31532066-5 2020 Herein, we present the long-range chirality recognition between neighboring 3-bromo-naphthalen-2-ol (BNOL) stripes on an inert Au(111) surface across the herringbone reconstruction as investigated by STM and DFT calculations. 3-bromo-naphthalen-2-ol 76-99 sulfotransferase family 1A member 3 Homo sapiens 200-203 31846337-4 2020 We demonstrate how a single non-magnetic neutral tetrabenzo[a,c,j,h]phenazine molecule can be on-surface coordinated with exactly two aluminum metal atoms (Al(III) oxidation state on the Au(111) surface) by low-temperature scanning tunneling microscope (LT-STM) single atom manipulation. tetrabenzo(8)circulene 49-59 sulfotransferase family 1A member 3 Homo sapiens 257-260 31846337-4 2020 We demonstrate how a single non-magnetic neutral tetrabenzo[a,c,j,h]phenazine molecule can be on-surface coordinated with exactly two aluminum metal atoms (Al(III) oxidation state on the Au(111) surface) by low-temperature scanning tunneling microscope (LT-STM) single atom manipulation. Phenazines 68-77 sulfotransferase family 1A member 3 Homo sapiens 257-260 31846337-4 2020 We demonstrate how a single non-magnetic neutral tetrabenzo[a,c,j,h]phenazine molecule can be on-surface coordinated with exactly two aluminum metal atoms (Al(III) oxidation state on the Au(111) surface) by low-temperature scanning tunneling microscope (LT-STM) single atom manipulation. Aluminum 134-142 sulfotransferase family 1A member 3 Homo sapiens 257-260 31846337-4 2020 We demonstrate how a single non-magnetic neutral tetrabenzo[a,c,j,h]phenazine molecule can be on-surface coordinated with exactly two aluminum metal atoms (Al(III) oxidation state on the Au(111) surface) by low-temperature scanning tunneling microscope (LT-STM) single atom manipulation. Aluminum 156-163 sulfotransferase family 1A member 3 Homo sapiens 257-260 31846337-4 2020 We demonstrate how a single non-magnetic neutral tetrabenzo[a,c,j,h]phenazine molecule can be on-surface coordinated with exactly two aluminum metal atoms (Al(III) oxidation state on the Au(111) surface) by low-temperature scanning tunneling microscope (LT-STM) single atom manipulation. Gold 187-194 sulfotransferase family 1A member 3 Homo sapiens 257-260 31560011-5 2019 Atomic-scale structural information from STM complement the Raman sensitivity to the single molecular bond to open the way to detailed understanding of these novel carbon nanostructures. Carbon 164-170 sulfotransferase family 1A member 3 Homo sapiens 41-44 31893221-6 2019 Based on this combination of electrochemical scanning tunneling microscopy (EC-STM) and CV data, we derive a detailed atomistic picture of the nanoisland evolution during potential cycling, delivering new insights into the initial stages of platinum electrode degradation. Platinum 241-249 sulfotransferase family 1A member 3 Homo sapiens 79-82 31693383-1 2019 We use electrochemical scanning tunneling microscopy (EC-STM) to image single-crystal surfaces of the layered bismuth chalcogenide Sn0.01Bi1.99Te2Se in situ under electrochemical control for the first time. Bismuth 110-130 sulfotransferase family 1A member 3 Homo sapiens 57-60 31693383-1 2019 We use electrochemical scanning tunneling microscopy (EC-STM) to image single-crystal surfaces of the layered bismuth chalcogenide Sn0.01Bi1.99Te2Se in situ under electrochemical control for the first time. Tin 131-133 sulfotransferase family 1A member 3 Homo sapiens 57-60 31693383-1 2019 We use electrochemical scanning tunneling microscopy (EC-STM) to image single-crystal surfaces of the layered bismuth chalcogenide Sn0.01Bi1.99Te2Se in situ under electrochemical control for the first time. Tellurium 141-148 sulfotransferase family 1A member 3 Homo sapiens 57-60 31693383-4 2019 Nanometer-resolution EC-STM images show that the pit depth is generally equal to the thickness of a complete chalcogenide quintuple layer. phenylalanyl-ureido-citrullinyl-valinyl-cycloarginal 109-121 sulfotransferase family 1A member 3 Homo sapiens 24-27 31742378-1 2019 The electrodeposition of AuBr4- and PtBr42- onto an adlayer of circobiphenyl-a structurally defined nanographene with low symmetry-on a Au(111) electrode was investigated via electrochemical scanning tunneling microscopy (EC-STM) to control and understand the formation of characteristic nanoclusters. Platinum 36-42 sulfotransferase family 1A member 3 Homo sapiens 225-228 31742378-1 2019 The electrodeposition of AuBr4- and PtBr42- onto an adlayer of circobiphenyl-a structurally defined nanographene with low symmetry-on a Au(111) electrode was investigated via electrochemical scanning tunneling microscopy (EC-STM) to control and understand the formation of characteristic nanoclusters. circumbiphenyl 63-76 sulfotransferase family 1A member 3 Homo sapiens 225-228 31742378-5 2019 EC-STM revealed the formation of characteristic dimers of Pt clusters ranging from 2-4 nm in diameter on the circobiphenyl adlayer. Platinum 58-60 sulfotransferase family 1A member 3 Homo sapiens 3-6 31742378-5 2019 EC-STM revealed the formation of characteristic dimers of Pt clusters ranging from 2-4 nm in diameter on the circobiphenyl adlayer. circumbiphenyl 109-122 sulfotransferase family 1A member 3 Homo sapiens 3-6 31652068-3 2019 Here, combining quasi-particle GW calculations, density functional theory (DFT) study on intrinsic defects, and scanning tunneling microscopy/spectroscopy (STM/STS) measurements, we conclude that stoichiometric TiS2 is a semiconductor with an indirect band gap of about 0.5 eV. Titanium 211-215 sulfotransferase family 1A member 3 Homo sapiens 156-159 31652068-5 2019 Our DFT results suggest that the dominant donor defect that is responsible for the self-doping under thermal equilibrium is Ti interstitial, which is corroborated by our STM/STS measurements. Titanium 124-126 sulfotransferase family 1A member 3 Homo sapiens 170-173 31872706-6 2019 According to the intrinsic clearance( CLint) value,the sulfonation rates of liquiritigenin-7-OH by expressed SULT enzymes followed the following rank order: SULT1 C4 > SULT1 A3 > SULT1 E1 > SULT1 A1 > SULT1 A2 > SULT1 B1 >SULT1 C2>SULT2 A1. liquiritigenin-7-oh 76-95 sulfotransferase family 1A member 3 Homo sapiens 168-176 31522492-6 2019 The mechanical switching is enabled by strong Au-C covalent bonding between the molecule and the electrodes, which allows the tensile force delivered by the STM piezo to break the molecule at its spiropyran C-O bond. Gold 46-48 sulfotransferase family 1A member 3 Homo sapiens 157-160 31522492-6 2019 The mechanical switching is enabled by strong Au-C covalent bonding between the molecule and the electrodes, which allows the tensile force delivered by the STM piezo to break the molecule at its spiropyran C-O bond. Carbon 49-50 sulfotransferase family 1A member 3 Homo sapiens 157-160 31536075-1 2019 Based on STM imaging and DFT calculations, we demonstrate that it is feasible to construct a series of metal-organic U + Cs structures composed of configuration-adjustable multiple-metal-center motifs, which is the consequence of the synergy and competition between hydrogen bonds and ionic bonds. Metals 103-108 sulfotransferase family 1A member 3 Homo sapiens 9-12 31536075-1 2019 Based on STM imaging and DFT calculations, we demonstrate that it is feasible to construct a series of metal-organic U + Cs structures composed of configuration-adjustable multiple-metal-center motifs, which is the consequence of the synergy and competition between hydrogen bonds and ionic bonds. Metals 181-186 sulfotransferase family 1A member 3 Homo sapiens 9-12 31872706-7 2019 Further,liquiritigenin-7-O-sulfonation was significantly correlated with the SULT1 A3 protein levels( P<0. liquiritigenin-7-o 8-26 sulfotransferase family 1A member 3 Homo sapiens 77-85 31872706-18 2019 Moreover,the sulfonation characters of liquiritigenin( 7-OH) in SULT1 A3 were strongly correlated with that in HEK-SULT1 A3 cells( P<0. liquiritigenin 39-53 sulfotransferase family 1A member 3 Homo sapiens 64-72 31872706-18 2019 Moreover,the sulfonation characters of liquiritigenin( 7-OH) in SULT1 A3 were strongly correlated with that in HEK-SULT1 A3 cells( P<0. 7-oh 55-59 sulfotransferase family 1A member 3 Homo sapiens 64-72 31872706-20 2019 In conclusion,liquiritigenin was subjected to efficient sulfonation,and SULT1 A3 enzyme plays an important role in the sulfonation of liquiritigenin-7-OH. liquiritigenin 14-28 sulfotransferase family 1A member 3 Homo sapiens 72-80 31872706-20 2019 In conclusion,liquiritigenin was subjected to efficient sulfonation,and SULT1 A3 enzyme plays an important role in the sulfonation of liquiritigenin-7-OH. liquiritigenin-7-oh 134-153 sulfotransferase family 1A member 3 Homo sapiens 72-80 31418761-0 2019 Chemistry of cysteine assembly on Au(100): electrochemistry, in situ STM and molecular modeling. Cysteine 13-21 sulfotransferase family 1A member 3 Homo sapiens 69-72 31418761-2 2019 We have studied the surface structure and adsorption dynamics of l-cysteine adlayers on Au(100) from aqueous solution using electrochemistry, high-resolution electrochemical scanning tunnelling microscopy (in situ STM), and molecular modelling. Cysteine 65-75 sulfotransferase family 1A member 3 Homo sapiens 214-217 31418761-7 2019 In situ STM showed that the adsorbed Cys is organized in stripes with "fork-like" features which co-exist in (11 x 2)-2Cys and (7 x 2)-2Cys lattices, quite differently from Cys adsorption on Au(111)-electrode surfaces. Cysteine 37-40 sulfotransferase family 1A member 3 Homo sapiens 8-11 31418761-8 2019 Stripe structures with bright STM contrast in the center suggest that a second Cys adlayer on top of a first adlayer is formed, supporting the dual-peak reductive desorption of Cys adlayers. Cysteine 79-82 sulfotransferase family 1A member 3 Homo sapiens 30-33 31418761-8 2019 Stripe structures with bright STM contrast in the center suggest that a second Cys adlayer on top of a first adlayer is formed, supporting the dual-peak reductive desorption of Cys adlayers. Cysteine 177-180 sulfotransferase family 1A member 3 Homo sapiens 30-33 31418761-10 2019 Virtually identical macroscopic electrochemical features were found, but in situ STM discloses many more defects for the racemic mixture than for the pure enantiomers due to structural mismatch of l- and d-Cys. l- and 197-203 sulfotransferase family 1A member 3 Homo sapiens 81-84 31418761-10 2019 Virtually identical macroscopic electrochemical features were found, but in situ STM discloses many more defects for the racemic mixture than for the pure enantiomers due to structural mismatch of l- and d-Cys. D-cysteine 204-209 sulfotransferase family 1A member 3 Homo sapiens 81-84 31251431-0 2019 Dechlorinated Ullmann Coupling Reaction of Aryl Chlorides on Ag(111): A Combined STM and XPS Study. aryl chlorides 43-57 sulfotransferase family 1A member 3 Homo sapiens 81-84 31153055-8 2019 In forward stepwise multiple regression, serum creatinine, TNFR2, and OPN were identified as significant, independent predictors of sTM. Creatinine 47-57 sulfotransferase family 1A member 3 Homo sapiens 132-135 31385576-1 2019 Molecular resolution STM is used to study the spatial structure and chirality of adsorbed Delta4,4-dicyclopenta[2,1-b:3,4-b]-dithiophene (TTE) on an Au(111) electrode, revealing an ordered, racemate adlayer made of homogeneously mixed R- and S-TTE on the (1 x 1) substrate and patches of R- or S-only TTE on the reconstructed Au(111) at more and less positive potentials. 3,4-b]-dithiophene 118-136 sulfotransferase family 1A member 3 Homo sapiens 21-24 31385576-1 2019 Molecular resolution STM is used to study the spatial structure and chirality of adsorbed Delta4,4-dicyclopenta[2,1-b:3,4-b]-dithiophene (TTE) on an Au(111) electrode, revealing an ordered, racemate adlayer made of homogeneously mixed R- and S-TTE on the (1 x 1) substrate and patches of R- or S-only TTE on the reconstructed Au(111) at more and less positive potentials. PHOSPHOMETHYL PHOSPHONIC ACID DEOXYTHYMIDYLATE ESTER 138-141 sulfotransferase family 1A member 3 Homo sapiens 21-24 31385576-1 2019 Molecular resolution STM is used to study the spatial structure and chirality of adsorbed Delta4,4-dicyclopenta[2,1-b:3,4-b]-dithiophene (TTE) on an Au(111) electrode, revealing an ordered, racemate adlayer made of homogeneously mixed R- and S-TTE on the (1 x 1) substrate and patches of R- or S-only TTE on the reconstructed Au(111) at more and less positive potentials. Gold 149-151 sulfotransferase family 1A member 3 Homo sapiens 21-24 31153055-7 2019 RESULTS: After adjustment for HD status, sTM showed a significant positive correlation with serum creatinine, TNFR2, OPN, HGF, SDF1alpha, sVEGFR2, Pi, iPTH, FGF-23, OPG, OC and ON. Creatinine 98-108 sulfotransferase family 1A member 3 Homo sapiens 41-44 31022709-2 2019 By fully incorporating a metallic tip on a silicon chip using modern micromachining and nanofabrication techniques, we realize so-called smart tips and show the possibility of device-based STM tips. Silicon 43-50 sulfotransferase family 1A member 3 Homo sapiens 189-192 31145702-0 2019 Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes. Phenylephrine 68-81 sulfotransferase family 1A member 3 Homo sapiens 10-17 31265312-1 2019 Various architectures have been generated and observed by STM at a solid/liquid interface resulting from an in situ chemical reaction between the bipyridine terminal groups of a ditopic ligand and Co(II) ions. 2,2'-Dipyridyl 146-156 sulfotransferase family 1A member 3 Homo sapiens 58-61 31026104-3 2019 Subsequently, these molecules were deposited onto Cu(111) and scanning-tunneling-microscopy(STM)-based atom manipulation was employed to dissociate the oxygen atoms. Oxygen 152-158 sulfotransferase family 1A member 3 Homo sapiens 92-95 31145702-0 2019 Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes. Phenylephrine 68-81 sulfotransferase family 1A member 3 Homo sapiens 106-113 31145702-3 2019 This study was carried out to investigate the effects of single nucleotide polymorphisms of human SULT1A3 and SULT1A4 genes on the sulfation of phenylephrine and salbutamol by SULT1A3 allozymes. Phenylephrine 144-157 sulfotransferase family 1A member 3 Homo sapiens 98-105 31145702-0 2019 Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes. Albuterol 86-96 sulfotransferase family 1A member 3 Homo sapiens 10-17 31145702-3 2019 This study was carried out to investigate the effects of single nucleotide polymorphisms of human SULT1A3 and SULT1A4 genes on the sulfation of phenylephrine and salbutamol by SULT1A3 allozymes. Phenylephrine 144-157 sulfotransferase family 1A member 3 Homo sapiens 176-183 31145702-3 2019 This study was carried out to investigate the effects of single nucleotide polymorphisms of human SULT1A3 and SULT1A4 genes on the sulfation of phenylephrine and salbutamol by SULT1A3 allozymes. Albuterol 162-172 sulfotransferase family 1A member 3 Homo sapiens 98-105 31145702-0 2019 Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes. Albuterol 86-96 sulfotransferase family 1A member 3 Homo sapiens 106-113 31145702-3 2019 This study was carried out to investigate the effects of single nucleotide polymorphisms of human SULT1A3 and SULT1A4 genes on the sulfation of phenylephrine and salbutamol by SULT1A3 allozymes. Albuterol 162-172 sulfotransferase family 1A member 3 Homo sapiens 176-183 31018027-0 2019 Carbohydrate Self-Assembly at Surfaces: STM Imaging of Sucrose Conformation and Ordering on Cu(100). Carbohydrates 0-12 sulfotransferase family 1A member 3 Homo sapiens 40-43 31145702-5 2019 RESULTS: Purified SULT1A3 allozymes, in comparison with the wild-type enzyme, showed differential sulfating activities toward phenylephrine and salbutamol. Phenylephrine 126-139 sulfotransferase family 1A member 3 Homo sapiens 18-25 31145702-5 2019 RESULTS: Purified SULT1A3 allozymes, in comparison with the wild-type enzyme, showed differential sulfating activities toward phenylephrine and salbutamol. Albuterol 144-154 sulfotransferase family 1A member 3 Homo sapiens 18-25 31145702-7 2019 CONCLUSION: The results obtained showed clearly the differential enzymatic characteristics of SULT1A3 allozymes in mediating the sulfation of phenylephrine and salbutamol. Phenylephrine 142-155 sulfotransferase family 1A member 3 Homo sapiens 94-101 31145702-7 2019 CONCLUSION: The results obtained showed clearly the differential enzymatic characteristics of SULT1A3 allozymes in mediating the sulfation of phenylephrine and salbutamol. Albuterol 160-170 sulfotransferase family 1A member 3 Homo sapiens 94-101 31197295-2 2019 The W 5dz2 orbital, the LUMO of the isolated cluster, plays a critical role in all aspects, forming a covalent bond between the metal and the silicon surface, and then providing an effective transmission channel that allows current to flow from the surface to STM tip. Metals 128-133 sulfotransferase family 1A member 3 Homo sapiens 260-263 31197295-2 2019 The W 5dz2 orbital, the LUMO of the isolated cluster, plays a critical role in all aspects, forming a covalent bond between the metal and the silicon surface, and then providing an effective transmission channel that allows current to flow from the surface to STM tip. Silicon 142-149 sulfotransferase family 1A member 3 Homo sapiens 260-263 31197295-3 2019 The STM images therefore provide a very direct probe of the W-Si surface bond. Silicon 62-64 sulfotransferase family 1A member 3 Homo sapiens 4-7 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. Tetrafluoroterephthalic acid 83-111 sulfotransferase family 1A member 3 Homo sapiens 50-53 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. Tetrafluoroterephthalic acid 83-111 sulfotransferase family 1A member 3 Homo sapiens 196-199 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. tftpa 113-118 sulfotransferase family 1A member 3 Homo sapiens 50-53 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. terephthalic acid 94-111 sulfotransferase family 1A member 3 Homo sapiens 50-53 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. terephthalic acid 94-111 sulfotransferase family 1A member 3 Homo sapiens 196-199 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. terephthalic acid 115-118 sulfotransferase family 1A member 3 Homo sapiens 50-53 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. Gold 170-172 sulfotransferase family 1A member 3 Homo sapiens 50-53 31244139-3 2019 The scanning tunneling microscopy break junction (STM-BJ) method is used to bridge tetrafluoroterephthalic acid (TFTPA) and terephthalic acid (TPA) molecules between the Au(111) electrode and the STM tip to measure the single-molecule conductance through the junction. Gold 170-172 sulfotransferase family 1A member 3 Homo sapiens 196-199 31275923-3 2019 Recent STM and AFM investigations as well as DFT-based calculations have indicated that in the near-surface of CeO2 (111), at low temperatures and vacancy concentrations, subsurface oxygen vacancies are more stable than surface ones, and the Ce3+ ions are next-nearest neighbors to both types of vacancies, which can be explained by the better ability of the system to relax the lattice strain induced by vacancy formation as well as by the excess charge localization. ceric oxide 111-115 sulfotransferase family 1A member 3 Homo sapiens 7-10 31018027-0 2019 Carbohydrate Self-Assembly at Surfaces: STM Imaging of Sucrose Conformation and Ordering on Cu(100). Sucrose 55-62 sulfotransferase family 1A member 3 Homo sapiens 40-43 31018027-0 2019 Carbohydrate Self-Assembly at Surfaces: STM Imaging of Sucrose Conformation and Ordering on Cu(100). Copper 92-94 sulfotransferase family 1A member 3 Homo sapiens 40-43 30994662-3 2019 Herein, we choose cytosine and NaCl as a model system and, from the interplay of STM imaging and DFT calculations, a hybrid network composed of both metal-organic and pure organic motifs interlinked by Cl ions via electrostatic interactions is observed on the Au(111) surface. Gold 260-262 sulfotransferase family 1A member 3 Homo sapiens 81-84 31121831-6 2019 The quantification of the fluorescent dye-tagged FA-AdP in STM was carried out by near-infrared fluorescence imaging. fa-adp 49-55 sulfotransferase family 1A member 3 Homo sapiens 59-62 30501782-1 2019 In this paper, single molecular junctions of Para-phthalic acid and Meta-phthalic acid with Au electrodes were studied by STM break junction approach. terephthalic acid 45-63 sulfotransferase family 1A member 3 Homo sapiens 122-125 30501782-1 2019 In this paper, single molecular junctions of Para-phthalic acid and Meta-phthalic acid with Au electrodes were studied by STM break junction approach. meta-phthalic acid 68-86 sulfotransferase family 1A member 3 Homo sapiens 122-125 30501782-1 2019 In this paper, single molecular junctions of Para-phthalic acid and Meta-phthalic acid with Au electrodes were studied by STM break junction approach. Gold 92-94 sulfotransferase family 1A member 3 Homo sapiens 122-125 30852903-0 2019 Bilayer Adsorption of Porphyrin Molecules Substituted with Carboxylic Acid atop the NN4A Network Revealed by STM and DFT. Porphyrins 22-31 sulfotransferase family 1A member 3 Homo sapiens 109-112 31106189-9 2019 Our results suggest that H2Pc prefers to be adsorbed on the surface Ti5c rows of anatase (101), in agreement with that seen in recent STM experiments on rutile (110). 2,11,20,29,37,38,39,40-Octazanonacyclo[28.6.1.13,10.112,19.121,28.04,9.013,18.022,27.031,36]tetraconta-1,3(40),4,6,8,10,12(39),13,15,17,19,21,23,25,27,30(37),31,33,35-nonadecaene 25-29 sulfotransferase family 1A member 3 Homo sapiens 134-137 30874258-0 2019 Hexagonal array formation by intermolecular halogen bonding using a binary blend of linear building blocks: STM study. Halogens 44-51 sulfotransferase family 1A member 3 Homo sapiens 108-111 30852903-0 2019 Bilayer Adsorption of Porphyrin Molecules Substituted with Carboxylic Acid atop the NN4A Network Revealed by STM and DFT. Carboxylic Acids 59-74 sulfotransferase family 1A member 3 Homo sapiens 109-112 30566916-1 2019 We report on the low-temperature scanning tunneling microscopy/spectroscopy (STM/STS) study of the (Bi, Na)/Si(1 1 1)[Formula: see text] reconstruction that is known to possess Fermi surface with apparently good nesting. Silicon 108-110 sulfotransferase family 1A member 3 Homo sapiens 77-80 30230050-0 2018 Corroles at the Real Solid-Liquid Interface: In Situ STM Investigation of a Water-Soluble Corrole Layer Deposited onto Au(111). Water 76-81 sulfotransferase family 1A member 3 Homo sapiens 53-56 30792428-0 2019 In-situ four-tip STM investigation of the transition from 2D to 3D charge transport in SrTiO3. strontium titanium oxide 87-93 sulfotransferase family 1A member 3 Homo sapiens 17-20 30516985-3 2019 We found that a single Fc unit readily interacts with the metal electrodes of an STM break junction (STM = scanning tunneling microscope) and that the zero-voltage bias conductance of an individual Fc molecular junction increased 5-fold, up to 80% of the conductance quantum G0 (77.4 muS), when the length of the molecular wire was increased from one to three connected Fc units. Metals 58-63 sulfotransferase family 1A member 3 Homo sapiens 81-84 30516985-3 2019 We found that a single Fc unit readily interacts with the metal electrodes of an STM break junction (STM = scanning tunneling microscope) and that the zero-voltage bias conductance of an individual Fc molecular junction increased 5-fold, up to 80% of the conductance quantum G0 (77.4 muS), when the length of the molecular wire was increased from one to three connected Fc units. Metals 58-63 sulfotransferase family 1A member 3 Homo sapiens 101-104 30873321-5 2019 Detailed analysis of the STM images emphasizes the crucial role of weak intermolecular hydrogen bonding, and molecule-substrate interactions in the formation of the observed polymorphs. Hydrogen 87-95 sulfotransferase family 1A member 3 Homo sapiens 25-28 30558427-7 2019 Using the H2 molecule as a chopper for STM-induced optical emission intensity, we demonstrate bunching in the plasmonic photon train in a single measurement over 6 orders of magnitude in the time domain (from microseconds to seconds) that takes only a few seconds. Hydrogen 10-12 sulfotransferase family 1A member 3 Homo sapiens 39-42 30398169-2 2018 Flakes originating from a single crystal of graphite, whose orientation is confirmed using STM, are studied using facet orientations and electron back-scatter diffraction (EBSD). Graphite 44-52 sulfotransferase family 1A member 3 Homo sapiens 91-94 30230050-0 2018 Corroles at the Real Solid-Liquid Interface: In Situ STM Investigation of a Water-Soluble Corrole Layer Deposited onto Au(111). corrole 0-7 sulfotransferase family 1A member 3 Homo sapiens 53-56 30230050-7 2018 The layer formation of P corroles onto the Au(111) surface was monitored by STM in situ, that is, with the substrate immersed in the solution. Gold 43-45 sulfotransferase family 1A member 3 Homo sapiens 76-79 30176366-0 2018 Sulfation disposition of liquiritigenin in SULT1A3 overexpressing HEK293 cells: The role of breast cancer resistance protein (BCRP) and multidrug resistance-associated protein 4 (MRP4) in sulfate efflux of liquiritigenin. liquiritigenin 25-39 sulfotransferase family 1A member 3 Homo sapiens 43-50 30365166-1 2018 We use clusters for the modeling of local ion resonances caused by low energy charge carriers in STM-induced desorption of benzene derivates from Si(111)-7 x 7. Benzene 123-130 sulfotransferase family 1A member 3 Homo sapiens 97-100 30365166-1 2018 We use clusters for the modeling of local ion resonances caused by low energy charge carriers in STM-induced desorption of benzene derivates from Si(111)-7 x 7. Silicon 146-148 sulfotransferase family 1A member 3 Homo sapiens 97-100 30176366-2 2018 The sulfonation disposition of liquiritigenin was investigated using SULT1A3 overexpressed HEK293 cells (HEK-SULT1A3 cells). liquiritigenin 31-45 sulfotransferase family 1A member 3 Homo sapiens 69-76 30176366-2 2018 The sulfonation disposition of liquiritigenin was investigated using SULT1A3 overexpressed HEK293 cells (HEK-SULT1A3 cells). liquiritigenin 31-45 sulfotransferase family 1A member 3 Homo sapiens 109-116 30176366-3 2018 Liquiritigenin generated one mono-sulfate metabolite (7-O-sulfate) in HEK-SULT1A3 cell lysate. liquiritigenin 0-14 sulfotransferase family 1A member 3 Homo sapiens 74-81 30176366-3 2018 Liquiritigenin generated one mono-sulfate metabolite (7-O-sulfate) in HEK-SULT1A3 cell lysate. mono-sulfate 29-41 sulfotransferase family 1A member 3 Homo sapiens 74-81 30176366-3 2018 Liquiritigenin generated one mono-sulfate metabolite (7-O-sulfate) in HEK-SULT1A3 cell lysate. 7-o-sulfate 54-65 sulfotransferase family 1A member 3 Homo sapiens 74-81 30176366-6 2018 Furthermore, 7-O-sulfate was rapidly generated and excreted in HEK-SULT1A3 cells. 7-o-sulfate 13-24 sulfotransferase family 1A member 3 Homo sapiens 67-74 30176366-11 2018 In conclusion, one sulfate metabolite was generated from liquiritigenin in HEK-SULT1A3 cells. Sulfates 19-26 sulfotransferase family 1A member 3 Homo sapiens 79-86 30176366-11 2018 In conclusion, one sulfate metabolite was generated from liquiritigenin in HEK-SULT1A3 cells. liquiritigenin 57-71 sulfotransferase family 1A member 3 Homo sapiens 79-86 30069558-0 2018 Chemistry of 4-[(4-bromophenyl)ethynyl]pyridine at metal surfaces studied by STM. 4-[(4-bromophenyl)ethynyl]pyridine 13-47 sulfotransferase family 1A member 3 Homo sapiens 77-80 30226744-3 2018 Herein, by combining scanning tunneling microscopy and spectroscopy (STM and STS) with first-principles calculations, we accomplish the on-site atomic-scale identification of the top four non-identical Se atoms in a unit cell of the anisotropic monolayer ReSe2 on the Au substrate. Selenium 202-204 sulfotransferase family 1A member 3 Homo sapiens 69-72 29978881-3 2018 In a previous proof-of-concept paper, we used simple alpha,omega-dithiol self-assembled monolayers on a gallium arsenide (GaAs) substrate to fabricate molecular Schottky diodes with a STM. alpha,omega-dithiol 53-72 sulfotransferase family 1A member 3 Homo sapiens 184-187 29978881-3 2018 In a previous proof-of-concept paper, we used simple alpha,omega-dithiol self-assembled monolayers on a gallium arsenide (GaAs) substrate to fabricate molecular Schottky diodes with a STM. gallium arsenide 104-120 sulfotransferase family 1A member 3 Homo sapiens 184-187 29978881-3 2018 In a previous proof-of-concept paper, we used simple alpha,omega-dithiol self-assembled monolayers on a gallium arsenide (GaAs) substrate to fabricate molecular Schottky diodes with a STM. gallium arsenide 122-126 sulfotransferase family 1A member 3 Homo sapiens 184-187 30013053-4 2018 Here we investigate borophene line defects at the atomic scale with ultrahigh vacuum (UHV) scanning tunnelling microscopy/spectroscopy (STM/STS) and density functional theory (DFT). borophene 20-29 sulfotransferase family 1A member 3 Homo sapiens 136-139 30188726-5 2018 It consists of alpha-helix and beta-strand conformations of an oligo-glycine peptide, which is bonded to a nickel electrode and to a gold electrode in a two-terminal setup, similar to a molecular junction or a local probe, for example, in STM or AFM configurations. oligo-glycine 63-76 sulfotransferase family 1A member 3 Homo sapiens 239-242 30204776-8 2018 STm mutants lacking the type-3 secretion system-1 induce less neutrophil ROS than the virulent WT. Reactive Oxygen Species 73-76 sulfotransferase family 1A member 3 Homo sapiens 0-3 30137083-1 2018 Surface-confined host-guest chemistry at the air/solid interface is used for trapping a functionalized 3D Zn-phthalocyanine complex into a 2D porous supramolecular template allowing the large area functionalization of an sp2-hybridized carbon-based substrate as evidenced by STM, resonance Raman spectroscopy, and water contact angle measurements. Zn(II)-phthalocyanine 106-123 sulfotransferase family 1A member 3 Homo sapiens 275-278 30137083-1 2018 Surface-confined host-guest chemistry at the air/solid interface is used for trapping a functionalized 3D Zn-phthalocyanine complex into a 2D porous supramolecular template allowing the large area functionalization of an sp2-hybridized carbon-based substrate as evidenced by STM, resonance Raman spectroscopy, and water contact angle measurements. Carbon 236-242 sulfotransferase family 1A member 3 Homo sapiens 275-278 29705271-0 2018 Effects of human SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of acetaminophen and opioid drugs by the cytosolic sulfotransferase SULT1A3. Acetaminophen 75-88 sulfotransferase family 1A member 3 Homo sapiens 17-24 29915084-3 2018 In this work, we implement a simple method for straining materials compatible with low-temperature scanning tunneling microscopy/spectroscopy (STM/S), and use it to strain-engineer CDWs in 2H-NbSe2 Our STM/S measurements, combined with theory, reveal how small strain-induced changes in the electronic band structure and phonon dispersion lead to dramatic changes in the CDW ordering wavevector and geometry. Deuterium 189-191 sulfotransferase family 1A member 3 Homo sapiens 143-146 30062353-2 2018 The formation of this network has been investigated by STM and has been elucidated in the light of sergeants & soldiers principle due to halogen bonding on a silicon surface. Halogens 141-148 sulfotransferase family 1A member 3 Homo sapiens 55-58 30062353-2 2018 The formation of this network has been investigated by STM and has been elucidated in the light of sergeants & soldiers principle due to halogen bonding on a silicon surface. Silicon 162-169 sulfotransferase family 1A member 3 Homo sapiens 55-58 29915084-3 2018 In this work, we implement a simple method for straining materials compatible with low-temperature scanning tunneling microscopy/spectroscopy (STM/S), and use it to strain-engineer CDWs in 2H-NbSe2 Our STM/S measurements, combined with theory, reveal how small strain-induced changes in the electronic band structure and phonon dispersion lead to dramatic changes in the CDW ordering wavevector and geometry. Deuterium 189-191 sulfotransferase family 1A member 3 Homo sapiens 202-205 30004771-3 2018 We show that nematicity only weakly affects T_{c}, but gives rise to cos2theta variation of the pairing gap on the hole pocket, whose magnitude and size agrees with angle resolved photoemission spectroscopy and STM data. cos2theta 69-78 sulfotransferase family 1A member 3 Homo sapiens 211-214 29705271-0 2018 Effects of human SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of acetaminophen and opioid drugs by the cytosolic sulfotransferase SULT1A3. Acetaminophen 75-88 sulfotransferase family 1A member 3 Homo sapiens 140-147 28374858-2 2018 SULT1A3/4 are important enzymes in the metabolism of catecholamines linked to neurodegenerative diseases such as Parkinson"s and Alzheimer"s. Catecholamines 53-67 sulfotransferase family 1A member 3 Homo sapiens 0-9 29796455-5 2018 Simulated STM images suggested the change in electron density that would occur upon adsorption of hydroxylamine in various adsorption configurations, and specifically indicated the N-O dissociative product to have greater electron density around the amine groups, and the hydroxyl groups to mainly contribute electron density to the unoccupied electronic states. Hydroxylamine 98-111 sulfotransferase family 1A member 3 Homo sapiens 10-13 29796455-5 2018 Simulated STM images suggested the change in electron density that would occur upon adsorption of hydroxylamine in various adsorption configurations, and specifically indicated the N-O dissociative product to have greater electron density around the amine groups, and the hydroxyl groups to mainly contribute electron density to the unoccupied electronic states. Nitrogen 181-182 sulfotransferase family 1A member 3 Homo sapiens 10-13 29796455-5 2018 Simulated STM images suggested the change in electron density that would occur upon adsorption of hydroxylamine in various adsorption configurations, and specifically indicated the N-O dissociative product to have greater electron density around the amine groups, and the hydroxyl groups to mainly contribute electron density to the unoccupied electronic states. Amines 106-111 sulfotransferase family 1A member 3 Homo sapiens 10-13 29761181-1 2018 Cyclic conjugated monomers comprising cyclopentadithiophene-vinylene trimers and their polymers on HOPG are observed using STM and AFM. cyclopentadithiophene-vinylene trimers 38-76 sulfotransferase family 1A member 3 Homo sapiens 123-126 29761181-3 2018 Their STM images exhibit single chains of planar polymers, whereas their AFM images show elongation of the polymer chains on HOPG. Polymers 49-57 sulfotransferase family 1A member 3 Homo sapiens 6-9 29761181-3 2018 Their STM images exhibit single chains of planar polymers, whereas their AFM images show elongation of the polymer chains on HOPG. Polymers 49-56 sulfotransferase family 1A member 3 Homo sapiens 6-9 29524394-2 2018 The current study aimed to clarify the effects of single nucleotide polymorphisms (SNPs) of human SULT1A3 and SULT1A4 genes on the enzymatic characteristics of the sulfation of dopamine, epinephrine, norepinephrine and serotonin by SULT1A3 allozymes. Serotonin 219-228 sulfotransferase family 1A member 3 Homo sapiens 98-105 29524394-6 2018 Purified SULT1A3 allozymes exhibited differential sulfating activity toward catecholamines and serotonin. Catecholamines 76-90 sulfotransferase family 1A member 3 Homo sapiens 9-16 29524394-6 2018 Purified SULT1A3 allozymes exhibited differential sulfating activity toward catecholamines and serotonin. Serotonin 95-104 sulfotransferase family 1A member 3 Homo sapiens 9-16 29524394-8 2018 Collectively, these findings provide useful information relevant to the differential metabolism of dopamine, epinephrine, norepinephrine and serotonin through sulfoconjugation in individuals having different SULT1A3/SULT1A4 genotypes. Dopamine 99-107 sulfotransferase family 1A member 3 Homo sapiens 208-215 29524394-8 2018 Collectively, these findings provide useful information relevant to the differential metabolism of dopamine, epinephrine, norepinephrine and serotonin through sulfoconjugation in individuals having different SULT1A3/SULT1A4 genotypes. Norepinephrine 122-136 sulfotransferase family 1A member 3 Homo sapiens 208-215 29524394-8 2018 Collectively, these findings provide useful information relevant to the differential metabolism of dopamine, epinephrine, norepinephrine and serotonin through sulfoconjugation in individuals having different SULT1A3/SULT1A4 genotypes. Serotonin 141-150 sulfotransferase family 1A member 3 Homo sapiens 208-215 29603557-3 2018 Quantitative in situ video-STM data on the surface diffusion of adsorbed sulfur atoms on Cu(100) electrodes in aqueous solution covered by bromide and chloride spectators, respectively, reveal in both cases a strong exponential potential dependence, but with opposite sign. Sulfur 73-79 sulfotransferase family 1A member 3 Homo sapiens 27-30 29603557-3 2018 Quantitative in situ video-STM data on the surface diffusion of adsorbed sulfur atoms on Cu(100) electrodes in aqueous solution covered by bromide and chloride spectators, respectively, reveal in both cases a strong exponential potential dependence, but with opposite sign. Copper 89-91 sulfotransferase family 1A member 3 Homo sapiens 27-30 29451137-0 2018 Self-assembled PCBM bilayers on graphene and HOPG examined by AFM and STM. PCBM 15-19 sulfotransferase family 1A member 3 Homo sapiens 70-73 29524394-0 2018 Sulfation of catecholamines and serotonin by SULT1A3 allozymes. Catecholamines 13-27 sulfotransferase family 1A member 3 Homo sapiens 45-52 29524394-0 2018 Sulfation of catecholamines and serotonin by SULT1A3 allozymes. Serotonin 32-41 sulfotransferase family 1A member 3 Homo sapiens 45-52 29524394-2 2018 The current study aimed to clarify the effects of single nucleotide polymorphisms (SNPs) of human SULT1A3 and SULT1A4 genes on the enzymatic characteristics of the sulfation of dopamine, epinephrine, norepinephrine and serotonin by SULT1A3 allozymes. Dopamine 177-185 sulfotransferase family 1A member 3 Homo sapiens 98-105 29524394-2 2018 The current study aimed to clarify the effects of single nucleotide polymorphisms (SNPs) of human SULT1A3 and SULT1A4 genes on the enzymatic characteristics of the sulfation of dopamine, epinephrine, norepinephrine and serotonin by SULT1A3 allozymes. Epinephrine 187-198 sulfotransferase family 1A member 3 Homo sapiens 98-105 29524394-2 2018 The current study aimed to clarify the effects of single nucleotide polymorphisms (SNPs) of human SULT1A3 and SULT1A4 genes on the enzymatic characteristics of the sulfation of dopamine, epinephrine, norepinephrine and serotonin by SULT1A3 allozymes. Norepinephrine 200-214 sulfotransferase family 1A member 3 Homo sapiens 98-105 29780493-3 2018 A tapelike hydrogen-bonded supramolecular array of barbiturated oligo(butylthiophene) molecules was directly visualized by STM at a liquid-solid interface. Hydrogen 11-19 sulfotransferase family 1A member 3 Homo sapiens 123-126 29474072-5 2018 The atomically precise structures and electronic properties of the obtained indenofluorene polymers have been unambiguously characterized by STM, nc-AFM, and STS, supported by theoretical calculations. indenofluorene polymers 76-99 sulfotransferase family 1A member 3 Homo sapiens 141-144 29780493-3 2018 A tapelike hydrogen-bonded supramolecular array of barbiturated oligo(butylthiophene) molecules was directly visualized by STM at a liquid-solid interface. oligo(butylthiophene) 64-85 sulfotransferase family 1A member 3 Homo sapiens 123-126 28631926-4 2018 Both STM images simulation and resulting energy alignment point to a tilted geometry for PTCDA on TiO2(110). 3,4,9,10-perylenetetracarboxylic dianhydride 89-94 sulfotransferase family 1A member 3 Homo sapiens 5-8 29365270-3 2018 We present results of a scanning tunneling microscopy/scanning tunneling spectroscopy (STM/STS) study of individual intragap states observed on the surfaces of hydrogen-passivated SiNCs deposited on the Au(111) surface. Hydrogen 160-168 sulfotransferase family 1A member 3 Homo sapiens 87-90 29396443-3 2018 As an example, we calculate the STM-induced spontaneous emission of a tetraphenylporphyrin (TPP) molecule coupled to a nanocavity plasmon. tetraphenylporphyrin 70-90 sulfotransferase family 1A member 3 Homo sapiens 32-35 29396443-3 2018 As an example, we calculate the STM-induced spontaneous emission of a tetraphenylporphyrin (TPP) molecule coupled to a nanocavity plasmon. tetraphenylporphyrin 92-95 sulfotransferase family 1A member 3 Homo sapiens 32-35 29303194-1 2018 We report on the scanning tunneling microscopy/spectroscopy (STM/STS) study of cobalt phthalocyanine (CoPc) molecules deposited onto a back-gated graphene device. cobalt phthalocyanine 79-100 sulfotransferase family 1A member 3 Homo sapiens 61-64 29322945-2 2018 The topographic STM images reveal that the self-assembled unidirectional and parallel NiSi NWs grow into the Si(110) substrate along the [Formula: see text] direction (i.e. the endotaxial growth) and exhibit multiple-layer growth. Silicon 88-90 sulfotransferase family 1A member 3 Homo sapiens 16-19 29077240-13 2018 For NCD, LT-STM had more CFs than LT-LT (p = 0.001) and lower PSs (p = 0.001). pss 62-65 sulfotransferase family 1A member 3 Homo sapiens 12-15 29308502-1 2018 Based on high-resolution STM imaging/manipulations and DFT calculations, we display the dynamic hydration process of adenine networks on Au(111) in real space, which results in controllable scission and stitching of adenine structures by water molecules. Adenine 117-124 sulfotransferase family 1A member 3 Homo sapiens 25-28 29308502-1 2018 Based on high-resolution STM imaging/manipulations and DFT calculations, we display the dynamic hydration process of adenine networks on Au(111) in real space, which results in controllable scission and stitching of adenine structures by water molecules. Adenine 216-223 sulfotransferase family 1A member 3 Homo sapiens 25-28 29308502-1 2018 Based on high-resolution STM imaging/manipulations and DFT calculations, we display the dynamic hydration process of adenine networks on Au(111) in real space, which results in controllable scission and stitching of adenine structures by water molecules. Water 238-243 sulfotransferase family 1A member 3 Homo sapiens 25-28 29303194-1 2018 We report on the scanning tunneling microscopy/spectroscopy (STM/STS) study of cobalt phthalocyanine (CoPc) molecules deposited onto a back-gated graphene device. cobalt phthalocyanine 102-106 sulfotransferase family 1A member 3 Homo sapiens 61-64 29303194-1 2018 We report on the scanning tunneling microscopy/spectroscopy (STM/STS) study of cobalt phthalocyanine (CoPc) molecules deposited onto a back-gated graphene device. Graphite 146-154 sulfotransferase family 1A member 3 Homo sapiens 61-64 28631926-4 2018 Both STM images simulation and resulting energy alignment point to a tilted geometry for PTCDA on TiO2(110). titanium dioxide 98-102 sulfotransferase family 1A member 3 Homo sapiens 5-8 29237391-6 2018 Salbutamol, a SULT1A3 substrate, showed little turnover in both enterocytes and hepatocytes, and more abundant sulfate conjugate was detected in enterocytes, indicating higher SULT activity in enterocytes than hepatocytes. Albuterol 0-10 sulfotransferase family 1A member 3 Homo sapiens 14-21 29232951-5 2018 Submolecular resolution STM is used to characterize this exotic large polycyclic aromatic compound on Au(111) yielding unprecedented insight into a dehydrogenative intramolecular aryl-aryl coupling reaction. Gold 102-104 sulfotransferase family 1A member 3 Homo sapiens 24-27 28891784-3 2018 In contrast, the number of remembered Pokemon stimuli, as indexed by Cowan"s K and late-window (1500-2000 msec) CDA amplitude, was significantly associated with individual differences in Pokemon familiarity when STM consolidation was incomplete because of a short presentation of Pokemon stimuli (500 msec, Experiment 2), but not when STM consolidation was allowed to complete given sufficient encoding time (1000 msec, Experiment 1). cda 112-115 sulfotransferase family 1A member 3 Homo sapiens 212-215 28946481-6 2018 Additionally, STM-electroluminescence (STMEL) is detected in C3N4 nanoflakes deposited on a gold substrate. c3n4 61-65 sulfotransferase family 1A member 3 Homo sapiens 14-17 29025375-0 2017 Dopamine-induced SULT1A3/4 promotes EMT and cancer stemness in hepatocellular carcinoma. Dopamine 0-8 sulfotransferase family 1A member 3 Homo sapiens 17-24 28967927-2 2017 The 2D nanostructures and chirality could be altered by the introduction of bromine atoms for both single component and binary surface assembly supported by STM and simulation results. Bromine 76-83 sulfotransferase family 1A member 3 Homo sapiens 157-160 29143027-3 2017 Here, we report on the formation of a covalent C-C bonding motif, namely 1,3-cyclobutadiene, via surface-confined [2 + 2] cycloaddition between pyrene moieties using low temperature scanning tunneling microscopy (LT-STM) and X-ray photoemission spectroscopy (XPS) measurements. Cyclobutadiene 73-91 sulfotransferase family 1A member 3 Homo sapiens 216-219 29143027-3 2017 Here, we report on the formation of a covalent C-C bonding motif, namely 1,3-cyclobutadiene, via surface-confined [2 + 2] cycloaddition between pyrene moieties using low temperature scanning tunneling microscopy (LT-STM) and X-ray photoemission spectroscopy (XPS) measurements. pyrene 144-150 sulfotransferase family 1A member 3 Homo sapiens 216-219 29038603-2 2017 From SP-STM images using Fe-coated W tips magnetized to the out-of-plane and [001] directions, we found that both Mn mono- and double-layers exhibit cycloidal rotation whose spins rotate in the planes normal to the propagating directions. TFF2 protein, human 5-7 sulfotransferase family 1A member 3 Homo sapiens 8-11 29038603-2 2017 From SP-STM images using Fe-coated W tips magnetized to the out-of-plane and [001] directions, we found that both Mn mono- and double-layers exhibit cycloidal rotation whose spins rotate in the planes normal to the propagating directions. Iron 25-27 sulfotransferase family 1A member 3 Homo sapiens 8-11 28070880-5 2017 RESULTS: Three of the thirteen human SULTs, SULT1A1, SULT1A3, and SULT1C4, were found to display sulfating activity toward tapentadol. Tapentadol 123-133 sulfotransferase family 1A member 3 Homo sapiens 53-60 28070880-6 2017 Kinetic analysis revealed that SULT1A3 displayed the highest catalytic efficiency in mediating the sulfation of tapentadol, followed by SULT1A1 and SULT1C4. Tapentadol 112-122 sulfotransferase family 1A member 3 Homo sapiens 31-38 29035514-3 2017 Combining STM, STS, and DFT studies, we report that the strong electronic interaction between transition metals and oxides could indeed govern the growth of low-dimensional oxide nanostructures. Oxides 116-122 sulfotransferase family 1A member 3 Homo sapiens 10-13 29035514-3 2017 Combining STM, STS, and DFT studies, we report that the strong electronic interaction between transition metals and oxides could indeed govern the growth of low-dimensional oxide nanostructures. Oxides 116-121 sulfotransferase family 1A member 3 Homo sapiens 10-13 28862430-1 2017 The molecular conformation of a bisbinaphthyldurene (BBD) molecule is manipulated using a low-temperature ultrahigh-vacuum scanning tunneling microscope (LT-UHV STM) on an Au(111) surface. bisbinaphthyldurene 32-51 sulfotransferase family 1A member 3 Homo sapiens 161-164 28862430-1 2017 The molecular conformation of a bisbinaphthyldurene (BBD) molecule is manipulated using a low-temperature ultrahigh-vacuum scanning tunneling microscope (LT-UHV STM) on an Au(111) surface. 5-tert-butyl-1,3-benzodioxole 53-56 sulfotransferase family 1A member 3 Homo sapiens 161-164 28786216-3 2017 Their hydrogen-bonded 2D on-surface self-assemblies are observed under STM at the solid/liquid interface; these structures are very different to those in the bulk crystal. Hydrogen 6-14 sulfotransferase family 1A member 3 Homo sapiens 71-74 28786216-4 2017 Upon combining the results of STM measurements and DFT calculations, the formation mechanism of different assemblies is revealed; in particular, the critical role of hydrogen bonding in the assemblies. Hydrogen 166-174 sulfotransferase family 1A member 3 Homo sapiens 30-33 28678020-7 2017 Simulated STM topographical images of stanene and group-V monolayers show distinctly different features in terms of their cross-sectional views and distance-height profiles. stanene 38-45 sulfotransferase family 1A member 3 Homo sapiens 10-13 28802998-6 2017 RESULTS: Of the thirteen human SULTs tested, only SULT1A3 and SULT1C4 were found to display O-DMT-sulfating activity, with different pH-dependency profiles. O-demethyltramadol 92-97 sulfotransferase family 1A member 3 Homo sapiens 50-57 28802998-10 2017 CONCLUSION: SULT1A3 and SULT1C4 were the major SULTs responsible for the sulfation of O-DMT. O-demethyltramadol 86-91 sulfotransferase family 1A member 3 Homo sapiens 12-19 29025375-2 2017 Hepatocellular carcinoma development is complex because of the metabolism disequilibrium involving SULT1A3/4, a predominant sulfotransferase that metabolizes sulfonic xenobiotics and endogenous catecholamines. Catecholamines 194-208 sulfotransferase family 1A member 3 Homo sapiens 99-106 29025375-6 2017 Ultra-high-pressure liquid chromatography-tandem mass spectrometry assay results further revealed that the concentration of dopamine (a substrate of SULT1A3/4) was negatively correlated with SULT1A3/4 protein expression. Dopamine 124-132 sulfotransferase family 1A member 3 Homo sapiens 149-156 29025375-6 2017 Ultra-high-pressure liquid chromatography-tandem mass spectrometry assay results further revealed that the concentration of dopamine (a substrate of SULT1A3/4) was negatively correlated with SULT1A3/4 protein expression. Dopamine 124-132 sulfotransferase family 1A member 3 Homo sapiens 191-198 29025375-7 2017 As a transcriptional regulator of SULT1A3/4 in turn, dopamine was used to induce SULT1A3/4 in vitro. Dopamine 53-61 sulfotransferase family 1A member 3 Homo sapiens 34-41 29025375-7 2017 As a transcriptional regulator of SULT1A3/4 in turn, dopamine was used to induce SULT1A3/4 in vitro. Dopamine 53-61 sulfotransferase family 1A member 3 Homo sapiens 81-88 29025375-8 2017 Interestingly, dopamine significantly induced SULT1A3/4 expression in liver cancer HepG2 cells, while decreased that in L02 cells. Dopamine 15-23 sulfotransferase family 1A member 3 Homo sapiens 46-53 29025375-10 2017 Furthermore, invasion and migration assays further revealed that dopamine-induced SULT1A3/4 dramatically stimulated the metastatic capacity of HepG2 cells. Dopamine 65-73 sulfotransferase family 1A member 3 Homo sapiens 82-89 28627535-5 2017 In simulated STM images, the three types of row-bridged adsorption structure have characteristic features, and the row-bridged dative-bonded configuration gives rise to features due to both adsorbed ethylenediamine molecules and the underlying Ge atoms. ethylenediamine 199-214 sulfotransferase family 1A member 3 Homo sapiens 13-16 28730208-1 2017 From the combination of STM imaging and DFT calculations, we show that both alkali metal and halogens interact with different sites of the target molecules resulting in structural formation in a synergistic way. Metals 83-88 sulfotransferase family 1A member 3 Homo sapiens 24-27 28696438-2 2017 By scanning tunneling microscopy imaging, we observed two different STM appearances of the melem molecule within the self-assembled nanostructure on Au(111), which resulted from the different intermolecular bonding configurations. Gold 149-151 sulfotransferase family 1A member 3 Homo sapiens 68-71 31457826-0 2017 Selective Adsorption of Coronene atop the Polycyclic Aromatic Diimide Monolayer Investigated by STM and DFT. coronene 24-32 sulfotransferase family 1A member 3 Homo sapiens 96-99 28871095-5 2017 The new RuO4-(2 x 1) reconstruction is stable in a wide range of environmental conditions, its simulated STM image perfectly matches experimental data, it is more thermodynamically stable than previously proposed reconstructions, and explains well pseudocapacitance of RuO2 cathodes. ruthenium tetraoxide 8-12 sulfotransferase family 1A member 3 Homo sapiens 105-108 28871095-5 2017 The new RuO4-(2 x 1) reconstruction is stable in a wide range of environmental conditions, its simulated STM image perfectly matches experimental data, it is more thermodynamically stable than previously proposed reconstructions, and explains well pseudocapacitance of RuO2 cathodes. ruo2 cathodes 269-282 sulfotransferase family 1A member 3 Homo sapiens 105-108 28853021-0 2017 First-Principles Study on the Stability and STM Image of Borophene. borophene 57-66 sulfotransferase family 1A member 3 Homo sapiens 44-47 28853021-7 2017 Additionally, our simulated STM images of these monoatomic-thin boron sheets on Ag(111) surface reproduce the experiment observations well and clearly identify the as-grown boron sheets. Boron 64-69 sulfotransferase family 1A member 3 Homo sapiens 28-31 28853021-7 2017 Additionally, our simulated STM images of these monoatomic-thin boron sheets on Ag(111) surface reproduce the experiment observations well and clearly identify the as-grown boron sheets. Boron 173-178 sulfotransferase family 1A member 3 Homo sapiens 28-31 28630292-5 2017 Here, the catechin-binding site of SULT1A3, which sulfonates monoamine neurotransmitters, is modeled on that of 1A1 and used to screen in silico for endogenous metabolite 1A3 allosteres. Catechin 10-18 sulfotransferase family 1A member 3 Homo sapiens 35-42 28630292-5 2017 Here, the catechin-binding site of SULT1A3, which sulfonates monoamine neurotransmitters, is modeled on that of 1A1 and used to screen in silico for endogenous metabolite 1A3 allosteres. Alkanesulfonates 50-60 sulfotransferase family 1A member 3 Homo sapiens 35-42 28630292-5 2017 Here, the catechin-binding site of SULT1A3, which sulfonates monoamine neurotransmitters, is modeled on that of 1A1 and used to screen in silico for endogenous metabolite 1A3 allosteres. monoamine 61-70 sulfotransferase family 1A member 3 Homo sapiens 35-42 28630292-7 2017 THB is shown to bind and inhibit SULT1A3 with high affinity, 23 (+-2) nM, and to bind weakly, if at all, to the four other major SULTs found in brain and liver. sapropterin 0-3 sulfotransferase family 1A member 3 Homo sapiens 33-40 28630292-9 2017 A structural comparison of SULT1A3 with SULT1A1 (its immediate evolutionary progenitor) reveals how SULT1A3 acquired high affinity for THB and that the majority of residue changes needed to transform 1A1 into 1A3 are clustered at the allosteric and active sites. sapropterin 135-138 sulfotransferase family 1A member 3 Homo sapiens 27-34 28630292-9 2017 A structural comparison of SULT1A3 with SULT1A1 (its immediate evolutionary progenitor) reveals how SULT1A3 acquired high affinity for THB and that the majority of residue changes needed to transform 1A1 into 1A3 are clustered at the allosteric and active sites. sapropterin 135-138 sulfotransferase family 1A member 3 Homo sapiens 100-107 28286122-5 2017 Two regioisomers of sulfated genistein were produced by E. coli cells expressing human SULT1A3, SULT1C4, or SULT1E1, and purified using Diaion HP20 resin, followed by high pressure liquid chromatography (HPLC). Genistein 29-38 sulfotransferase family 1A member 3 Homo sapiens 87-94 28286122-6 2017 Structural analysis using mass spectrometry (MS) and nuclear magnetic resonance (NMR) revealed that E. coli cells expressing SULT1A3 preferentially produced genistein 4"-sulfate, whereas E. coli cells expressing SULT1C4 preferentially produced genistein 7-sulfate. Genistein 4'-sulfate 157-177 sulfotransferase family 1A member 3 Homo sapiens 125-132 28615633-5 2017 Most noticeably, we show that these patches induce a modulated charge distribution on the Oxygen atoms, in remarkable agreement with recent X-ray and STM observations. Oxygen 90-96 sulfotransferase family 1A member 3 Homo sapiens 150-153 28621981-0 2017 Adatom Extraction from Pristine Metal Terraces by Dissociative Oxygen Adsorption: Combined STM and Density Functional Theory Investigation of O/Ag(110). adatom 0-6 sulfotransferase family 1A member 3 Homo sapiens 91-94 28520435-2 2017 We have characterized local atomic and electronic structures of a periodically nanorippled graphene (3.4 nm period) prepared on a macrofacet of the 6H-SiC crystal using scanning tunneling microscopy/spectroscopy (STM/STS) and angle-resolved photoelectron spectroscopy (ARPES). Graphite 91-99 sulfotransferase family 1A member 3 Homo sapiens 213-216 28520435-4 2017 The STM/STS results indicate the strength of electron-phonon coupling to the out-of-plane phonon at the K points of graphene is periodically modified in accordance with the ripple structure. Graphite 116-124 sulfotransferase family 1A member 3 Homo sapiens 4-7 28304284-7 2017 We point out that, in contrast to SGM experiments on gapped semiconductors, the STM tip can induce a pn junction in graphene, which improves contrast and resolution in SGM. Graphite 116-124 sulfotransferase family 1A member 3 Homo sapiens 80-83 28177672-3 2017 At 10 mumol L-1 O-DMN concentration, however, only SULT1A1 and SULT1A3 displayed detectable activity, with the former being nearly 2 orders of magnitude more active than the latter. l-1 o-dmn 12-21 sulfotransferase family 1A member 3 Homo sapiens 63-70 28459587-3 2017 In situ low-temperature scanning tunneling microscopy (LT-STM) measurements were used to monitor the growth of the single-layer blue phosphorus, which forms triangular structures arranged hexagonally on the tellurium layer. blue 128-132 sulfotransferase family 1A member 3 Homo sapiens 58-61 28459587-3 2017 In situ low-temperature scanning tunneling microscopy (LT-STM) measurements were used to monitor the growth of the single-layer blue phosphorus, which forms triangular structures arranged hexagonally on the tellurium layer. Phosphorus 133-143 sulfotransferase family 1A member 3 Homo sapiens 58-61 28459587-4 2017 As revealed by in situ X-ray photoelectron spectroscopy, LT-STM measurements, and density functional theory calculation, the blue phosphorus layer weakly interacts with the underlying tellurium layer. Phosphorus 130-140 sulfotransferase family 1A member 3 Homo sapiens 60-63 28383079-6 2017 Yet, performing the iodine exposure at elevated surface temperatures similarly results in detachment of the organic networks via intercalation of an iodine monolayer also on Au(111) as evidenced by characteristic changes in STM. Iodine 20-26 sulfotransferase family 1A member 3 Homo sapiens 224-227 28441724-7 2017 Metabolism of picroside II (M4) into M4 sulfate (M8) was catalyzed by SULT1A1, SULT1E1, SULT1A2, SULT1A3, and SULT1C4. picroside II 14-26 sulfotransferase family 1A member 3 Homo sapiens 97-104 28441724-7 2017 Metabolism of picroside II (M4) into M4 sulfate (M8) was catalyzed by SULT1A1, SULT1E1, SULT1A2, SULT1A3, and SULT1C4. m4 sulfate 37-47 sulfotransferase family 1A member 3 Homo sapiens 97-104 28248487-21 2017 Finally an STM investigation of the nucleation behavior of a helicene, prepared via a remarkably short and efficient route, on a metal surface is described. helicenes 61-69 sulfotransferase family 1A member 3 Homo sapiens 11-14 28248487-21 2017 Finally an STM investigation of the nucleation behavior of a helicene, prepared via a remarkably short and efficient route, on a metal surface is described. Metals 129-134 sulfotransferase family 1A member 3 Homo sapiens 11-14 28383079-6 2017 Yet, performing the iodine exposure at elevated surface temperatures similarly results in detachment of the organic networks via intercalation of an iodine monolayer also on Au(111) as evidenced by characteristic changes in STM. Iodine 149-155 sulfotransferase family 1A member 3 Homo sapiens 224-227 28281744-2 2017 Recent advances in STM include tunneling from spin-polarized and superconducting tips, time-domain spectroscopy, and the fabrication of atomically precise Si nanoelectronics. Silicon 155-157 sulfotransferase family 1A member 3 Homo sapiens 19-22 28281744-4 2017 probe a single-atom transistor in silicon, fabricated using the precision of a STM, at microwave frequencies. Silicon 34-41 sulfotransferase family 1A member 3 Homo sapiens 79-82 28150825-2 2017 STM results revealed that H-T-BO, a BODIPY-based derivative, can form a semi-closed molecular network at the 1-phenyloctane/HOPG interface. h-t-bo 26-32 sulfotransferase family 1A member 3 Homo sapiens 0-3 28289217-2 2017 Here, we show that a combined atomic force microscopy/scanning tunneling microscopy (AFM/STM) experiment can both distinguish neutral O2 molecules in the triplet state from negatively charged (O2)- radicals and charge and discharge the molecules at will. Oxygen 134-136 sulfotransferase family 1A member 3 Homo sapiens 89-92 28289217-2 2017 Here, we show that a combined atomic force microscopy/scanning tunneling microscopy (AFM/STM) experiment can both distinguish neutral O2 molecules in the triplet state from negatively charged (O2)- radicals and charge and discharge the molecules at will. Oxygen 193-195 sulfotransferase family 1A member 3 Homo sapiens 89-92 28198627-2 2017 The inelastic contribution to the STM current is found to excite a large number of skeletal vibrational modes of the molecule, thereby inducing a deformation of the potential energy landscape along the hydrogen transfer coordinate. Hydrogen 202-210 sulfotransferase family 1A member 3 Homo sapiens 34-37 28150825-2 2017 STM results revealed that H-T-BO, a BODIPY-based derivative, can form a semi-closed molecular network at the 1-phenyloctane/HOPG interface. n-octylbenzene 109-123 sulfotransferase family 1A member 3 Homo sapiens 0-3 28150825-3 2017 After introducing C70 fullerene molecules into the network, two kinds of self-assembled nanoarrays were observed by STM. fullerene C70 18-31 sulfotransferase family 1A member 3 Homo sapiens 116-119 28178800-4 2017 As a consequence, STM imaging at room temperature results in more stable imaging at the monolayer coverage on Cu(100) than on Au(111), and work function measurements indicate a large interface dipole upon deposition of a monolayer of IL on Cu. Copper 110-112 sulfotransferase family 1A member 3 Homo sapiens 18-21 28178800-4 2017 As a consequence, STM imaging at room temperature results in more stable imaging at the monolayer coverage on Cu(100) than on Au(111), and work function measurements indicate a large interface dipole upon deposition of a monolayer of IL on Cu. Gold 126-128 sulfotransferase family 1A member 3 Homo sapiens 18-21 28008878-6 2017 Our results therefore suggest that a common non-adiabatic process mediates atomic and molecular manipulation induced by the STM on the Si(111)-7x7 surface and may also mediate similar manipulation induced by the laser irradiation of the Si(111)-7x7 surface. Silicon 237-239 sulfotransferase family 1A member 3 Homo sapiens 124-127 27924336-4 2017 We demonstrate the threading of a hexayne within a macrocycle to form a rotaxane and report measurements of the electrical conductance of this single supramolecular assembly within an STM break junction. hexayne 34-41 sulfotransferase family 1A member 3 Homo sapiens 184-187 28054048-1 2017 A new method to directly modify the surface structure and energy levels of a porphyrin monolayer was examined in the molecular scale using scanning tunneling microscopy and spectroscopy (STM and STS) and presented in this communication. Porphyrins 77-86 sulfotransferase family 1A member 3 Homo sapiens 187-190 28054048-4 2017 Reflection-absorption infrared spectroscopy (RAIRS) measurements further indicated that the STM observed intermolecular linkages are stabilized via hydrogen bonding. Hydrogen 148-156 sulfotransferase family 1A member 3 Homo sapiens 92-95 28008878-6 2017 Our results therefore suggest that a common non-adiabatic process mediates atomic and molecular manipulation induced by the STM on the Si(111)-7x7 surface and may also mediate similar manipulation induced by the laser irradiation of the Si(111)-7x7 surface. Silicon 135-137 sulfotransferase family 1A member 3 Homo sapiens 124-127 28058415-3 2017 In contrast to bilayers and multilayers, the trilayer structure appears to grow pseudomorphic with the Au(111) substrate, and in addition we reveal the presence of a hydroxyl overlayer on this island type as evidenced by the appearance of a superstructure in STM correlated with the fingerprints of OH species in XPS and valence band spectroscopy. Hydroxyl Radical 166-174 sulfotransferase family 1A member 3 Homo sapiens 259-262 27924336-4 2017 We demonstrate the threading of a hexayne within a macrocycle to form a rotaxane and report measurements of the electrical conductance of this single supramolecular assembly within an STM break junction. Rotaxanes 72-80 sulfotransferase family 1A member 3 Homo sapiens 184-187 27709716-5 2016 Further experimental observation disclosed that the boronic ester-linked system is sensitive to instantaneous voltage pulses and the stimulation of the STM tip. boronic ester 52-65 sulfotransferase family 1A member 3 Homo sapiens 152-155 28725524-5 2017 Taking advantage of the uniaxial out-of-plane magnetic anisotropy of Co bilayer nanoisland on Cu(111), in-field spin-STM on this system has enabled a quantitative determination, and thereby, a categorization of the magnetic states of the tips. Copper 94-96 sulfotransferase family 1A member 3 Homo sapiens 117-120 27782454-1 2016 We present a room temperature STM study of perylene adsorption on Ag(110) at the monolayer coverage regime. Perylene 43-51 sulfotransferase family 1A member 3 Homo sapiens 30-33 27722251-2 2016 A 2,3,6,7,10,11-hexahydroxy-triphenylene close-packing structure was observed by STM instead of unorganized clusters, as well as amine and acid nanostructures. 2,3,6,7,10,11-hexahydroxytriphenylene 2-40 sulfotransferase family 1A member 3 Homo sapiens 81-84 27603175-2 2016 According to the formation energy and the simulated STM image, the Ge atoms substituted by the Au atoms have been confirmed as occurring at a Au coverage lower than 0.25 Ml. Gold 95-97 sulfotransferase family 1A member 3 Homo sapiens 52-55 27778005-1 2016 In this article, we investigate a single molecule magnet bis(phthalocyaninato)terbium(iii) (TbPc2) molecule film by using low temperature STM. bis(phthalocyaninato)terbium(iii) 57-90 sulfotransferase family 1A member 3 Homo sapiens 138-141 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 51-53 sulfotransferase family 1A member 3 Homo sapiens 0-3 27714039-4 2016 Our results reveal that there exist three energetically favorable borophene structures (beta5, chi1, and chi2) on the Ag(111) surface and their simulated STM images are in good agreement with experimental results, suggesting the coexistence of boron phases during the growth. borophene 66-75 sulfotransferase family 1A member 3 Homo sapiens 154-157 27459268-2 2016 In this Letter, we use scanning tunneling microscopy and spectroscopy (STM/STS) to study the electron confinement within individual ring-shaped cycloparaphenylene (CPP) molecules forming self-assembled films on Ag(111) and Au(111) surfaces. cpp 164-167 sulfotransferase family 1A member 3 Homo sapiens 71-74 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 27397949-2 2016 STM images indicate that growth morphology of both Si on Si and Si on H-terminated Si (H: Si) is epitaxial in nature at temperatures as low as 250 C. For Si on Si growth at 250 C, we show that the Si epitaxial growth front maintains a constant morphology after reaching a specific thickness threshold. Silicon 57-59 sulfotransferase family 1A member 3 Homo sapiens 0-3 26667964-1 2016 The self-organization of tri-adamantyl (TAB) benzene molecules has been investigated using low temperature scanning tunneling microscopy (LT-STM). tri-adamantyl (tab) benzene 25-52 sulfotransferase family 1A member 3 Homo sapiens 141-144 27140292-6 2016 The STM studies were completed by electrochemical methods, like cyclic voltammetry, the potentiostatic intermittent titration technique and charge/discharge tests of MCMB electrodes. mcmb 166-170 sulfotransferase family 1A member 3 Homo sapiens 4-7 27517780-2 2016 We demonstrate that the previous assignment of the dark objects in STM to chemisorbed oxygen atoms is incorrect and incompatible with trefoil-like structures observed in atomic-resolution images in current work. Oxygen 86-92 sulfotransferase family 1A member 3 Homo sapiens 67-70 27379457-7 2016 Ambient STM imaging showed the formation of long 1D SMON rather than 2D assembly on the basal plane of highly oriented pyrolytic graphite (HOPG) surface after simple dropcasting of the solution of preassembled concentric hexagons onto a freshly cleaved surface of HOPG. Graphite 129-137 sulfotransferase family 1A member 3 Homo sapiens 8-11 26667964-5 2016 The calculations demonstrate that the stability of the largest structures is obtained through the increase of the interfacial energy induced by the rotation of the adamantyl groups, a behavior whose consequences explain the subtle contrasts observed in the experimental STM images. adamantyl 164-173 sulfotransferase family 1A member 3 Homo sapiens 270-273 27300256-1 2016 Through STM images, we show that azobenzene-terminated alkanethiols hover and twirl when confined between the Ag tip and Au(111) substrate of an STM junction. azobenzene 33-43 sulfotransferase family 1A member 3 Homo sapiens 8-11 27445217-5 2016 Our STM investigations clearly resolve a high intrinsic concentration of individual sulfur atom vacancies, and experimentally identify the nature of the defect induced electronic mid-gap states, by combining topographic STM images with ab intio calculations. Sulfur 84-90 sulfotransferase family 1A member 3 Homo sapiens 4-7 27448898-0 2016 Metal dependent motif transition in a self-assembled monolayer of bipyridine derivatives via coordination: An STM study. Metals 0-5 sulfotransferase family 1A member 3 Homo sapiens 110-113 27448898-0 2016 Metal dependent motif transition in a self-assembled monolayer of bipyridine derivatives via coordination: An STM study. 2,2'-Dipyridyl 66-76 sulfotransferase family 1A member 3 Homo sapiens 110-113 27086932-3 2016 Titanyl-TiO2 and titanyl-Ti2O3 reconstructions can be used for rationalizing the experimental findings, matching the STM images and the changes in the band gap. titanyl-tio2 0-12 sulfotransferase family 1A member 3 Homo sapiens 117-120 27086932-3 2016 Titanyl-TiO2 and titanyl-Ti2O3 reconstructions can be used for rationalizing the experimental findings, matching the STM images and the changes in the band gap. titanyl-ti2o3 17-30 sulfotransferase family 1A member 3 Homo sapiens 117-120 27300256-1 2016 Through STM images, we show that azobenzene-terminated alkanethiols hover and twirl when confined between the Ag tip and Au(111) substrate of an STM junction. azobenzene 33-43 sulfotransferase family 1A member 3 Homo sapiens 145-148 27300256-1 2016 Through STM images, we show that azobenzene-terminated alkanethiols hover and twirl when confined between the Ag tip and Au(111) substrate of an STM junction. alkanethiols 55-67 sulfotransferase family 1A member 3 Homo sapiens 8-11 27300256-1 2016 Through STM images, we show that azobenzene-terminated alkanethiols hover and twirl when confined between the Ag tip and Au(111) substrate of an STM junction. alkanethiols 55-67 sulfotransferase family 1A member 3 Homo sapiens 145-148 27300256-1 2016 Through STM images, we show that azobenzene-terminated alkanethiols hover and twirl when confined between the Ag tip and Au(111) substrate of an STM junction. Gold 121-123 sulfotransferase family 1A member 3 Homo sapiens 8-11 27300256-1 2016 Through STM images, we show that azobenzene-terminated alkanethiols hover and twirl when confined between the Ag tip and Au(111) substrate of an STM junction. Gold 121-123 sulfotransferase family 1A member 3 Homo sapiens 145-148 27189131-7 2016 Atomically resolved STM images on the hills of the nanostructures on the Ge(001) surface have confirmed the presence of a graphene monolayer. Graphite 122-130 sulfotransferase family 1A member 3 Homo sapiens 20-23 26605698-3 2016 Supported by first-principles calculations we show how this tip termination can be identified by contrast analysis in noncontact atomic force and scanning tunneling microscopy (NC-AFM, STM) on a partially oxidized Cu(110) surface. Copper 214-216 sulfotransferase family 1A member 3 Homo sapiens 185-188 27165124-0 2016 Understanding the STM images of epitaxial graphene on a reconstructed 6H-SiC(0001) surface: the role of tip-induced mechanical distortion of graphene. Graphite 42-50 sulfotransferase family 1A member 3 Homo sapiens 18-21 27165124-6 2016 Therefore, a constant current STM image of EG on a reconstructed 6H-SiC(0001) surface does not reproduce its real topography but corresponds to the measured LDOS modulations, which depend on the variable tip-induced graphene distortion within the (6 x 6) quasi-cell. Graphite 216-224 sulfotransferase family 1A member 3 Homo sapiens 30-33 27172905-4 2016 Especially, the cycloparaphenylene structure is firstly observed by STM. cycloparaphenylene 16-34 sulfotransferase family 1A member 3 Homo sapiens 68-71 26991048-5 2016 The molecular arrangements, the increase of the average number of molecules per unit cell via ripening, and the rearrangement upon manipulation with the STM tip indicate an influence of the dipole moment on the molecular assembly and the rearrangement. dipole 190-196 sulfotransferase family 1A member 3 Homo sapiens 153-156 26805467-11 2016 The expression levels of CYP3A4, UGT1A, SULT1A1, P-gp, MRP2, and MRP3 were remarkably increased in the CS-treated cells, whereas the protein levels of SULT1A3 and BCRP were decreased. 7,3'-dihydroxy-4'-methoxyisoflavone 103-105 sulfotransferase family 1A member 3 Homo sapiens 151-158 26766161-2 2016 Here, using scanning tunneling microscopy and spectroscopy (STM/STS) supported by theoretical modeling, we study the interaction of a planar organic molecule (trinaphthylene) with a hydrogen-passivated Ge(001):H substrate and a single dangling bond quantum dot on that surface. Trinaphthylene 159-173 sulfotransferase family 1A member 3 Homo sapiens 60-63 26766161-2 2016 Here, using scanning tunneling microscopy and spectroscopy (STM/STS) supported by theoretical modeling, we study the interaction of a planar organic molecule (trinaphthylene) with a hydrogen-passivated Ge(001):H substrate and a single dangling bond quantum dot on that surface. Hydrogen 182-190 sulfotransferase family 1A member 3 Homo sapiens 60-63 26766161-3 2016 The electronic structure of the molecule adsorbed on the hydrogen-passivated surface is similar to the gas phase structure and the measurements show that HOMO and LUMO states contribute to the STM filled and empty state images, respectively. Hydrogen 57-65 sulfotransferase family 1A member 3 Homo sapiens 193-196 26544119-4 2016 Kinetic parameters of SULT1A1, SULT1A3, SULT1C4, and SULT1E1 that showed stronger 6-gingerol-sulfating activity were determined. gingerol 82-92 sulfotransferase family 1A member 3 Homo sapiens 31-38 27208961-1 2016 We present scanning tunneling microscopy and spectroscopy (STM/STS) investigations of the electronic structures of different alkyl-substituted oligothiophenes on the Au(111) surface. alkyl-substituted oligothiophenes 125-158 sulfotransferase family 1A member 3 Homo sapiens 59-62 27208961-2 2016 STM imaging showed that on Au(111), oligothiophenes adopted distinct straight and bent conformations. Gold 27-29 sulfotransferase family 1A member 3 Homo sapiens 0-3 27208961-3 2016 By combining STS maps with STM images, we visualize, in real space, particle-in-a-box-like oligothiophene molecular orbitals. oligothiophene 91-105 sulfotransferase family 1A member 3 Homo sapiens 27-30 27079234-7 2016 Plasma higher concentrations of sTM in cases are not caused by TM expression and may be only a result of Hcy induced endothelial injury. Homocysteine 105-108 sulfotransferase family 1A member 3 Homo sapiens 32-35 27036469-0 2016 STM study of PTCDA on Sn/Si(111)-2 3x2 3. 3,4,9,10-perylenetetracarboxylic dianhydride 13-18 sulfotransferase family 1A member 3 Homo sapiens 0-3 27036469-0 2016 STM study of PTCDA on Sn/Si(111)-2 3x2 3. Tin 22-24 sulfotransferase family 1A member 3 Homo sapiens 0-3 27036469-0 2016 STM study of PTCDA on Sn/Si(111)-2 3x2 3. Silicon 25-27 sulfotransferase family 1A member 3 Homo sapiens 0-3 26938931-8 2016 maintain a stable lone pair configuration that selectively bonds to specific, undercoordinated transition metal atoms available following rupture of a metal point contact in the STM-BJ experiments. Metals 106-111 sulfotransferase family 1A member 3 Homo sapiens 178-181 26599691-9 2016 Among phenol sulfotransferase SULT1A1 was not sensitive to studied factors, whereas the expression of SULT1A3 was depended on oxygen only in minimal medium. Oxygen 126-132 sulfotransferase family 1A member 3 Homo sapiens 102-109 26741732-7 2016 The latter procedure was previously proposed to result in a structure with three surface vanadium atoms in the 2D unit cell and we confirm this with simulated STM images. Vanadium 89-97 sulfotransferase family 1A member 3 Homo sapiens 159-162 27582324-0 2016 Human Cytosolic Sulfotransferase SULT1A3 Mediates the Sulfation of Dextrorphan. Dextrorphan 67-78 sulfotransferase family 1A member 3 Homo sapiens 33-40 26628411-4 2016 Structural isomers of bis-substituted anthraquinone derivatives 1,8-A-2OCn, 2,6-A-2OCn, 1,4-A-2OCn and 1,5-A-2OCn (n = 15, 16) were used and investigated by STM. bis-substituted anthraquinone 22-51 sulfotransferase family 1A member 3 Homo sapiens 157-160 27582324-3 2016 Data from the enzymatic assays showed that, of all thirteen known human SULTs, SULT1A3 displayed the strongest dextrorphan-sulfating activity. Dextrorphan 111-122 sulfotransferase family 1A member 3 Homo sapiens 79-86 26885457-0 2015 Effects of spin-orbit coupling and many-body correlations in STM transport through copper phthalocyanine. copper phthalocyanine 83-104 sulfotransferase family 1A member 3 Homo sapiens 61-64 27449410-5 2016 Kinetic parameters of the sulfation of clioquinol and iodoquinol by three SULTs, SULT1A1, SULT1A3, and SULT1C4, that showed the strongest clioquinol/iodoquinolsulfating activity were determined. Clioquinol 39-49 sulfotransferase family 1A member 3 Homo sapiens 90-97 27449410-5 2016 Kinetic parameters of the sulfation of clioquinol and iodoquinol by three SULTs, SULT1A1, SULT1A3, and SULT1C4, that showed the strongest clioquinol/iodoquinolsulfating activity were determined. Iodoquinol 54-64 sulfotransferase family 1A member 3 Homo sapiens 90-97 27449410-5 2016 Kinetic parameters of the sulfation of clioquinol and iodoquinol by three SULTs, SULT1A1, SULT1A3, and SULT1C4, that showed the strongest clioquinol/iodoquinolsulfating activity were determined. Clioquinol 138-148 sulfotransferase family 1A member 3 Homo sapiens 90-97 27449410-5 2016 Kinetic parameters of the sulfation of clioquinol and iodoquinol by three SULTs, SULT1A1, SULT1A3, and SULT1C4, that showed the strongest clioquinol/iodoquinolsulfating activity were determined. iodoquinolsulfating 149-168 sulfotransferase family 1A member 3 Homo sapiens 90-97 26998528-5 2016 Simulated STM images reproduce the patterns seen experimentally, and identify the bright protrusions as Ba atoms. Barium 104-106 sulfotransferase family 1A member 3 Homo sapiens 10-13 26548479-3 2015 We explore the cooperative interactions among CO2 molecules, Au-PDI chains and Au substrates that are responsible for the self-catalyzed capture by low temperature scanning tunneling microscopy (LT-STM), X-ray photoelectron spectroscopy (XPS), infrared reflection absorption spectroscopy (IRAS), temperature-programmed desorption (TPD), and dispersion corrected density functional theory (DFT). N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide 46-49 sulfotransferase family 1A member 3 Homo sapiens 198-201 26482225-2 2015 STM and atomic-resolution non-contact AFM imaging reveal rectangular flakes of nanographene featuring parallel pairs of zig-zag and armchair edges resulting from the lateral fusion of two pentacene subunits. nanographene 79-91 sulfotransferase family 1A member 3 Homo sapiens 0-3 26560972-3 2015 Here we report the STM observation of a graphene superlattice with concave (nanomesh) morphology on Au(111). Graphite 40-48 sulfotransferase family 1A member 3 Homo sapiens 19-22 26560972-3 2015 Here we report the STM observation of a graphene superlattice with concave (nanomesh) morphology on Au(111). Gold 100-102 sulfotransferase family 1A member 3 Homo sapiens 19-22 26611713-6 2015 As expected, the recombinant SULT1A3 enzyme showed a high similarity in raloxifene sulfonation profiles with the lysate preparation. Raloxifene Hydrochloride 72-82 sulfotransferase family 1A member 3 Homo sapiens 29-36 26518039-3 2015 We capture nanometer resolution images of electronically excited PbS quantum dots (QDs) by single molecule absorption scanning tunneling microscopy (SMA-STM). Lead 65-68 sulfotransferase family 1A member 3 Homo sapiens 153-156 26067475-3 2015 A systematic analysis showed that three of the twelve human SULTs, SULT1A1, SULT1A3 and SULT1C4, displayed the strongest sulphating activity towards acetaminophen. Acetaminophen 149-162 sulfotransferase family 1A member 3 Homo sapiens 76-83 26611713-0 2015 Sulfonation of raloxifene in HEK293 cells overexpressing SULT1A3: Involvement of breast cancer resistance protein (BCRP/ABCG2) and multidrug resistance-associated protein 4 (MRP4/ABCC4) in excretion of sulfate metabolites. Raloxifene Hydrochloride 15-25 sulfotransferase family 1A member 3 Homo sapiens 57-64 26611713-0 2015 Sulfonation of raloxifene in HEK293 cells overexpressing SULT1A3: Involvement of breast cancer resistance protein (BCRP/ABCG2) and multidrug resistance-associated protein 4 (MRP4/ABCC4) in excretion of sulfate metabolites. Sulfates 202-209 sulfotransferase family 1A member 3 Homo sapiens 57-64 26291395-0 2015 Efflux transport of chrysin and apigenin sulfates in HEK293 cells overexpressing SULT1A3: The role of multidrug resistance-associated protein 4 (MRP4/ABCC4). Sulfates 41-49 sulfotransferase family 1A member 3 Homo sapiens 81-88 26291395-11 2015 The SULT1A3 modified HEK293 cells were an appropriate tool to study SULT1A3-mediated sulfonation and to characterize BCRP/MRP4-mediated sulfate transport. Sulfates 136-143 sulfotransferase family 1A member 3 Homo sapiens 4-11 26256407-4 2015 We show that chemical identification of boron and nitrogen substitutional defects can be achieved in the STM channel due to the quantum interference effect, arising due to the specific electronic structure of nitrogen dopant sites. Boron 40-45 sulfotransferase family 1A member 3 Homo sapiens 105-108 26117434-6 2015 Preliminary results with STM and AFM atomic resolution imaging at 4.5 K of the silicon Si(111)-7x7 surface are presented. Silicon 79-86 sulfotransferase family 1A member 3 Homo sapiens 25-28 26278062-0 2015 Heat-induced formation of one-dimensional coordination polymers on Au(111): an STM study. Polymers 55-63 sulfotransferase family 1A member 3 Homo sapiens 79-82 26278062-0 2015 Heat-induced formation of one-dimensional coordination polymers on Au(111): an STM study. Gold 67-69 sulfotransferase family 1A member 3 Homo sapiens 79-82 28791089-1 2015 We report STM investigations on a linear oligophenyleneethylene (OPE)-based self-assembling Pd(ii) complex 1 that forms highly-ordered concentration dependent patterns on HOPG. oligophenyleneethylene 41-63 sulfotransferase family 1A member 3 Homo sapiens 10-13 28791089-1 2015 We report STM investigations on a linear oligophenyleneethylene (OPE)-based self-assembling Pd(ii) complex 1 that forms highly-ordered concentration dependent patterns on HOPG. phosphorylethanolamine 65-68 sulfotransferase family 1A member 3 Homo sapiens 10-13 28791089-1 2015 We report STM investigations on a linear oligophenyleneethylene (OPE)-based self-assembling Pd(ii) complex 1 that forms highly-ordered concentration dependent patterns on HOPG. pd(ii) complex 92-106 sulfotransferase family 1A member 3 Homo sapiens 10-13 26247871-1 2015 Through a careful design of the molecular precursor we have successfully constructed the metal-organic Sierpinski triangles on Au(111) via on-surface coordination chemistry, which is demonstrated by the interplay of high-resolution STM imaging and DFT calculations. Metals 89-94 sulfotransferase family 1A member 3 Homo sapiens 232-235 26256407-4 2015 We show that chemical identification of boron and nitrogen substitutional defects can be achieved in the STM channel due to the quantum interference effect, arising due to the specific electronic structure of nitrogen dopant sites. Nitrogen 50-58 sulfotransferase family 1A member 3 Homo sapiens 105-108 26256407-4 2015 We show that chemical identification of boron and nitrogen substitutional defects can be achieved in the STM channel due to the quantum interference effect, arising due to the specific electronic structure of nitrogen dopant sites. Nitrogen 209-217 sulfotransferase family 1A member 3 Homo sapiens 105-108 26301490-11 2015 It is demonstrated for surface-oxidized Cu(100) that simultaneous 3D-AFM/STM yields resolution of both the Cu and O atoms. Copper 40-42 sulfotransferase family 1A member 3 Homo sapiens 73-76 26301490-11 2015 It is demonstrated for surface-oxidized Cu(100) that simultaneous 3D-AFM/STM yields resolution of both the Cu and O atoms. Copper 107-109 sulfotransferase family 1A member 3 Homo sapiens 73-76 27279673-1 2015 We have deposited 4-aminophenol on Pt(111) surfaces in ultra-high vacuum and studied the strength of its adsorption through a combination of STM, LEED, XPS and ab initio calculations. 4-aminophenol 18-31 sulfotransferase family 1A member 3 Homo sapiens 141-144 26291093-1 2015 Using inelastic electron tunneling spectroscopy with the scanning tunneling microscope (STM-IETS) and density functional theory calculations (DFT), we investigated properties of a single H2 molecule trapped in nanocavities with controlled shape and separation between the STM tip and the Au (110) surface. Hydrogen 187-189 sulfotransferase family 1A member 3 Homo sapiens 88-91 26291093-1 2015 Using inelastic electron tunneling spectroscopy with the scanning tunneling microscope (STM-IETS) and density functional theory calculations (DFT), we investigated properties of a single H2 molecule trapped in nanocavities with controlled shape and separation between the STM tip and the Au (110) surface. Hydrogen 187-189 sulfotransferase family 1A member 3 Homo sapiens 272-275 25941087-2 2015 The current study was designed to identify the human SULTs that are capable of sulfating ritodrine and to investigate how genetic polymorphism of the major ritodrine-sulfating SULT, SULT1A3, may affect its sulfating activity. Ritodrine 156-165 sulfotransferase family 1A member 3 Homo sapiens 182-189 26196408-1 2015 Low-temperature scanning tunneling microscopy (LT-STM) was used to move hydrogen atoms and dissociate NH molecules on a Pt(111) surface covered with an ordered array of nitrogen atoms in a (2 x 2) structure. Hydrogen 72-80 sulfotransferase family 1A member 3 Homo sapiens 50-53 25941087-3 2015 A systematic analysis revealed that of the 13 known human SULTs, SULT1A1, SULT1A3, and SULT1C4, were capable of mediating the sulfation of ritodrine, with SULT1A3 displaying the strongest sulfating activity. Ritodrine 139-148 sulfotransferase family 1A member 3 Homo sapiens 74-81 25941087-3 2015 A systematic analysis revealed that of the 13 known human SULTs, SULT1A1, SULT1A3, and SULT1C4, were capable of mediating the sulfation of ritodrine, with SULT1A3 displaying the strongest sulfating activity. Ritodrine 139-148 sulfotransferase family 1A member 3 Homo sapiens 155-162 25941087-6 2015 Purified SULT1A3 allozymes were shown to exhibit differential sulfating activity toward ritodrine. Ritodrine 88-97 sulfotransferase family 1A member 3 Homo sapiens 9-16 26083646-1 2015 Incorporating spin-polarized scanning tunneling microscopy (SP-STM) measurements and first-principles calculations, we resolve spin-polarized states and consequent features in a pentacene(PEN)-Co hybrid system. pentacene 178-187 sulfotransferase family 1A member 3 Homo sapiens 63-66 26192733-4 2015 These graphene-BNNT heterojunctions were characterized at room temperature by four-probe scanning tunneling microscopy (4-probe STM) under real-time monitoring of scanning electron microscopy (SEM). Graphite 6-14 sulfotransferase family 1A member 3 Homo sapiens 128-131 26230805-1 2015 An emerging route to nanostructured hybrid organic-metal interfaces with tailored properties is their manipulation by nanomechanical forces as exerted by STM and AFM tips. Metals 51-56 sulfotransferase family 1A member 3 Homo sapiens 154-157 26230817-1 2015 STM conductance spectroscopy and mapping has been used to analyze the impact of molecular adsorption on the quantized electronic structure of individual metal nanoparticles. Metals 153-158 sulfotransferase family 1A member 3 Homo sapiens 0-3 25900852-0 2015 STM study of electrical transport properties of one dimensional contacts between MnSi(~1.7) nanowires and Si(111) and (110) substrates. Silicon 83-85 sulfotransferase family 1A member 3 Homo sapiens 0-3 25704561-0 2015 Surface Trapping and STM Observation of Conformational Isomers of a Bis(Terpyridine) Ligand from Metallosupramolecular Grids. bis(terpyridine) 68-84 sulfotransferase family 1A member 3 Homo sapiens 21-24 26037044-0 2015 Theory for STM images of resonances in the near-field regime: application to adsorbates and local defects on graphene. Graphite 109-117 sulfotransferase family 1A member 3 Homo sapiens 11-14 25899765-1 2015 PURPOSE: To compare safety and efficacy of surgeon-tailored polypropylene mesh through needleless single-incision technique (STM) versus tension-free vaginal tape-obturator (TVT-O) aiming to decrease cost of treatment of stress urinary incontinence (SUI). Polypropylenes 60-73 sulfotransferase family 1A member 3 Homo sapiens 125-128 25676631-6 2015 SULT1A3 is a major isoform catalyzing sulfonation of curcumin and demethoxycurcumin, but not for bisdemethoxycurcumin. Curcumin 53-61 sulfotransferase family 1A member 3 Homo sapiens 0-7 25913869-3 2015 In situ studies are presented of Au(111) electrodes in 1-butyl-1-methylpyrrolidinium bis(trifluoromethylsulfonyl)imide ([BMP][TFSA]) by high-speed scanning tunneling microscopy (video-STM). Gold 33-35 sulfotransferase family 1A member 3 Homo sapiens 184-187 25913869-3 2015 In situ studies are presented of Au(111) electrodes in 1-butyl-1-methylpyrrolidinium bis(trifluoromethylsulfonyl)imide ([BMP][TFSA]) by high-speed scanning tunneling microscopy (video-STM). 1-butyl-1-methylpyrrolidinium bis(trifluoromethylsulfonyl)imide 55-118 sulfotransferase family 1A member 3 Homo sapiens 184-187 25913869-3 2015 In situ studies are presented of Au(111) electrodes in 1-butyl-1-methylpyrrolidinium bis(trifluoromethylsulfonyl)imide ([BMP][TFSA]) by high-speed scanning tunneling microscopy (video-STM). tfsa 126-130 sulfotransferase family 1A member 3 Homo sapiens 184-187 25727408-3 2015 STM characterization reveals that the rigidity and affinity of building blocks to the surface has essential effects on the topology of the 2D polymers. Polymers 142-150 sulfotransferase family 1A member 3 Homo sapiens 0-3 25676631-6 2015 SULT1A3 is a major isoform catalyzing sulfonation of curcumin and demethoxycurcumin, but not for bisdemethoxycurcumin. demethoxycurcumin 66-83 sulfotransferase family 1A member 3 Homo sapiens 0-7 25611676-2 2015 Cyclic voltammetry (CV), electrochemically controlled scanning tunneling microscopy (EC-STM), and density functional theory (DFT) calculations have been employed in the present study to address the adsorption of the four nucleobases adenine (A), cytosine (C), guanine (G), and thymine (T), on the Au(110)-electrode surface. nucleobases 221-232 sulfotransferase family 1A member 3 Homo sapiens 88-91 25735599-3 2015 The morphology and physical properties of nanoparticle-supported graphene are investigated by atomic force microscopy, optical reflectance spectroscopy, scanning tunneling microscopy and spectroscopy (STM/STS), and confocal Raman spectroscopy. Graphite 65-73 sulfotransferase family 1A member 3 Homo sapiens 201-204 25735599-6 2015 STM and STS measurements show that the local density of electronic states in graphene is modulated by the underlying gold nanoparticles. Graphite 77-85 sulfotransferase family 1A member 3 Homo sapiens 0-3 25165021-6 2015 CONCLUSION: The common trunk of the SHM and STM is the prime choice for laryngeal reinnervation using AC-RLN non-selective anastomosis. ac-rln 102-108 sulfotransferase family 1A member 3 Homo sapiens 44-47 25414133-0 2015 Mapping the site-specific potential energy landscape for chemisorbed and physisorbed aromatic molecules on the Si(1 1 1)-7 x 7 surface by time-lapse STM. Silicon 111-113 sulfotransferase family 1A member 3 Homo sapiens 149-152 24692077-0 2015 SULT 1A3 single-nucleotide polymorphism and the single dose pharmacokinetics of inhaled salbutamol enantiomers: are some athletes at risk of higher urine levels? Albuterol 88-98 sulfotransferase family 1A member 3 Homo sapiens 0-8 24692077-1 2015 The study was designed to investigate the effect of a common genetic variation of the main salbutamol metabolizing enzyme SULT1A3 (single nucleotide polymorphism 105A>G, rs1975350) on the stereoselective pharmacokinetics of salbutamol. Albuterol 91-101 sulfotransferase family 1A member 3 Homo sapiens 122-129 24692077-1 2015 The study was designed to investigate the effect of a common genetic variation of the main salbutamol metabolizing enzyme SULT1A3 (single nucleotide polymorphism 105A>G, rs1975350) on the stereoselective pharmacokinetics of salbutamol. Albuterol 227-237 sulfotransferase family 1A member 3 Homo sapiens 122-129 25376428-2 2014 Herein, we demonstrate that an electric field applied between an STM tip and a substrate triggered the formation of a bilayer structure at the solid-liquid interface. 4-IODO-1-VINYL-1H-PYRAZOLE 149-155 sulfotransferase family 1A member 3 Homo sapiens 65-68 27877752-3 2015 Secondly, oscillation in tunneling current between binary states, which is considered to reflect a conformational change in the topmost Zn-Te structure between the reconstructed and bulk-like ideal structures, was directly observed by STM. zn-te 136-141 sulfotransferase family 1A member 3 Homo sapiens 235-238 25489793-0 2014 The evolution of the polycrystalline copper surface, first to Cu(111) and then to Cu(100), at a fixed CO2RR potential: a study by operando EC-STM. polycrystalline 21-36 sulfotransferase family 1A member 3 Homo sapiens 142-145 25489793-0 2014 The evolution of the polycrystalline copper surface, first to Cu(111) and then to Cu(100), at a fixed CO2RR potential: a study by operando EC-STM. Copper 37-43 sulfotransferase family 1A member 3 Homo sapiens 142-145 25489793-1 2014 A study based on operando electrochemical scanning tunneling microscopy (EC-STM) has shown that a polycrystalline Cu electrode held at a fixed negative potential, -0.9 V (vs SHE), in the vicinity of CO2 reduction reactions (CO2RR) in 0.1 M KOH, undergoes stepwise surface reconstruction, first to Cu(111) within 30 min, and then to Cu(100) after another 30 min; no further surface transformations occurred after establishment of the Cu(100) surface. Copper 114-116 sulfotransferase family 1A member 3 Homo sapiens 76-79 25489793-1 2014 A study based on operando electrochemical scanning tunneling microscopy (EC-STM) has shown that a polycrystalline Cu electrode held at a fixed negative potential, -0.9 V (vs SHE), in the vicinity of CO2 reduction reactions (CO2RR) in 0.1 M KOH, undergoes stepwise surface reconstruction, first to Cu(111) within 30 min, and then to Cu(100) after another 30 min; no further surface transformations occurred after establishment of the Cu(100) surface. N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide 199-202 sulfotransferase family 1A member 3 Homo sapiens 76-79 25157669-1 2014 Electrochemical scanning tunneling microscopy (EC-STM) was employed to study the aggregation of trichogin OMe (TCG), an antimicrobial peptide, incorporated into a lipid monolayer. trichogin ome 96-109 sulfotransferase family 1A member 3 Homo sapiens 50-53 25157669-1 2014 Electrochemical scanning tunneling microscopy (EC-STM) was employed to study the aggregation of trichogin OMe (TCG), an antimicrobial peptide, incorporated into a lipid monolayer. TMG-chitotriomycin 111-114 sulfotransferase family 1A member 3 Homo sapiens 50-53 25337794-1 2014 The fundamental structure of an isolated water dimer on Pt(111) was determined by means of a spectroscopic method using scanning tunneling microscopy (STM) and density functional theory (DFT) calculations. Water 41-46 sulfotransferase family 1A member 3 Homo sapiens 151-154 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Water 4-9 sulfotransferase family 1A member 3 Homo sapiens 163-166 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Water 4-9 sulfotransferase family 1A member 3 Homo sapiens 168-174 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Hydrogen 66-74 sulfotransferase family 1A member 3 Homo sapiens 163-166 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Hydrogen 66-74 sulfotransferase family 1A member 3 Homo sapiens 168-174 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Water 180-185 sulfotransferase family 1A member 3 Homo sapiens 163-166 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Water 180-185 sulfotransferase family 1A member 3 Homo sapiens 168-174 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Water 180-185 sulfotransferase family 1A member 3 Homo sapiens 163-166 25337794-2 2014 Two water molecules on adjacent atop sites form a dimer through a hydrogen bond, and they rotate even at a substrate temperature of 5 K. Action spectroscopy using STM (STM-AS) for water dimer hopping allows us to obtain the vibrational spectrum of a single water dimer on Pt(111). Water 180-185 sulfotransferase family 1A member 3 Homo sapiens 168-174 25145767-2 2014 The STM manipulations demonstrate the feasibility of switching such weak-hydrogen-bonding patterns. Hydrogen 73-81 sulfotransferase family 1A member 3 Homo sapiens 4-7 25251167-5 2014 As shown from a combination of scanning tunneling microscopy, X-ray photoelectron spectroscopy, and density functional theory calculations, all four hydroxy groups of THB dehydrogenate upon thermal activation at 440 K. This highly reactive ligand binds to Cu adatom trimers, which are resolved by high-resolution STM. 1,2,4,5-tetrahydroxybenzene 167-170 sulfotransferase family 1A member 3 Homo sapiens 313-316 26278608-0 2014 Concerted Thermal-Plus-Electronic Nonlocal Desorption of Chlorobenzene from Si(111)-7 x 7 in the STM. chlorobenzene 57-70 sulfotransferase family 1A member 3 Homo sapiens 97-100 26278608-0 2014 Concerted Thermal-Plus-Electronic Nonlocal Desorption of Chlorobenzene from Si(111)-7 x 7 in the STM. Silicon 76-78 sulfotransferase family 1A member 3 Homo sapiens 97-100 26278608-1 2014 The rate of desorption of chemisorbed chlorobenzene molecules from the Si(111)-7 x 7 surface, induced by nonlocal charge injection from an STM tip, depends on the surface temperature. chlorobenzene 38-51 sulfotransferase family 1A member 3 Homo sapiens 139-142 26278608-1 2014 The rate of desorption of chemisorbed chlorobenzene molecules from the Si(111)-7 x 7 surface, induced by nonlocal charge injection from an STM tip, depends on the surface temperature. Silicon 71-73 sulfotransferase family 1A member 3 Homo sapiens 139-142 25145767-1 2014 From an interplay of high-resolution STM imaging/manipulation and DFT calculations, we have revealed that different self-assembled nanostructures of BA molecules on Cu(110) are attributable to specific molecular adsorption geometries, and thus the corresponding intermolecular hydrogen bonding patterns. Barium 149-151 sulfotransferase family 1A member 3 Homo sapiens 37-40 25145767-1 2014 From an interplay of high-resolution STM imaging/manipulation and DFT calculations, we have revealed that different self-assembled nanostructures of BA molecules on Cu(110) are attributable to specific molecular adsorption geometries, and thus the corresponding intermolecular hydrogen bonding patterns. Copper 165-167 sulfotransferase family 1A member 3 Homo sapiens 37-40 25264847-0 2014 Switching at the nanoscale: light- and STM-tip-induced switch of a thiolated diarylethene self-assembly on Au(111). thiolated diarylethene 67-89 sulfotransferase family 1A member 3 Homo sapiens 39-42 25264847-0 2014 Switching at the nanoscale: light- and STM-tip-induced switch of a thiolated diarylethene self-assembly on Au(111). Gold 107-109 sulfotransferase family 1A member 3 Homo sapiens 39-42 25264847-1 2014 The light-induced and STM-tip-induced switching of photochromic thiol functionalized terphenylthiazole-based diarylethene self-assembly on Au(111) has been investigated in ambient conditions. Sulfhydryl Compounds 64-69 sulfotransferase family 1A member 3 Homo sapiens 22-25 25264847-1 2014 The light-induced and STM-tip-induced switching of photochromic thiol functionalized terphenylthiazole-based diarylethene self-assembly on Au(111) has been investigated in ambient conditions. terphenylthiazole 85-102 sulfotransferase family 1A member 3 Homo sapiens 22-25 25264847-1 2014 The light-induced and STM-tip-induced switching of photochromic thiol functionalized terphenylthiazole-based diarylethene self-assembly on Au(111) has been investigated in ambient conditions. diarylethene 109-121 sulfotransferase family 1A member 3 Homo sapiens 22-25 25169153-4 2014 We can resolve the exact adsorption site and the configuration of fullerene by means of low-temperature scanning tunnelling microscopy (LT-STM) and density functional theory (DFT) calculations. Fullerenes 66-75 sulfotransferase family 1A member 3 Homo sapiens 139-142 24835946-1 2014 In the present work the inclusion complexation of three sulfonamide (SA) drugs, namely sulfisoxazole (SSX), sulfamethizole (SMZ), and Sulfamethazine (STM) with beta-cyclodextrin (beta-CD) has been investigated using UV-Vis spectroscopy, DSC, (1)H NMR spectroscopy, and molecular modeling methods. Sulfonamides 56-67 sulfotransferase family 1A member 3 Homo sapiens 150-153 24835946-1 2014 In the present work the inclusion complexation of three sulfonamide (SA) drugs, namely sulfisoxazole (SSX), sulfamethizole (SMZ), and Sulfamethazine (STM) with beta-cyclodextrin (beta-CD) has been investigated using UV-Vis spectroscopy, DSC, (1)H NMR spectroscopy, and molecular modeling methods. Sulfonamides 69-71 sulfotransferase family 1A member 3 Homo sapiens 150-153 24835946-1 2014 In the present work the inclusion complexation of three sulfonamide (SA) drugs, namely sulfisoxazole (SSX), sulfamethizole (SMZ), and Sulfamethazine (STM) with beta-cyclodextrin (beta-CD) has been investigated using UV-Vis spectroscopy, DSC, (1)H NMR spectroscopy, and molecular modeling methods. Sulfamethazine 134-148 sulfotransferase family 1A member 3 Homo sapiens 150-153 24835946-1 2014 In the present work the inclusion complexation of three sulfonamide (SA) drugs, namely sulfisoxazole (SSX), sulfamethizole (SMZ), and Sulfamethazine (STM) with beta-cyclodextrin (beta-CD) has been investigated using UV-Vis spectroscopy, DSC, (1)H NMR spectroscopy, and molecular modeling methods. betadex 160-177 sulfotransferase family 1A member 3 Homo sapiens 150-153 24835946-1 2014 In the present work the inclusion complexation of three sulfonamide (SA) drugs, namely sulfisoxazole (SSX), sulfamethizole (SMZ), and Sulfamethazine (STM) with beta-cyclodextrin (beta-CD) has been investigated using UV-Vis spectroscopy, DSC, (1)H NMR spectroscopy, and molecular modeling methods. betadex 179-186 sulfotransferase family 1A member 3 Homo sapiens 150-153 24835946-3 2014 Obtained results revealed that SA drugs form 1:1 inclusion complex with beta-CD with Kb of 650, 1532, 714M(-1) at 25 C for SSX, SMZ, and STM, respectively. betadex 72-79 sulfotransferase family 1A member 3 Homo sapiens 137-140 25123291-1 2014 By means of STM and nc-AFM the self-assembly of a new donor-acceptor (DA) dyad molecule on highly oriented pyrolytic graphite is identified and compared to molecular simulations. Graphite 117-125 sulfotransferase family 1A member 3 Homo sapiens 12-15 24777119-0 2014 Self-assembled alkanethiol monolayers on gold surfaces: resolving the complex structure at the interface by STM. alkanethiol 15-26 sulfotransferase family 1A member 3 Homo sapiens 108-111 24832963-5 2014 A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Oxymorphone 145-156 sulfotransferase family 1A member 3 Homo sapiens 198-205 24832963-5 2014 A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Morphine 227-235 sulfotransferase family 1A member 3 Homo sapiens 198-205 24832963-5 2014 A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Hydromorphone 240-253 sulfotransferase family 1A member 3 Homo sapiens 198-205 24832963-5 2014 A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Butorphanol 288-299 sulfotransferase family 1A member 3 Homo sapiens 198-205 24832963-5 2014 A systematic analysis using eleven known human SULTs and kinetic experiment revealed SULT1A1 as the major responsible SULTs for the sulfation of oxymorphone, nalbuphine, nalorphine, and naltrexone, SULT1A3 for the sulfation of morphine and hydromorphone, and SULT2A1 for the sulfation of butorphanol and levorphanol. Levorphanol 304-315 sulfotransferase family 1A member 3 Homo sapiens 198-205 24984144-1 2014 The supramolecular patterns of a thienophenanthrene derivative could be switched among dissimilar polymorphs with different halogen-bond densities by solution concentration, which is demonstrated through a combination of STM and density functional theory (DFT) calculations. thienophenanthrene 33-51 sulfotransferase family 1A member 3 Homo sapiens 221-224 24956261-0 2014 A silver nanowire-based tip suitable for STM tip-enhanced Raman scattering. Silver 2-8 sulfotransferase family 1A member 3 Homo sapiens 41-44 24956261-1 2014 A chemically synthesized silver nanowire was used for atomic-resolution STM imaging and tip-enhanced Raman scattering (TERS) spectroscopy, yielding excellent reproducibility. Silver 25-31 sulfotransferase family 1A member 3 Homo sapiens 72-75 25089732-4 2014 STM observations revealed that these molecules formed porous 2D networks whose pores were decorated with either fluoroalkane or simple alkane perimeters. fluoroalkane 112-124 sulfotransferase family 1A member 3 Homo sapiens 0-3 25089732-4 2014 STM observations revealed that these molecules formed porous 2D networks whose pores were decorated with either fluoroalkane or simple alkane perimeters. Alkanes 118-124 sulfotransferase family 1A member 3 Homo sapiens 0-3 24984144-1 2014 The supramolecular patterns of a thienophenanthrene derivative could be switched among dissimilar polymorphs with different halogen-bond densities by solution concentration, which is demonstrated through a combination of STM and density functional theory (DFT) calculations. Halogens 124-131 sulfotransferase family 1A member 3 Homo sapiens 221-224 25053445-2 2014 We present an approach to mount porphyrins in ordered monolayers on Au(111) by self-assembly and verify it, employing STM, absorption spectroscopy, and quantum chemical calculations. Porphyrins 32-42 sulfotransferase family 1A member 3 Homo sapiens 118-121 24905213-5 2014 Also, the presence of a distortion in a reconstructed surface pattern not only induces the presence of long-range order but also is able to drive the organization of DIP into two coexisting homochiral domains, in quantitative agreement with STM experiments. 3,5-diisopropylsalicylic acid 166-169 sulfotransferase family 1A member 3 Homo sapiens 241-244 24978587-3 2014 Herein, we demonstrate a method to build single-molecule wires with metalloporphyrins via their central metal ion by chemically modifying both an STM tip and surface electrodes with pyridin-4-yl-methanethiol, a molecule that has strong affinity for coordination with the metal ion of the porphyrin. Metalloporphyrins 68-85 sulfotransferase family 1A member 3 Homo sapiens 146-149 24978587-3 2014 Herein, we demonstrate a method to build single-molecule wires with metalloporphyrins via their central metal ion by chemically modifying both an STM tip and surface electrodes with pyridin-4-yl-methanethiol, a molecule that has strong affinity for coordination with the metal ion of the porphyrin. Metals 68-73 sulfotransferase family 1A member 3 Homo sapiens 146-149 24978587-3 2014 Herein, we demonstrate a method to build single-molecule wires with metalloporphyrins via their central metal ion by chemically modifying both an STM tip and surface electrodes with pyridin-4-yl-methanethiol, a molecule that has strong affinity for coordination with the metal ion of the porphyrin. Pyridin-4-ylmethanethiol 182-207 sulfotransferase family 1A member 3 Homo sapiens 146-149 24978587-3 2014 Herein, we demonstrate a method to build single-molecule wires with metalloporphyrins via their central metal ion by chemically modifying both an STM tip and surface electrodes with pyridin-4-yl-methanethiol, a molecule that has strong affinity for coordination with the metal ion of the porphyrin. Metals 104-109 sulfotransferase family 1A member 3 Homo sapiens 146-149 24978587-3 2014 Herein, we demonstrate a method to build single-molecule wires with metalloporphyrins via their central metal ion by chemically modifying both an STM tip and surface electrodes with pyridin-4-yl-methanethiol, a molecule that has strong affinity for coordination with the metal ion of the porphyrin. Porphyrins 75-84 sulfotransferase family 1A member 3 Homo sapiens 146-149 24990633-2 2014 We review the efforts so far, and then discuss the specific case of a silica bilayer, which exists in a crystalline and a vitreous variety, and puts us into a position to investigate, for the first time, the real space structure (AFM/STM) of a two-dimensional glass and its properties. Silicon Dioxide 70-76 sulfotransferase family 1A member 3 Homo sapiens 234-237 24773244-2 2014 The double-decker bis(phthalocyaninato)terbium(III) complex, which is single-molecule magnet and forms a Kondo resonance on a Au(111) surface through an unpaired pi-radical spin, is studied using scanning tunneling microscopy/spectroscopy (STM/STS). bis(phthalocyaninato)terbium(iii) 18-51 sulfotransferase family 1A member 3 Homo sapiens 240-243 24996100-2 2014 Here we report a combined STM and transport method capable of surface conductivity measurement of step-free or single-step containing surface regions and having minimal interaction with the sample, and by which we quantitatively determine the intrinsic conductivity of the Si-(7x7) surface. Silicon 273-275 sulfotransferase family 1A member 3 Homo sapiens 26-29 24718559-1 2014 The formation of large assemblies on the Si(111)-B surface is discussed with the help of STM simulations and DFT calculations. Silicon 41-43 sulfotransferase family 1A member 3 Homo sapiens 89-92 24525679-1 2014 Interplay between high-resolution STM imaging and DFT calculations demonstrates that through introduction of Ni atoms the self-assembled structures of cytosine could undergo a structural transformation from 1-D chains to 0-D clusters on Au(111). Cytosine 151-159 sulfotransferase family 1A member 3 Homo sapiens 34-37 24785057-5 2014 We find that the simulated filled-state STM images of surface-layer oxygen vacancies and fluorine impurities are essentially identical, which would render problematic their experimental distinction by such images alone. Oxygen 68-74 sulfotransferase family 1A member 3 Homo sapiens 40-43 24785057-5 2014 We find that the simulated filled-state STM images of surface-layer oxygen vacancies and fluorine impurities are essentially identical, which would render problematic their experimental distinction by such images alone. Fluorine 89-97 sulfotransferase family 1A member 3 Homo sapiens 40-43 24785057-7 2014 Based on these results, we propose that the surface defects observed in STM experiments on CeO2 single crystals reported heretofore were not oxygen vacancies, but fluorine impurities. ceric oxide 91-95 sulfotransferase family 1A member 3 Homo sapiens 72-75 24785057-7 2014 Based on these results, we propose that the surface defects observed in STM experiments on CeO2 single crystals reported heretofore were not oxygen vacancies, but fluorine impurities. Oxygen 141-147 sulfotransferase family 1A member 3 Homo sapiens 72-75 24785057-7 2014 Based on these results, we propose that the surface defects observed in STM experiments on CeO2 single crystals reported heretofore were not oxygen vacancies, but fluorine impurities. Fluorine 163-171 sulfotransferase family 1A member 3 Homo sapiens 72-75 24785057-8 2014 Since the similarity of the simulated STM images of the two defects is due primarily to the relative energies of the 2p states of oxygen and fluorine ions, this confusion might also occur for other oxides which have been either doped or contaminated with fluorine. Oxygen 130-136 sulfotransferase family 1A member 3 Homo sapiens 38-41 24785057-8 2014 Since the similarity of the simulated STM images of the two defects is due primarily to the relative energies of the 2p states of oxygen and fluorine ions, this confusion might also occur for other oxides which have been either doped or contaminated with fluorine. Fluorine 141-149 sulfotransferase family 1A member 3 Homo sapiens 38-41 24785057-8 2014 Since the similarity of the simulated STM images of the two defects is due primarily to the relative energies of the 2p states of oxygen and fluorine ions, this confusion might also occur for other oxides which have been either doped or contaminated with fluorine. Fluorine 255-263 sulfotransferase family 1A member 3 Homo sapiens 38-41 24651211-3 2014 Here, we report an in-situ low-temperature scanning tunneling microscopy (LT-STM) study of the elementary process of chemical vapor deposition (CVD) graphene growth via thermal decomposition of methane on Cu(110), including the formation of monodispersed carbon clusters at the initial stage, the graphene nucleation and the ripening of graphene islands to form continuous graphene film. Graphite 149-157 sulfotransferase family 1A member 3 Homo sapiens 77-80 24651211-3 2014 Here, we report an in-situ low-temperature scanning tunneling microscopy (LT-STM) study of the elementary process of chemical vapor deposition (CVD) graphene growth via thermal decomposition of methane on Cu(110), including the formation of monodispersed carbon clusters at the initial stage, the graphene nucleation and the ripening of graphene islands to form continuous graphene film. Methane 194-201 sulfotransferase family 1A member 3 Homo sapiens 77-80 24651211-3 2014 Here, we report an in-situ low-temperature scanning tunneling microscopy (LT-STM) study of the elementary process of chemical vapor deposition (CVD) graphene growth via thermal decomposition of methane on Cu(110), including the formation of monodispersed carbon clusters at the initial stage, the graphene nucleation and the ripening of graphene islands to form continuous graphene film. Carbon 255-261 sulfotransferase family 1A member 3 Homo sapiens 77-80 24651211-3 2014 Here, we report an in-situ low-temperature scanning tunneling microscopy (LT-STM) study of the elementary process of chemical vapor deposition (CVD) graphene growth via thermal decomposition of methane on Cu(110), including the formation of monodispersed carbon clusters at the initial stage, the graphene nucleation and the ripening of graphene islands to form continuous graphene film. Graphite 297-305 sulfotransferase family 1A member 3 Homo sapiens 77-80 24651211-3 2014 Here, we report an in-situ low-temperature scanning tunneling microscopy (LT-STM) study of the elementary process of chemical vapor deposition (CVD) graphene growth via thermal decomposition of methane on Cu(110), including the formation of monodispersed carbon clusters at the initial stage, the graphene nucleation and the ripening of graphene islands to form continuous graphene film. Graphite 297-305 sulfotransferase family 1A member 3 Homo sapiens 77-80 24651211-3 2014 Here, we report an in-situ low-temperature scanning tunneling microscopy (LT-STM) study of the elementary process of chemical vapor deposition (CVD) graphene growth via thermal decomposition of methane on Cu(110), including the formation of monodispersed carbon clusters at the initial stage, the graphene nucleation and the ripening of graphene islands to form continuous graphene film. Graphite 297-305 sulfotransferase family 1A member 3 Homo sapiens 77-80 24651211-4 2014 STM measurement, supported by DFT calculations, suggests that the carbon clusters on the surface are C2H5. Carbon 66-72 sulfotransferase family 1A member 3 Homo sapiens 0-3 24651211-4 2014 STM measurement, supported by DFT calculations, suggests that the carbon clusters on the surface are C2H5. Ethyl radical 101-105 sulfotransferase family 1A member 3 Homo sapiens 0-3 24654926-2 2014 Combining high-resolution STM experiments and DFT calculations, we have unambiguously unveiled the atomic structure of the boundary between a graphene zigzag edge and a Pt(111) step. Graphite 142-150 sulfotransferase family 1A member 3 Homo sapiens 26-29 24443959-3 2014 Here, we utilize measurements of electronic density of states (DOS), using scanning tunneling microscopy/spectroscopy (STM/STS), to identify energy levels responsible for photocatalytic reduction of CO2-water in an artificial photosynthetic process. Carbon Dioxide 199-202 sulfotransferase family 1A member 3 Homo sapiens 119-122 24395081-1 2014 From the interplay of STM imaging and DFT calculations we have investigated the isomerization of an alkene molecule on Cu(110) under ultrahigh vacuum conditions. Alkenes 100-106 sulfotransferase family 1A member 3 Homo sapiens 22-25 24443959-3 2014 Here, we utilize measurements of electronic density of states (DOS), using scanning tunneling microscopy/spectroscopy (STM/STS), to identify energy levels responsible for photocatalytic reduction of CO2-water in an artificial photosynthetic process. Water 203-208 sulfotransferase family 1A member 3 Homo sapiens 119-122 24244344-6 2013 Pd-doped Cu wire exhibits larger time-to-failure and cycles-to-failure in both wearout reliability tests in Highly Accelerated Temperature and Humidity (HAST) and Temperature Cycling (TC) tests. Palladium 0-2 sulfotransferase family 1A member 3 Homo sapiens 153-157 24136195-3 2013 In primates but not lower order animals, a sulfotransferase (SULT1A3) is present that can rapidly metabolize dopamine to dopamine sulfate. Dopamine 109-117 sulfotransferase family 1A member 3 Homo sapiens 61-68 24136195-3 2013 In primates but not lower order animals, a sulfotransferase (SULT1A3) is present that can rapidly metabolize dopamine to dopamine sulfate. dopamine sulfate 121-137 sulfotransferase family 1A member 3 Homo sapiens 61-68 24136195-4 2013 Here, we show that SULT1A3 and a closely related protein SULT1A1 are highly inducible by dopamine. Dopamine 89-97 sulfotransferase family 1A member 3 Homo sapiens 19-26 24136195-7 2013 Pharmacological agents that inhibited induction or siRNA targeting SULT1A3 significantly increased the susceptibility of cells to dopamine toxicity. Dopamine 130-138 sulfotransferase family 1A member 3 Homo sapiens 67-74 24136195-8 2013 Taken together, these results show that dopamine can induce its own metabolism and protect neuron-like cells from damage, suggesting that SULT1A3 activity may be a risk factor for dopamine-dependent neurodegenerative diseases. Dopamine 40-48 sulfotransferase family 1A member 3 Homo sapiens 138-145 24136195-8 2013 Taken together, these results show that dopamine can induce its own metabolism and protect neuron-like cells from damage, suggesting that SULT1A3 activity may be a risk factor for dopamine-dependent neurodegenerative diseases. Dopamine 180-188 sulfotransferase family 1A member 3 Homo sapiens 138-145 24325337-8 2014 Simulations of the STM image of methionine assemblies were consistent with the experimental STM image. Methionine 32-42 sulfotransferase family 1A member 3 Homo sapiens 19-22 24325337-8 2014 Simulations of the STM image of methionine assemblies were consistent with the experimental STM image. Methionine 32-42 sulfotransferase family 1A member 3 Homo sapiens 92-95 25429512-3 2014 Of the twelve human SULTs analyzed, SULT1A3 displayed the strongest sulfating activity toward phenylephrine. Phenylephrine 94-107 sulfotransferase family 1A member 3 Homo sapiens 36-43 25429512-5 2014 Kinetic analysis revealed that SULT1A3- mediated sulfation of phenylephrine occurred in the same order of magnitude compared with that previously reported for SULT1A3-mediated sulfation of dopamine. Phenylephrine 62-75 sulfotransferase family 1A member 3 Homo sapiens 31-38 25429512-5 2014 Kinetic analysis revealed that SULT1A3- mediated sulfation of phenylephrine occurred in the same order of magnitude compared with that previously reported for SULT1A3-mediated sulfation of dopamine. Dopamine 189-197 sulfotransferase family 1A member 3 Homo sapiens 31-38 25429512-5 2014 Kinetic analysis revealed that SULT1A3- mediated sulfation of phenylephrine occurred in the same order of magnitude compared with that previously reported for SULT1A3-mediated sulfation of dopamine. Dopamine 189-197 sulfotransferase family 1A member 3 Homo sapiens 159-166 24367760-5 2013 In combination with recent density functional theory calculations, the sub-molecularly resolved STM images allow to clearly discriminate between the [BMP](+) cation and [TFSA](-) anion. 1-butyl-1-methylpyrrolidinium bis(trifluoromethylsulfonyl)imide 150-153 sulfotransferase family 1A member 3 Homo sapiens 96-99 24065072-4 2013 The reconstruction from topographic images of graphene bending energy maps sheds light on the local electro-mechanical response of graphene under STM imaging and unveils the role of the stress induced by the vicinity of the graphene-metal interface in the formation and the manipulation of these ripples. Graphite 46-54 sulfotransferase family 1A member 3 Homo sapiens 146-149 24065072-4 2013 The reconstruction from topographic images of graphene bending energy maps sheds light on the local electro-mechanical response of graphene under STM imaging and unveils the role of the stress induced by the vicinity of the graphene-metal interface in the formation and the manipulation of these ripples. Graphite 131-139 sulfotransferase family 1A member 3 Homo sapiens 146-149 24065072-4 2013 The reconstruction from topographic images of graphene bending energy maps sheds light on the local electro-mechanical response of graphene under STM imaging and unveils the role of the stress induced by the vicinity of the graphene-metal interface in the formation and the manipulation of these ripples. Graphite 131-139 sulfotransferase family 1A member 3 Homo sapiens 146-149 24244344-6 2013 Pd-doped Cu wire exhibits larger time-to-failure and cycles-to-failure in both wearout reliability tests in Highly Accelerated Temperature and Humidity (HAST) and Temperature Cycling (TC) tests. Copper 9-11 sulfotransferase family 1A member 3 Homo sapiens 153-157 24166292-3 2013 We address this issue via spatially resolved imaging and spectroscopic studies of the Sr2IrO4 surface using scanning tunneling microscopy/spectroscopy (STM/S). sr2iro4 86-93 sulfotransferase family 1A member 3 Homo sapiens 152-155 24237541-0 2013 Rotation of a single acetylene molecule on Cu(001) by tunneling electrons in STM. Acetylene 21-30 sulfotransferase family 1A member 3 Homo sapiens 77-80 24206512-0 2013 Identifying magnetic anisotropy of the topological surface state of Cr(0.05)Sb(1.95)Te(3) with spin-polarized STM. Chromium 68-70 sulfotransferase family 1A member 3 Homo sapiens 110-113 24162548-2 2013 Scanning tunneling microscopy imaging directly demonstrates that the orientation of individual fullerene with an adsorption geometry of 5-6 bond is rotated by integral times as 30 degree after a pulse bias is applied between the STM tip and the molecule. Fullerenes 95-104 sulfotransferase family 1A member 3 Homo sapiens 229-232 24206512-0 2013 Identifying magnetic anisotropy of the topological surface state of Cr(0.05)Sb(1.95)Te(3) with spin-polarized STM. Antimony 76-78 sulfotransferase family 1A member 3 Homo sapiens 110-113 23913196-2 2013 Au and Pd were sequentially deposited onto a gamma-Fe2O3 (0001) substrate in ultra high vacuum by metal vapour deposition and probed by LEIS and STM. Gold 0-2 sulfotransferase family 1A member 3 Homo sapiens 145-148 23999460-1 2013 Adsorption of tetrahydroxybenzene (THB) on Cu(111) and Au(111) surfaces is studied using a combination of STM, XPS, and DFT. 1,2,4,5-tetrahydroxybenzene 14-33 sulfotransferase family 1A member 3 Homo sapiens 106-109 23999460-1 2013 Adsorption of tetrahydroxybenzene (THB) on Cu(111) and Au(111) surfaces is studied using a combination of STM, XPS, and DFT. 1,2,4,5-tetrahydroxybenzene 35-38 sulfotransferase family 1A member 3 Homo sapiens 106-109 24003896-2 2013 Here, we demonstrate that spin states of Co-porphyrin on Au(111) can be reversibly switched over by binding and unbinding of the NO molecule and can be sensed using scanning tunneling microscopy and spectroscopy (STM and STS). co-porphyrin 41-53 sulfotransferase family 1A member 3 Homo sapiens 213-216 24003896-2 2013 Here, we demonstrate that spin states of Co-porphyrin on Au(111) can be reversibly switched over by binding and unbinding of the NO molecule and can be sensed using scanning tunneling microscopy and spectroscopy (STM and STS). Gold 57-59 sulfotransferase family 1A member 3 Homo sapiens 213-216 23913196-4 2013 At this stage, LEIS shows both metals to be present but heating the combined system to 573 K resulted in the loss of the Au signal in the LEIS and disappearance of the smaller particles from the STM images indicating the formation of Au@Pd core-shell structures. Gold 234-236 sulfotransferase family 1A member 3 Homo sapiens 195-198 23692665-4 2013 [Smerieri, M.; Vattuone, L.; Costa, D.; Tielens, F.; Savio, L. Self-Assembly of (S)-Glutamic Acid on Ag(100): A Combined LT-STM and Ab Initio Investigation. Glutamic Acid 80-97 sulfotransferase family 1A member 3 Homo sapiens 124-127 23883551-0 2013 Oxygen adsorption on the Al9Co2(001) surface: first-principles and STM study. Oxygen 0-6 sulfotransferase family 1A member 3 Homo sapiens 67-70 23883551-0 2013 Oxygen adsorption on the Al9Co2(001) surface: first-principles and STM study. al9co2 25-31 sulfotransferase family 1A member 3 Homo sapiens 67-70 23883551-1 2013 Atomic oxygen adsorption on a pure aluminum terminated Al9Co2(001) surface is studied by first-principle calculations coupled with STM measurements. Oxygen 7-13 sulfotransferase family 1A member 3 Homo sapiens 131-134 23883551-1 2013 Atomic oxygen adsorption on a pure aluminum terminated Al9Co2(001) surface is studied by first-principle calculations coupled with STM measurements. Aluminum 35-43 sulfotransferase family 1A member 3 Homo sapiens 131-134 23938843-4 2013 In this study, we advanced STM-CL technique by introducing a novel optical fiber probe with Cr thin film coating (Cr-FP), which was found to work as a STM probe, as an electron field-emitter for local carrier excitation, and as an alignment-free efficient local STM-CL collector which blinds luminescence after the minority carrier diffusion. Chromium 92-94 sulfotransferase family 1A member 3 Homo sapiens 27-30 23938843-4 2013 In this study, we advanced STM-CL technique by introducing a novel optical fiber probe with Cr thin film coating (Cr-FP), which was found to work as a STM probe, as an electron field-emitter for local carrier excitation, and as an alignment-free efficient local STM-CL collector which blinds luminescence after the minority carrier diffusion. Chromium 92-94 sulfotransferase family 1A member 3 Homo sapiens 151-154 23938843-4 2013 In this study, we advanced STM-CL technique by introducing a novel optical fiber probe with Cr thin film coating (Cr-FP), which was found to work as a STM probe, as an electron field-emitter for local carrier excitation, and as an alignment-free efficient local STM-CL collector which blinds luminescence after the minority carrier diffusion. Chromium 92-94 sulfotransferase family 1A member 3 Homo sapiens 151-154 23788363-8 2013 In situ STM shows that molecular scale structures of the size of Spd-stabilized ds-ONs are densely packed over the Au(111) surface in potential ranges around the capacitive peak potential. ds-ons 80-86 sulfotransferase family 1A member 3 Homo sapiens 8-11 23788363-8 2013 In situ STM shows that molecular scale structures of the size of Spd-stabilized ds-ONs are densely packed over the Au(111) surface in potential ranges around the capacitive peak potential. Gold 115-117 sulfotransferase family 1A member 3 Homo sapiens 8-11 23870088-8 2013 CONCLUSIONS: Collectively, our results demonstrate that P-STM is a useful tool for detecting Thr-19-phosphorylated lamin A/C in cells and reveal quantitative changes in the phosphorylation status of major lamin A/C phosphorylation sites during mitosis. Threonine 93-96 sulfotransferase family 1A member 3 Homo sapiens 58-61 23737128-2 2013 By combining the technique with DFT calculations, STM manipulation was extended to the probing of intermolecular hydrogen-bonding configurations in self-assembled nanostructures. Hydrogen 113-121 sulfotransferase family 1A member 3 Homo sapiens 50-53 23675983-3 2013 Here, we use in situ low-temperature scanning tunneling microscopy (LT-STM) to reveal the graphene growth intermediates at different stages via thermal decomposition of methane on Cu(111). Graphite 90-98 sulfotransferase family 1A member 3 Homo sapiens 71-74 23802977-1 2013 At low coverage of water on Cu(110), substrate-mediated electrostatics lead to zigzagging chains along [001] as observed with STM [T. Yamada, S. Tamamori, H. Okuyama, and T. Aruga, "Anisotropic water chain growth on Cu(110) observed with scanning tunneling microscopy" Phys. Water 19-24 sulfotransferase family 1A member 3 Homo sapiens 126-129 23802977-1 2013 At low coverage of water on Cu(110), substrate-mediated electrostatics lead to zigzagging chains along [001] as observed with STM [T. Yamada, S. Tamamori, H. Okuyama, and T. Aruga, "Anisotropic water chain growth on Cu(110) observed with scanning tunneling microscopy" Phys. Copper 28-30 sulfotransferase family 1A member 3 Homo sapiens 126-129 23802977-1 2013 At low coverage of water on Cu(110), substrate-mediated electrostatics lead to zigzagging chains along [001] as observed with STM [T. Yamada, S. Tamamori, H. Okuyama, and T. Aruga, "Anisotropic water chain growth on Cu(110) observed with scanning tunneling microscopy" Phys. Water 194-199 sulfotransferase family 1A member 3 Homo sapiens 126-129 23675983-3 2013 Here, we use in situ low-temperature scanning tunneling microscopy (LT-STM) to reveal the graphene growth intermediates at different stages via thermal decomposition of methane on Cu(111). Methane 169-176 sulfotransferase family 1A member 3 Homo sapiens 71-74 23675983-3 2013 Here, we use in situ low-temperature scanning tunneling microscopy (LT-STM) to reveal the graphene growth intermediates at different stages via thermal decomposition of methane on Cu(111). Copper 180-182 sulfotransferase family 1A member 3 Homo sapiens 71-74 23439967-1 2013 In this work, the structure of the tetraphenylporphyrin (H2TPP) monolayer grown on the oxygen passivated Cu(110)-(2 x 1)O surface has been investigated with LT-STM and elucidated by DFT-calculations. tetraphenylporphyrin 35-55 sulfotransferase family 1A member 3 Homo sapiens 160-163 23488728-4 2013 By positioning the tip of an STM above a nanoparticle, a double barrier tunnel junction (DBTJ) is created, and Coulomb blockade is demonstrated at 40 K. This is the first time Coulomb blockade is observed with an organic monolayer on oxide-free silicon. coulomb 111-118 sulfotransferase family 1A member 3 Homo sapiens 29-32 23488728-4 2013 By positioning the tip of an STM above a nanoparticle, a double barrier tunnel junction (DBTJ) is created, and Coulomb blockade is demonstrated at 40 K. This is the first time Coulomb blockade is observed with an organic monolayer on oxide-free silicon. Oxides 234-239 sulfotransferase family 1A member 3 Homo sapiens 29-32 23488728-4 2013 By positioning the tip of an STM above a nanoparticle, a double barrier tunnel junction (DBTJ) is created, and Coulomb blockade is demonstrated at 40 K. This is the first time Coulomb blockade is observed with an organic monolayer on oxide-free silicon. Silicon 245-252 sulfotransferase family 1A member 3 Homo sapiens 29-32 23450169-1 2013 We present a modification of the standard electron transport methodology based on the (non-equilibrium) Green"s function formalism to efficiently simulate STM-images. formalism 121-130 sulfotransferase family 1A member 3 Homo sapiens 155-158 23439967-1 2013 In this work, the structure of the tetraphenylporphyrin (H2TPP) monolayer grown on the oxygen passivated Cu(110)-(2 x 1)O surface has been investigated with LT-STM and elucidated by DFT-calculations. h2tpp 57-62 sulfotransferase family 1A member 3 Homo sapiens 160-163 23439967-3 2013 The STM images suggest alternating chirality for the molecules within one unit cell which is supported by DFT total energy calculations for monolayers on the Cu-O substrate. cu-o 158-162 sulfotransferase family 1A member 3 Homo sapiens 4-7 23340829-1 2013 The native copper adatoms get trapped in a self-assembled molecular nanostructure which is mainly formed by the intermolecular van der Waals interactions, and two dominating specific binding modes between the adatoms and the molecules are revealed at the atomic scale by high-resolution STM imaging. Copper 11-17 sulfotransferase family 1A member 3 Homo sapiens 287-290 23396479-1 2013 STM brings to light chirality aspects of the self-assembly of a functionalized helicene at the interface between a liquid and the solid substrates, gold and graphite. helicenes 79-87 sulfotransferase family 1A member 3 Homo sapiens 0-3 23396479-1 2013 STM brings to light chirality aspects of the self-assembly of a functionalized helicene at the interface between a liquid and the solid substrates, gold and graphite. Graphite 157-165 sulfotransferase family 1A member 3 Homo sapiens 0-3 23264958-0 2013 Isolated facial and meridional tris(bipyridine)Ru(II) for STM studies on Au(111). tris(bipyridine 31-46 sulfotransferase family 1A member 3 Homo sapiens 58-61 23073185-7 2013 In situ STM disclosed molecular scale features in varying coverage on addition of the metal ions. Metals 86-91 sulfotransferase family 1A member 3 Homo sapiens 8-11 23811605-2 2013 Scanning tunneling microscopy/spectroscopy (STM/S) corroborated by ab initio calculations, reveals the atomistic details of the molecular structure, and provides a clear signature of electronic and vibrational properties of the poly(phenylacetylene)s chains. poly(phenylacetylene) 228-249 sulfotransferase family 1A member 3 Homo sapiens 44-47 23236158-1 2012 We present direct visualization of pores formed by alamethicin (Alm) in a matrix of phospholipids using electrochemical scanning tunneling microscopy (EC-STM). Alamethicin 51-62 sulfotransferase family 1A member 3 Homo sapiens 154-157 23236158-1 2012 We present direct visualization of pores formed by alamethicin (Alm) in a matrix of phospholipids using electrochemical scanning tunneling microscopy (EC-STM). Alamethicin 64-67 sulfotransferase family 1A member 3 Homo sapiens 154-157 23236158-1 2012 We present direct visualization of pores formed by alamethicin (Alm) in a matrix of phospholipids using electrochemical scanning tunneling microscopy (EC-STM). Phospholipids 84-97 sulfotransferase family 1A member 3 Homo sapiens 154-157 23349902-8 2013 In children with UM, UA levels correlate with parasite density (r = 0.092, p = 0.043), sICAM-1 (r = 0.255, p<0.0001) and sTM (r = 0.175, p = 0.0001) levels. Uric Acid 21-23 sulfotransferase family 1A member 3 Homo sapiens 124-127 23349902-9 2013 After adjusting for parasite density, UA levels predict sTM levels. Uric Acid 38-40 sulfotransferase family 1A member 3 Homo sapiens 56-59 23018382-3 2012 Above the monolayer coverage (at which the oxide film has a lepidocrocite-like structure), STM images show the formation of multilayer islands with a distribution of heights. Oxides 43-48 sulfotransferase family 1A member 3 Homo sapiens 91-94 23126569-5 2012 Combined STM imaging and gap-mode Raman experiments provide structure evidence to support the formation of covalent Au-C contacts and further oligomerization. Gold 116-118 sulfotransferase family 1A member 3 Homo sapiens 9-12 22917559-7 2012 A two-stage enzymatic assay showed the sequential methylation and sulfation of dopamine, epinephrine, isoproterenol, and isoetharine mediated by, respectively, the COMT and the cytosolic sulfotransferase SULT1A3. Dopamine 79-87 sulfotransferase family 1A member 3 Homo sapiens 204-211 22917559-7 2012 A two-stage enzymatic assay showed the sequential methylation and sulfation of dopamine, epinephrine, isoproterenol, and isoetharine mediated by, respectively, the COMT and the cytosolic sulfotransferase SULT1A3. Epinephrine 89-100 sulfotransferase family 1A member 3 Homo sapiens 204-211 22917559-7 2012 A two-stage enzymatic assay showed the sequential methylation and sulfation of dopamine, epinephrine, isoproterenol, and isoetharine mediated by, respectively, the COMT and the cytosolic sulfotransferase SULT1A3. Isoproterenol 102-115 sulfotransferase family 1A member 3 Homo sapiens 204-211 22917559-7 2012 A two-stage enzymatic assay showed the sequential methylation and sulfation of dopamine, epinephrine, isoproterenol, and isoetharine mediated by, respectively, the COMT and the cytosolic sulfotransferase SULT1A3. Isoetharine 121-132 sulfotransferase family 1A member 3 Homo sapiens 204-211 22751488-4 2012 Upon increasing the potential again, a second c(4 x 4) phase with a different appearance in the STM images forms, which is attributed to partial dealloying, involving desorption of Pb from energetically less favorable sites. Lead 181-183 sulfotransferase family 1A member 3 Homo sapiens 96-99 22958159-1 2012 The electronic properties of alkanethiol self-assembled monolayers (alkanethiolate SAMs) associated with their molecular-scale geometry are investigated using scanning tunneling microscopy and spectroscopy (STM/STS). alkanethiol 29-40 sulfotransferase family 1A member 3 Homo sapiens 207-210 22958159-1 2012 The electronic properties of alkanethiol self-assembled monolayers (alkanethiolate SAMs) associated with their molecular-scale geometry are investigated using scanning tunneling microscopy and spectroscopy (STM/STS). alkanethiolate 68-82 sulfotransferase family 1A member 3 Homo sapiens 207-210 22865591-1 2012 Bromine atom transfer to a silicon surface as a function of physisorbed adsorbate alignment (see picture: left, vertical 1-bromopentane; right, horizontal 1-bromopentane) of 1-bromopropane and 1-bromopentane on Si(111)-7x7 has been studied by STM. Bromine 0-7 sulfotransferase family 1A member 3 Homo sapiens 243-246 22865591-1 2012 Bromine atom transfer to a silicon surface as a function of physisorbed adsorbate alignment (see picture: left, vertical 1-bromopentane; right, horizontal 1-bromopentane) of 1-bromopropane and 1-bromopentane on Si(111)-7x7 has been studied by STM. Silicon 27-34 sulfotransferase family 1A member 3 Homo sapiens 243-246 22865591-1 2012 Bromine atom transfer to a silicon surface as a function of physisorbed adsorbate alignment (see picture: left, vertical 1-bromopentane; right, horizontal 1-bromopentane) of 1-bromopropane and 1-bromopentane on Si(111)-7x7 has been studied by STM. 1-bromopropane 174-188 sulfotransferase family 1A member 3 Homo sapiens 243-246 23016599-8 2012 We also investigate electronic tunnel transport through oligothiophene islands with the STM. oligothiophene 56-70 sulfotransferase family 1A member 3 Homo sapiens 88-91 22954335-0 2012 In situ STM investigation of aromatic poly(azomethine) arrays constructed by "on-site" equilibrium polymerization. aromatic poly(azomethine) 29-54 sulfotransferase family 1A member 3 Homo sapiens 8-11 22847275-1 2012 This combined experimental (STM, XPS) and molecular dynamics simulation study highlights the complex and subtle interplay of solvent effects and surface interactions on the 2-D self-assembly pattern of a Schiff-base macrocycle containing catechol moieties at the liquid-solid interface. Schiff Bases 204-215 sulfotransferase family 1A member 3 Homo sapiens 28-31 22847275-1 2012 This combined experimental (STM, XPS) and molecular dynamics simulation study highlights the complex and subtle interplay of solvent effects and surface interactions on the 2-D self-assembly pattern of a Schiff-base macrocycle containing catechol moieties at the liquid-solid interface. catechol 238-246 sulfotransferase family 1A member 3 Homo sapiens 28-31 22847275-2 2012 STM imaging reveals a hexagonal ordering of the macrocycles at the n-tetradecane/Au(111) interface, compatible with a desorption of the lateral chains of the macrocycle. n-tetradecane 67-80 sulfotransferase family 1A member 3 Homo sapiens 0-3 22847275-2 2012 STM imaging reveals a hexagonal ordering of the macrocycles at the n-tetradecane/Au(111) interface, compatible with a desorption of the lateral chains of the macrocycle. Gold 81-83 sulfotransferase family 1A member 3 Homo sapiens 0-3 22763752-4 2012 A systematic analysis using 11 purified human SULTs revealed SULT1A3 as the major SULT responsible for the sulfation of ractopamine and salbutamol. ractopamine 120-131 sulfotransferase family 1A member 3 Homo sapiens 61-68 22763752-4 2012 A systematic analysis using 11 purified human SULTs revealed SULT1A3 as the major SULT responsible for the sulfation of ractopamine and salbutamol. Albuterol 136-146 sulfotransferase family 1A member 3 Homo sapiens 61-68 22763752-6 2012 Moreover, the inhibitory effects of ractopamine and salbutamol on SULT1A3-mediated dopamine sulfation were investigated. ractopamine 36-47 sulfotransferase family 1A member 3 Homo sapiens 66-73 22763752-6 2012 Moreover, the inhibitory effects of ractopamine and salbutamol on SULT1A3-mediated dopamine sulfation were investigated. Albuterol 52-62 sulfotransferase family 1A member 3 Homo sapiens 66-73 22763752-6 2012 Moreover, the inhibitory effects of ractopamine and salbutamol on SULT1A3-mediated dopamine sulfation were investigated. Dopamine 83-91 sulfotransferase family 1A member 3 Homo sapiens 66-73 22763752-9 2012 Collectively, these results imply that the sulfation mediated by SULT1A3 may play an important role in the metabolism and detoxification of ractopamine and salbutamol. ractopamine 140-151 sulfotransferase family 1A member 3 Homo sapiens 65-72 22763752-9 2012 Collectively, these results imply that the sulfation mediated by SULT1A3 may play an important role in the metabolism and detoxification of ractopamine and salbutamol. Albuterol 156-166 sulfotransferase family 1A member 3 Homo sapiens 65-72 22710438-7 2012 Besides the ability in studying the assembling structures at the interfaces, STM also provides a reasonable way to evaluate the distribution of the molecular weight of conjugated polymers by statistic of the contour length of the adsorbed polymer chains. Polymers 179-187 sulfotransferase family 1A member 3 Homo sapiens 77-80 22765649-4 2012 Our combined scanning tunneling microscopy/spectroscopy (STM/STS) and first-principles computational modeling study reveals site-selective positioning of C(60) molecules on Ce(TPP)(2) porphyrin double-decker arrays with the fullerene centered on the pi-system of the top bowl-shaped tetrapyrrole macrocycle. ce(tpp)(2) porphyrin 173-193 sulfotransferase family 1A member 3 Homo sapiens 57-60 22706791-0 2012 Synthesis and STM imaging of symmetric and dissymmetric ethynyl-bridged dimers of boron-subphthalocyanine bowl-shaped nanowheels. 4-ethynylbiphenyl 56-63 sulfotransferase family 1A member 3 Homo sapiens 14-17 22735164-5 2012 At variance the classical Bernal stacking manifests the strongest interlayer coupling by destroying the Dirac point and exhibiting a graphite-like STM appearance. Graphite 133-141 sulfotransferase family 1A member 3 Homo sapiens 147-150 22706791-0 2012 Synthesis and STM imaging of symmetric and dissymmetric ethynyl-bridged dimers of boron-subphthalocyanine bowl-shaped nanowheels. boron-subphthalocyanine 82-105 sulfotransferase family 1A member 3 Homo sapiens 14-17 22564759-7 2012 UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively. 4-hydroxy-3-methoxyethylamphetamine 59-63 sulfotransferase family 1A member 3 Homo sapiens 80-87 22564759-7 2012 UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively. 3,4-dihydroxyethylamphetamine 132-136 sulfotransferase family 1A member 3 Homo sapiens 80-87 22564759-7 2012 UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively. 4-hydroxy-3-methoxyethylamphetamine 59-63 sulfotransferase family 1A member 3 Homo sapiens 92-99 22564759-7 2012 UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively. 3,4-dihydroxyethylamphetamine 132-136 sulfotransferase family 1A member 3 Homo sapiens 92-99 22564759-7 2012 UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively. 4-hydroxy-3-methoxyethylamphetamine 141-145 sulfotransferase family 1A member 3 Homo sapiens 80-87 22676369-0 2012 Electrodeposition of copper on a Pt(111) electrode in sulfuric acid containing poly(ethylene glycol) and chloride ions as probed by in situ STM. Copper 21-27 sulfotransferase family 1A member 3 Homo sapiens 140-143 22564759-7 2012 UGT2B7, 2B15, and 2B17 were involved in glucuronidation of HMEA and SULT1A1 and SULT1A3 and SULT1A3 and SULT1E1 in the sulfation of DHEA and HMEA, respectively. 4-hydroxy-3-methoxyethylamphetamine 141-145 sulfotransferase family 1A member 3 Homo sapiens 92-99 22676369-0 2012 Electrodeposition of copper on a Pt(111) electrode in sulfuric acid containing poly(ethylene glycol) and chloride ions as probed by in situ STM. Polyethylene Glycols 79-100 sulfotransferase family 1A member 3 Homo sapiens 140-143 22676369-0 2012 Electrodeposition of copper on a Pt(111) electrode in sulfuric acid containing poly(ethylene glycol) and chloride ions as probed by in situ STM. Chlorides 105-113 sulfotransferase family 1A member 3 Homo sapiens 140-143 22676369-1 2012 This study employed real-time in situ STM imaging to examine the adsorption of PEG molecules on Pt(111) modified by a monolayer of copper adatoms and the subsequent bulk Cu deposition in 1 M H(2)SO(4) + 1 mM CuSO(4)+ 1 mM KCl + 88 muM PEG. Polyethylene Glycols 79-82 sulfotransferase family 1A member 3 Homo sapiens 38-41 22676369-10 2012 This STM study provided atomic- or molecular-level insight into the effect of PEG additives on the deposition of Cu. Polyethylene Glycols 78-81 sulfotransferase family 1A member 3 Homo sapiens 5-8 22728400-0 2012 Molecular orbital imaging of cobalt phthalocyanine on native oxidized copper layers using STM. cobalt phthalocyanine 29-50 sulfotransferase family 1A member 3 Homo sapiens 90-93 22946908-6 2012 A systematic analysis using eleven known human SULTs revealed SULT1A3 and SULT2A1 as the major responsible SULTs for the sulfation of, respectively, pentazocine and buprenorphine; whereas three other SULTs, SULT1A1, SULT1A2, and SULT1C4, were capable of sulfating naloxone. Pentazocine 149-160 sulfotransferase family 1A member 3 Homo sapiens 62-69 22612064-5 2012 However, at greater electron energies, we are able to locally manipulate the water using the STM tip. Water 77-82 sulfotransferase family 1A member 3 Homo sapiens 93-96 22946908-6 2012 A systematic analysis using eleven known human SULTs revealed SULT1A3 and SULT2A1 as the major responsible SULTs for the sulfation of, respectively, pentazocine and buprenorphine; whereas three other SULTs, SULT1A1, SULT1A2, and SULT1C4, were capable of sulfating naloxone. Buprenorphine 165-178 sulfotransferase family 1A member 3 Homo sapiens 62-69 22345052-5 2012 A linear molecular assembly of the octyloxy compound at a liquid/graphite interface was observed by STM measurements. Graphite 65-73 sulfotransferase family 1A member 3 Homo sapiens 100-103 22495597-1 2012 Suspended graphene has been studied by STM for the first time. Graphite 10-18 sulfotransferase family 1A member 3 Homo sapiens 39-42 22458813-1 2012 In this study, we selectively enhanced two types of adsorption of 3-mercaptoisobutyric acid on a Ge(100) surface by using the tunneling electrons from an STM and the catalytic effect of an STM tip. 3-mercapto-2-methylpropionic acid 66-91 sulfotransferase family 1A member 3 Homo sapiens 154-157 22680886-5 2012 Simulated STM images of gold atoms trapped in the pores of the Melamine network predict that the atoms should appear as bright spots inside Melamine hexagons. melamine 63-71 sulfotransferase family 1A member 3 Homo sapiens 10-13 22680886-5 2012 Simulated STM images of gold atoms trapped in the pores of the Melamine network predict that the atoms should appear as bright spots inside Melamine hexagons. melamine 140-148 sulfotransferase family 1A member 3 Homo sapiens 10-13 22680886-7 2012 These predictions have been supported by preliminary STM experiments which show bright spots inside Melamine hexagons at low Melamine coverages, while empty pores are mostly observed at large coverages. melamine 100-108 sulfotransferase family 1A member 3 Homo sapiens 53-56 22458813-1 2012 In this study, we selectively enhanced two types of adsorption of 3-mercaptoisobutyric acid on a Ge(100) surface by using the tunneling electrons from an STM and the catalytic effect of an STM tip. 3-mercapto-2-methylpropionic acid 66-91 sulfotransferase family 1A member 3 Homo sapiens 189-192 22458813-5 2012 In addition, via the use of a tungsten STM tip coated with a tungsten oxide (WO(3)) layer, we selectively catalyzed the adsorption through the thiol group. tungsten oxide 61-75 sulfotransferase family 1A member 3 Homo sapiens 39-42 22458813-5 2012 In addition, via the use of a tungsten STM tip coated with a tungsten oxide (WO(3)) layer, we selectively catalyzed the adsorption through the thiol group. wo(3)) 77-83 sulfotransferase family 1A member 3 Homo sapiens 39-42 22458813-5 2012 In addition, via the use of a tungsten STM tip coated with a tungsten oxide (WO(3)) layer, we selectively catalyzed the adsorption through the thiol group. Sulfhydryl Compounds 143-148 sulfotransferase family 1A member 3 Homo sapiens 39-42 22300373-0 2012 Formation of nanometer-sized surface platinum oxide clusters on a stepped Pt(557) single crystal surface induced by oxygen: a high-pressure STM and ambient-pressure XPS study. platinum oxide 37-51 sulfotransferase family 1A member 3 Homo sapiens 140-143 22352375-0 2012 SULT1A3-mediated regiospecific 7-O-sulfation of flavonoids in Caco-2 cells can be explained by the relevant molecular docking studies. Flavonoids 48-58 sulfotransferase family 1A member 3 Homo sapiens 0-7 22352375-8 2012 In conclusion, molecular docking studies explain why SULT1A3 exclusively mediates sulfonation at the 7-OH position of flavones/flavonols, and correlation studies indicate that SULT1A3 is the main isoform responsible for flavonoid sulfonation in the Caco-2 cells. Flavones 118-126 sulfotransferase family 1A member 3 Homo sapiens 53-60 22352375-8 2012 In conclusion, molecular docking studies explain why SULT1A3 exclusively mediates sulfonation at the 7-OH position of flavones/flavonols, and correlation studies indicate that SULT1A3 is the main isoform responsible for flavonoid sulfonation in the Caco-2 cells. Flavones 118-126 sulfotransferase family 1A member 3 Homo sapiens 176-183 22352375-8 2012 In conclusion, molecular docking studies explain why SULT1A3 exclusively mediates sulfonation at the 7-OH position of flavones/flavonols, and correlation studies indicate that SULT1A3 is the main isoform responsible for flavonoid sulfonation in the Caco-2 cells. Flavonols 127-136 sulfotransferase family 1A member 3 Homo sapiens 53-60 22352375-8 2012 In conclusion, molecular docking studies explain why SULT1A3 exclusively mediates sulfonation at the 7-OH position of flavones/flavonols, and correlation studies indicate that SULT1A3 is the main isoform responsible for flavonoid sulfonation in the Caco-2 cells. Flavonols 127-136 sulfotransferase family 1A member 3 Homo sapiens 176-183 22352375-8 2012 In conclusion, molecular docking studies explain why SULT1A3 exclusively mediates sulfonation at the 7-OH position of flavones/flavonols, and correlation studies indicate that SULT1A3 is the main isoform responsible for flavonoid sulfonation in the Caco-2 cells. Flavonoids 220-229 sulfotransferase family 1A member 3 Homo sapiens 53-60 22352375-8 2012 In conclusion, molecular docking studies explain why SULT1A3 exclusively mediates sulfonation at the 7-OH position of flavones/flavonols, and correlation studies indicate that SULT1A3 is the main isoform responsible for flavonoid sulfonation in the Caco-2 cells. Flavonoids 220-229 sulfotransferase family 1A member 3 Homo sapiens 176-183 22310968-0 2012 Synthesis, magnetic properties, and STM spectroscopy of an unprecedented octanuclear chloro-bridged nickel(II) double cubane. nickel(ii) double cubane 100-124 sulfotransferase family 1A member 3 Homo sapiens 36-39 22300373-1 2012 We studied the oxygen-induced restructuring process on a stepped Pt(557) single crystal surface using high-pressure scanning tunneling microscopy (HP-STM) and ambient-pressure X-ray photoelectron spectroscopy (AP-XPS) at O(2) pressures up to 1 Torr. Oxygen 15-21 sulfotransferase family 1A member 3 Homo sapiens 150-153 22300373-2 2012 HP-STM has revealed that nanometer-sized clusters are created on Pt(557) at 1 Torr of O(2) and at room temperature. Oxygen 86-90 sulfotransferase family 1A member 3 Homo sapiens 3-6 22218732-1 2012 We present STM data that show that it is possible to use a metal induced 2 x 7 reconstruction of Si(001) to narrow the width distribution of Dy silicide nanowires. Metals 59-64 sulfotransferase family 1A member 3 Homo sapiens 11-14 22274993-2 2012 The STM topography data reveal that Pb adatoms form a similar superstructure to that observed in the case of Si adatoms on a bare Si(111)5 x 2-Au surface. Lead 36-38 sulfotransferase family 1A member 3 Homo sapiens 4-7 22274993-4 2012 Bias dependent STM topography and spectroscopy together with the DFT calculations allow us to distinguish Pb from Si adatoms. Lead 106-108 sulfotransferase family 1A member 3 Homo sapiens 15-18 22290796-1 2012 The large tendency of catechol rings to adsorb on surfaces has been studied by STM experiments with molecular resolution combined with molecular-dynamics simulations. catechol 22-30 sulfotransferase family 1A member 3 Homo sapiens 79-82 22218732-1 2012 We present STM data that show that it is possible to use a metal induced 2 x 7 reconstruction of Si(001) to narrow the width distribution of Dy silicide nanowires. Silicon 97-99 sulfotransferase family 1A member 3 Homo sapiens 11-14 22218732-1 2012 We present STM data that show that it is possible to use a metal induced 2 x 7 reconstruction of Si(001) to narrow the width distribution of Dy silicide nanowires. silicide 144-152 sulfotransferase family 1A member 3 Homo sapiens 11-14 23207770-4 2012 A systematic analysis revealed four ethanol-sulfating SULTs, SULT1A1, SULT1A2, SULT1A3, and SULT1C4, among the eleven human SULT enzymes previously prepared and purified. Ethanol 36-43 sulfotransferase family 1A member 3 Homo sapiens 79-86 22088136-2 2012 Successful STM imaging of the molecules adsorbed on a gold surface indicated that one thiol group controls the orientation of the molecule and that the protein maintains its native form under the experimental conditions. Sulfhydryl Compounds 86-91 sulfotransferase family 1A member 3 Homo sapiens 11-14 22088136-3 2012 Stable protein-gold STM tip electrical contact was directly observed to form via the second free thiol group in current-voltage and current-distance measurements. Sulfhydryl Compounds 97-102 sulfotransferase family 1A member 3 Homo sapiens 20-23 21989950-9 2012 Direct sulfation of brivanib was catalyzed by multiple SULT enzymes, including SULT1A1, SULT1B1, SULT2A1, SULT1A3, and SULT1E1. brivanib 20-28 sulfotransferase family 1A member 3 Homo sapiens 106-113 22546188-0 2012 Modifying the STM tip for the " ultimate " imaging of the Si(111)-7x7 surface and metal-supported molecules. Silicon 58-60 sulfotransferase family 1A member 3 Homo sapiens 14-17 22546188-0 2012 Modifying the STM tip for the " ultimate " imaging of the Si(111)-7x7 surface and metal-supported molecules. Metals 82-87 sulfotransferase family 1A member 3 Homo sapiens 14-17 22837666-1 2012 Surface self-assembly process of 9-anthracene carboxylic acid (AnCA) on Ag(111) was investigated using STM. 9-anthroic acid 33-61 sulfotransferase family 1A member 3 Homo sapiens 103-106 21825114-9 2012 Human SULT1A1, SULT1A2 and SULT1A3 as well as murine Sult1a1 and Sult1d1 also activated some hydroxymethyl-substituted furans to varying degrees. hydroxymethyl-substituted furans 93-125 sulfotransferase family 1A member 3 Homo sapiens 27-34 22299981-2 2012 Here, we describe the etching of gold STM probes suitable for chemical functionalization with moieties bearing thiol groups. Sulfhydryl Compounds 111-116 sulfotransferase family 1A member 3 Homo sapiens 38-41 23155482-4 2012 Three types of silicene superstructures on Ag(111) surface have been considered and the simulated STM images are compared with experimental observations. silicene 15-23 sulfotransferase family 1A member 3 Homo sapiens 98-101 22905317-4 2012 Scanning tunneling microscopy and spectroscopy (STM and STS) of NG revealed the presence of localized states in the conduction band induced by N(2)(AA)-doping, which was confirmed by ab initio calculations. Nitrogen 143-147 sulfotransferase family 1A member 3 Homo sapiens 48-51 22005757-0 2011 Epitaxial growth of diindenoperylene ultrathin films on Ag(111) investigated by LT-STM and LEED. diindenoperylene 20-36 sulfotransferase family 1A member 3 Homo sapiens 83-86 21795466-5 2011 SULT1A1 and SULT1A3 catalyzed sulfation of DHMA, and SULT1A3 and SULT1E1 catalyzed sulfation of HMMA. alpha-methylepinine 43-47 sulfotransferase family 1A member 3 Homo sapiens 12-19 22111691-1 2011 Self-assembled monolayers of a water-insoluble porphyrin, tetraphenyl porphyrin (TPP), in the presence of an aqueous electrolyte were characterized in situ with electrochemical scanning tunneling microscopy (EC-STM) at working electrode potentials of between 0.5 and -0.2 V. Isolated domains of TPP monolayers with differing orientation were observed on Au(111) in 0.1 M HClO(4) over this entire potential window. tetraphenylporphyrin 58-79 sulfotransferase family 1A member 3 Homo sapiens 211-214 21933112-6 2011 In particular, the structural basis for regioselective metabolism of flavonoids by SULT1A3 and UGT1A1 is discussed. Flavonoids 69-79 sulfotransferase family 1A member 3 Homo sapiens 83-90 21955062-0 2011 Faradaic phase transition of dibenzyl viologen on an HOPG electrode surface studied by in situ electrochemical STM and electroreflectance spectroscopy. dibenzyl viologen 29-46 sulfotransferase family 1A member 3 Homo sapiens 111-114 21955062-1 2011 Phase transitions of an adsorption layer of dibenzyl viologen (dBV) as a typical diaryl viologen on a basal plane of a highly oriented pyrolytic graphite (HOPG) electrode are described using voltammetry, in situ electrochemical scanning tunneling microscopy (EC-STM), and electroreflectance (ER) spectroscopy. dibenzyl viologen 44-61 sulfotransferase family 1A member 3 Homo sapiens 262-265 21955062-1 2011 Phase transitions of an adsorption layer of dibenzyl viologen (dBV) as a typical diaryl viologen on a basal plane of a highly oriented pyrolytic graphite (HOPG) electrode are described using voltammetry, in situ electrochemical scanning tunneling microscopy (EC-STM), and electroreflectance (ER) spectroscopy. Buformin 63-66 sulfotransferase family 1A member 3 Homo sapiens 262-265 21955062-5 2011 In situ EC-STM images of the 2D condensed monolayer demonstrated stripe patterns of the rows of dBV( +) molecules forming 3-fold rotationally symmetric domains. dbv( +) 96-103 sulfotransferase family 1A member 3 Homo sapiens 11-14 21795466-8 2011 Marked enantioselectivity could be observed for S-DHMA sulfation by SULT1A3 and in human liver cytosol, whereas no differences were observed for HMMA sulfation. alpha-methylepinine 50-54 sulfotransferase family 1A member 3 Homo sapiens 68-75 21913288-1 2011 Birds of a feather flock together: STM and DFT studies provide the first example of spontaneous chiral resolution of a helicene on a surface. helicenes 119-127 sulfotransferase family 1A member 3 Homo sapiens 35-38 22107674-0 2011 Giant alkali-metal-induced lattice relaxation as the driving force of the insulating phase of alkali-metal/Si(111):B. Ab initio density-functional theory calculations, photoemission spectroscopy (PES), scanning tunneling microscopy, and spectroscopy (STM, STS) have been used to solve the 2sqrt[3]x2sqrt[3]R30 surface reconstruction observed previously by LEED on 0.5 ML K/Si:B. Metals 13-18 sulfotransferase family 1A member 3 Homo sapiens 251-254 21879758-3 2011 On the 7x7 reconstruction of the Si(111) surface, charge transport through the surface has been demonstrated by others using charge injection by STM tips. Silicon 33-35 sulfotransferase family 1A member 3 Homo sapiens 145-148 21869953-1 2011 First generation poly(triazole-phenylene) dendrimers equipped with peripheral alkyl or carboxylic acid groups to engage in van der Waals and hydrogen-bonding interactions, respectively, assemble into distinct two-dimensional nano-structures at the solid-liquid interface as revealed by high resolution STM investigations. poly(triazole-phenylene) 17-41 sulfotransferase family 1A member 3 Homo sapiens 302-305 21845278-1 2011 STM imaging following the adsorption of (S)-lysine on Au{111} leads to the observation of Au nanofingers whose growth directions correlate with the unit cell vectors of ordered 2-D phases of lysine. Lysine 40-50 sulfotransferase family 1A member 3 Homo sapiens 0-3 21820498-0 2011 Clioquinol is sulfated by human jejunum cytosol and SULT1A3, a human-specific dopamine sulfotransferase. Clioquinol 0-10 sulfotransferase family 1A member 3 Homo sapiens 52-59 21820498-6 2011 We found that sulfating activities of human jejunal cytosols to clioquinol were well correlated with those to dopamine, a typical SULT1A3 substrate. Dopamine 110-118 sulfotransferase family 1A member 3 Homo sapiens 130-137 21820498-7 2011 Consistently, recombinant SULT1A3 showed the highest activity to clioquinol in vitro among the human SULTs examined. Clioquinol 65-75 sulfotransferase family 1A member 3 Homo sapiens 26-33 21820498-8 2011 The S(50) value for the clioquinol sulfation by SULT1A3 was similar to the K(m) value for that by cytosols from human jejunum, where SULT1A3 is abundantly expressed. Clioquinol 24-34 sulfotransferase family 1A member 3 Homo sapiens 48-55 21820498-8 2011 The S(50) value for the clioquinol sulfation by SULT1A3 was similar to the K(m) value for that by cytosols from human jejunum, where SULT1A3 is abundantly expressed. Clioquinol 24-34 sulfotransferase family 1A member 3 Homo sapiens 133-140 21820498-9 2011 Moreover, clioquinol inhibited both human jejunal cytosol- and SULT1A3-mediated sulfations of dopamine in a dose-dependent manner, showing similar IC(50) values. Clioquinol 10-20 sulfotransferase family 1A member 3 Homo sapiens 63-70 21820498-9 2011 Moreover, clioquinol inhibited both human jejunal cytosol- and SULT1A3-mediated sulfations of dopamine in a dose-dependent manner, showing similar IC(50) values. Dopamine 94-102 sulfotransferase family 1A member 3 Homo sapiens 63-70 21820498-10 2011 These results suggest that SULT1A3, which is highly expressed in intestine but not in liver, is responsible for the clioquinol sulfation in humans, raising a possibility that orally administered clioquinol might inhibit dopamine sulfation in human intestines. Clioquinol 116-126 sulfotransferase family 1A member 3 Homo sapiens 27-34 21820498-10 2011 These results suggest that SULT1A3, which is highly expressed in intestine but not in liver, is responsible for the clioquinol sulfation in humans, raising a possibility that orally administered clioquinol might inhibit dopamine sulfation in human intestines. Clioquinol 195-205 sulfotransferase family 1A member 3 Homo sapiens 27-34 21820498-10 2011 These results suggest that SULT1A3, which is highly expressed in intestine but not in liver, is responsible for the clioquinol sulfation in humans, raising a possibility that orally administered clioquinol might inhibit dopamine sulfation in human intestines. Dopamine 220-228 sulfotransferase family 1A member 3 Homo sapiens 27-34 21845278-1 2011 STM imaging following the adsorption of (S)-lysine on Au{111} leads to the observation of Au nanofingers whose growth directions correlate with the unit cell vectors of ordered 2-D phases of lysine. Gold 54-56 sulfotransferase family 1A member 3 Homo sapiens 0-3 21845278-1 2011 STM imaging following the adsorption of (S)-lysine on Au{111} leads to the observation of Au nanofingers whose growth directions correlate with the unit cell vectors of ordered 2-D phases of lysine. Gold 90-92 sulfotransferase family 1A member 3 Homo sapiens 0-3 21507465-3 2011 MATERIALS AND METHODS: Using a functional assay which quantifies the activity of sTM activity (TMa), we performed a pilot study to analyze the ratio TMa/TM:Ag in a control group of 25 healthy children, 8 children with autologous and 16 children with allogeneic BMT. 4,4-dimethylcholesta-8,14-dien-3-ol 95-98 sulfotransferase family 1A member 3 Homo sapiens 81-84 21845278-1 2011 STM imaging following the adsorption of (S)-lysine on Au{111} leads to the observation of Au nanofingers whose growth directions correlate with the unit cell vectors of ordered 2-D phases of lysine. Lysine 44-50 sulfotransferase family 1A member 3 Homo sapiens 0-3 21809833-1 2011 We show, by complementary spectroscopic and STM analysis, that Cr(7)Ni derivatives are suitable to be sublimed in UHV conditions. cr(7)ni 63-70 sulfotransferase family 1A member 3 Homo sapiens 44-47 21796276-1 2011 High-resolution STM imaging of the structures formed by carbamazepine molecules adsorbed onto a pseudo-ordered carbamazepine monolayer on Au(111) shows the formation of previously unreported 1-dimensional supramolecular assemblies. Carbamazepine 56-69 sulfotransferase family 1A member 3 Homo sapiens 16-19 21796276-1 2011 High-resolution STM imaging of the structures formed by carbamazepine molecules adsorbed onto a pseudo-ordered carbamazepine monolayer on Au(111) shows the formation of previously unreported 1-dimensional supramolecular assemblies. Carbamazepine 111-124 sulfotransferase family 1A member 3 Homo sapiens 16-19 21811734-0 2011 A general model of metal underpotential deposition in the presence of thiol-based additives based on an in situ STM study. Metals 19-24 sulfotransferase family 1A member 3 Homo sapiens 112-115 21811734-0 2011 A general model of metal underpotential deposition in the presence of thiol-based additives based on an in situ STM study. Sulfhydryl Compounds 70-75 sulfotransferase family 1A member 3 Homo sapiens 112-115 21507465-3 2011 MATERIALS AND METHODS: Using a functional assay which quantifies the activity of sTM activity (TMa), we performed a pilot study to analyze the ratio TMa/TM:Ag in a control group of 25 healthy children, 8 children with autologous and 16 children with allogeneic BMT. 4,4-dimethylcholesta-8,14-dien-3-ol 149-152 sulfotransferase family 1A member 3 Homo sapiens 81-84 21565261-2 2011 With alpha-cyclodextrin, this conjugate forms a polypseudorotaxane, which was characterised by means of (1)H NMR spectra, powder X-ray diffraction patterns and STM microscopy. alpha-cyclodextrin 5-23 sulfotransferase family 1A member 3 Homo sapiens 160-163 21749063-5 2011 With a view on first-principle insight into the in situ STM behavior of robust redox (as opposed to nonredox) molecules, we present in this report a density functional theory (DFT) study of the complexes in both free and adsorbate state, in either state exposed to both stoichiometric counterions and a large assembly of solvent water molecules. Water 329-334 sulfotransferase family 1A member 3 Homo sapiens 56-59 21565261-2 2011 With alpha-cyclodextrin, this conjugate forms a polypseudorotaxane, which was characterised by means of (1)H NMR spectra, powder X-ray diffraction patterns and STM microscopy. polypseudorotaxane 48-66 sulfotransferase family 1A member 3 Homo sapiens 160-163 21717545-0 2011 A nanosized molybdenum oxide wheel with a unique electronic-necklace structure: STM study with submolecular resolution. molybdenum trioxide 12-28 sulfotransferase family 1A member 3 Homo sapiens 80-83 21687894-1 2011 The ZnO(0001)-Zn terminated crystal face was studied after reduction at high temperatures by combination of STM, STS, XPS and TDS. Zinc Oxide 4-7 sulfotransferase family 1A member 3 Homo sapiens 108-111 21687894-1 2011 The ZnO(0001)-Zn terminated crystal face was studied after reduction at high temperatures by combination of STM, STS, XPS and TDS. Zinc 4-6 sulfotransferase family 1A member 3 Homo sapiens 108-111 21675741-1 2011 STM images of multidomain epitaxial graphene on Pt(111) have been combined with a geometrical model to investigate the origin of the coincidence Moire superstructures. Graphite 36-44 sulfotransferase family 1A member 3 Homo sapiens 0-3 21594266-1 2011 The electrochemical interface of Au(100) and 1-butyl-3-methyl-imidazolium hexafluorophosphate has been characterized by cyclic voltammetry, electrochemical impedance spectroscopy and in situ STM, especially in two distinct potential ranges. Gold 33-35 sulfotransferase family 1A member 3 Homo sapiens 191-194 21504173-3 2011 The data reflects a well-defined surface structure that maintains proton order even at surprisingly high temperatures of 140 K. The diffraction data we measure is consistent with a structure recently derived from STM measurements performed at 6 K. Comparison with recent DFT calculation is in partial agreement, suggesting that these calculations might be underestimating the contribution of relative water molecule orientations to the binding energy. Water 401-406 sulfotransferase family 1A member 3 Homo sapiens 213-216 21594266-1 2011 The electrochemical interface of Au(100) and 1-butyl-3-methyl-imidazolium hexafluorophosphate has been characterized by cyclic voltammetry, electrochemical impedance spectroscopy and in situ STM, especially in two distinct potential ranges. 1-butyl-3-methylimidazolium hexafluorophosphate 45-93 sulfotransferase family 1A member 3 Homo sapiens 191-194 21524100-3 2011 This produces a ringlike feature in STM images, whose diameter depends on the tunneling conditions and distance to charged arsenic vacancies. Arsenic 123-130 sulfotransferase family 1A member 3 Homo sapiens 36-39 21595454-0 2011 In situ STM evidence for the adsorption geometry of three N-heteroaromatic thiols on Au(111). Sulfhydryl Compounds 75-81 sulfotransferase family 1A member 3 Homo sapiens 8-11 21595454-3 2011 Molecularly resolved STM images show that all three molecules form striped adlayers in the desorption region on the Au(111) surface. Gold 116-118 sulfotransferase family 1A member 3 Homo sapiens 21-24 21599081-2 2011 We focus in particular on hexadecafluorophthalocyanine (F(16)CuPc), using both theoretical and experimental (scanning tunneling microscopy - STM) studies. hexadecafluorophthalocyanine 26-54 sulfotransferase family 1A member 3 Homo sapiens 141-144 21599081-7 2011 This transfer is controlled by the layer thickness of, or the applied voltage on, epitaxial graphene resulting in selective F(16)CuPc adsorption, as observed in STM experiments. Graphite 92-100 sulfotransferase family 1A member 3 Homo sapiens 161-164 21513407-3 2011 In situ LT-STM experiments also indicate the formation of a molecularly sharp C(60)/6P interface with hexagonally-close-packed C(60) layers nucleated atop 6P layer on graphite. Graphite 167-175 sulfotransferase family 1A member 3 Homo sapiens 11-14 21465630-1 2011 The growth of adenine on Au(111) from the submonolayer up to several microns film thickness is studied by combining STM and surface X-ray diffraction techniques. Adenine 14-21 sulfotransferase family 1A member 3 Homo sapiens 116-119 21245037-2 2011 We also report here the synthesis, structure and STM current-imaging studies of DNA oligonucleotides containing the nucleobases (thymine) derivatized with 5-phenyl-telluride functionality (5-Te). Oligonucleotides 84-100 sulfotransferase family 1A member 3 Homo sapiens 49-52 21245037-2 2011 We also report here the synthesis, structure and STM current-imaging studies of DNA oligonucleotides containing the nucleobases (thymine) derivatized with 5-phenyl-telluride functionality (5-Te). nucleobases 116-127 sulfotransferase family 1A member 3 Homo sapiens 49-52 21245037-2 2011 We also report here the synthesis, structure and STM current-imaging studies of DNA oligonucleotides containing the nucleobases (thymine) derivatized with 5-phenyl-telluride functionality (5-Te). Thymine 129-136 sulfotransferase family 1A member 3 Homo sapiens 49-52 21245037-2 2011 We also report here the synthesis, structure and STM current-imaging studies of DNA oligonucleotides containing the nucleobases (thymine) derivatized with 5-phenyl-telluride functionality (5-Te). 5-phenyl-telluride 155-173 sulfotransferase family 1A member 3 Homo sapiens 49-52 21711870-0 2011 STM-induced light emission from thin films of perylene derivatives on the HOPG and Au substrates. Perylene 46-54 sulfotransferase family 1A member 3 Homo sapiens 0-3 21711870-0 2011 STM-induced light emission from thin films of perylene derivatives on the HOPG and Au substrates. Gold 83-85 sulfotransferase family 1A member 3 Homo sapiens 0-3 21341779-4 2011 For the CuPcOC8/PmPV composite film with 1:1 weight ratio, STM results reveal a preferential adsorption of PmPV on graphite surface, while AFM results indicate the phase segregation in the upper layer. pmpv 16-20 sulfotransferase family 1A member 3 Homo sapiens 59-62 21406881-7 2011 SP-STM experiments have evidenced that the antiferromagnetic layer coupling remains in the chromium mounds after deposition and is not significantly affected by the presence of the segregants. TFF2 protein, human 0-2 sulfotransferase family 1A member 3 Homo sapiens 3-6 21309565-6 2011 Raman and STM characterizations corroborate that the graphene sheets exfoliated by our electrochemical method preserve the intrinsic structure of graphene. Graphite 53-61 sulfotransferase family 1A member 3 Homo sapiens 10-13 21322530-1 2011 We investigate the adsorption and conformation of free-base porphines on Cu(110) using STM, reflection absorption infrared spectroscopy, and periodic DFT calculations in order to understand how the central polypyrrole macrocycle, common to all porphyrins, interacts with a reactive metal surface. porphine 60-69 sulfotransferase family 1A member 3 Homo sapiens 87-90 21711733-0 2011 Phase transition on the Si(001) clean surface prepared in UHV MBE chamber: a study by high-resolution STM and in situ RHEED. Silicon 24-26 sulfotransferase family 1A member 3 Homo sapiens 102-105 21711733-1 2011 The Si(001) surface deoxidized by short annealing at T ~ 925 C in the ultrahigh vacuum molecuar beam epitaxy chamber has been in situ investigated using high-resolution scanning tunneling microscopy (STM)and redegreesected high-energy electron diffraction (RHEED. Silicon 4-6 sulfotransferase family 1A member 3 Homo sapiens 200-203 21265533-7 2011 Furthermore, STM tip-substrate displacement data provide additional evidence that the electrodes bind to the outermost benzene rings of the pi-pi-stacked molecular wires. Benzene 119-126 sulfotransferase family 1A member 3 Homo sapiens 13-16 21168432-5 2011 Enzymatic assays using the eleven known human cytosolic sulfotransferases (SULTs) revealed SULT1A3 as the enzyme responsible for catalyzing the sulfation of chlorotyrosine and nitrotyrosine. 3-chlorotyrosine 157-171 sulfotransferase family 1A member 3 Homo sapiens 91-98 21168432-5 2011 Enzymatic assays using the eleven known human cytosolic sulfotransferases (SULTs) revealed SULT1A3 as the enzyme responsible for catalyzing the sulfation of chlorotyrosine and nitrotyrosine. 3-nitrotyrosine 176-189 sulfotransferase family 1A member 3 Homo sapiens 91-98 21168432-7 2011 Kinetic constants of the sulfation of chlorotyrosine and nitrotyrosine by SULT1A3 were determined. 3-chlorotyrosine 38-52 sulfotransferase family 1A member 3 Homo sapiens 74-81 21168432-7 2011 Kinetic constants of the sulfation of chlorotyrosine and nitrotyrosine by SULT1A3 were determined. 3-nitrotyrosine 57-70 sulfotransferase family 1A member 3 Homo sapiens 74-81 21168432-8 2011 Collectively, these results suggest that sulfation by SULT1A3 in lung endothelial and epithelial cells may play a role in the inactivation and/or disposal of excess chlorotyrosine and nitrotyrosine generated during inflammation. 3-chlorotyrosine 165-179 sulfotransferase family 1A member 3 Homo sapiens 54-61 21168432-8 2011 Collectively, these results suggest that sulfation by SULT1A3 in lung endothelial and epithelial cells may play a role in the inactivation and/or disposal of excess chlorotyrosine and nitrotyrosine generated during inflammation. 3-nitrotyrosine 184-197 sulfotransferase family 1A member 3 Homo sapiens 54-61 20676456-7 2010 However, the STM images show a long-range coincidence between the periodicity of the oxide film and that of the substrate along the short side of the oxide unit cell revealing that this lattice parameter is not exactly equal to that of the substrate. Oxides 85-90 sulfotransferase family 1A member 3 Homo sapiens 13-16 21117684-7 2011 Finally, the surface observation for HOPG modified with diazonium derivative by EC-STM showed a typical monolayer structure, in which the ferrocene moieties were packed densely at random. diazynium 56-65 sulfotransferase family 1A member 3 Homo sapiens 83-86 21117684-7 2011 Finally, the surface observation for HOPG modified with diazonium derivative by EC-STM showed a typical monolayer structure, in which the ferrocene moieties were packed densely at random. ferrocene 138-147 sulfotransferase family 1A member 3 Homo sapiens 83-86 21977410-1 2011 Surfaces of thin oxide films were investigated by means of a dual mode NC-AFM/STM. Oxides 17-22 sulfotransferase family 1A member 3 Homo sapiens 78-81 21678774-1 2011 Recent STM experiments show that by exposing h-BN/Rh(111) nanomesh to water or atomic hydrogen interesting phenomena can be observed. Water 70-75 sulfotransferase family 1A member 3 Homo sapiens 7-10 21678774-1 2011 Recent STM experiments show that by exposing h-BN/Rh(111) nanomesh to water or atomic hydrogen interesting phenomena can be observed. Hydrogen 86-94 sulfotransferase family 1A member 3 Homo sapiens 7-10 21678774-4 2011 For example, we could determine that the frequently observed three protrusions within the pore appearing in STM images obtained after dosing small amounts of water, are most likely determined by water hexamers. Water 158-163 sulfotransferase family 1A member 3 Homo sapiens 108-111 21678774-4 2011 For example, we could determine that the frequently observed three protrusions within the pore appearing in STM images obtained after dosing small amounts of water, are most likely determined by water hexamers. Water 195-200 sulfotransferase family 1A member 3 Homo sapiens 108-111 20859603-4 2010 The synthesized conjugates form polypseudorotaxanes with alpha-cyclodextrin which were characterized by 2D NOESY NMR spectra, powder X-ray diffraction patterns and in one case also by STM microscopy. polypseudorotaxanes 32-51 sulfotransferase family 1A member 3 Homo sapiens 184-187 20938548-1 2010 Scanning tunneling microscope light emission (STM-LE) spectroscopy has been utilized to elucidate the luminescence phenomena of Ag nanoparticles capped with myristate (myristate-capped AgNP) and 2-methyl-1-propanethiolate (C(4)S-capped AgNP) on the dodecanethiol-precovered Au substrate. Myristic Acid 157-166 sulfotransferase family 1A member 3 Homo sapiens 46-49 20938548-1 2010 Scanning tunneling microscope light emission (STM-LE) spectroscopy has been utilized to elucidate the luminescence phenomena of Ag nanoparticles capped with myristate (myristate-capped AgNP) and 2-methyl-1-propanethiolate (C(4)S-capped AgNP) on the dodecanethiol-precovered Au substrate. Myristic Acid 168-177 sulfotransferase family 1A member 3 Homo sapiens 46-49 20938548-1 2010 Scanning tunneling microscope light emission (STM-LE) spectroscopy has been utilized to elucidate the luminescence phenomena of Ag nanoparticles capped with myristate (myristate-capped AgNP) and 2-methyl-1-propanethiolate (C(4)S-capped AgNP) on the dodecanethiol-precovered Au substrate. agnp 185-189 sulfotransferase family 1A member 3 Homo sapiens 46-49 20964393-1 2010 Sub-5 nm metallic hafnium diboride (HfB(2)) nanostructures were directly written onto Si(100)-2 x 1:H surfaces using ultrahigh vacuum scanning tunneling microscope (UHV-STM) electron beam induced deposition (EBID) of a carbon-free precursor molecule, tetrakis(tetrahydroborato)hafnium, Hf(BH(4))(4). hfb(2) 36-42 sulfotransferase family 1A member 3 Homo sapiens 169-172 20964393-3 2010 To our knowledge, this is the first demonstration of sub-5 nm metallic nanostructures in an STM-EBID experiment. metallic 62-70 sulfotransferase family 1A member 3 Homo sapiens 92-95 20823501-0 2010 Understanding atomic-resolved STM images on TiO2(110)-(1 x 1) surface by DFT calculations. titanium dioxide 44-48 sulfotransferase family 1A member 3 Homo sapiens 30-33 21231324-0 2010 Observation and destruction of an elusive adsorbate with STM: O2/TiO2(110). Oxygen 62-64 sulfotransferase family 1A member 3 Homo sapiens 57-60 21231324-0 2010 Observation and destruction of an elusive adsorbate with STM: O2/TiO2(110). titanium dioxide 65-69 sulfotransferase family 1A member 3 Homo sapiens 57-60 21231324-4 2010 The adsorbed O2 easily dissociates during the STM measurements, and the formation of O(ad)"s at both sides of the original V(O) is observed. Oxygen 13-15 sulfotransferase family 1A member 3 Homo sapiens 46-49 21033816-2 2010 STM images show that the In(2)O forms an ordered monolayer on both InAs and InGaAs surfaces. indium arsenide 67-71 sulfotransferase family 1A member 3 Homo sapiens 0-3 20676456-7 2010 However, the STM images show a long-range coincidence between the periodicity of the oxide film and that of the substrate along the short side of the oxide unit cell revealing that this lattice parameter is not exactly equal to that of the substrate. Oxides 150-155 sulfotransferase family 1A member 3 Homo sapiens 13-16 20607163-0 2010 Electronic transport properties of individual 4,4"-bis(mercaptoalkyl)-biphenyl derivatives measured in STM-based break junctions. 4,4"-bis(mercaptoalkyl)-biphenyl derivatives 46-90 sulfotransferase family 1A member 3 Homo sapiens 103-106 20607163-7 2010 This relatively high value of conductance for the single Au(tip)-1BP9-Au(substrate) junction is attributed to an increased coupling of the BP unit to the adjacent electrode, i.e. the STM-tip or the Au-substrate. Gold 57-59 sulfotransferase family 1A member 3 Homo sapiens 183-186 20607163-7 2010 This relatively high value of conductance for the single Au(tip)-1BP9-Au(substrate) junction is attributed to an increased coupling of the BP unit to the adjacent electrode, i.e. the STM-tip or the Au-substrate. Benzo(a)pyrene 66-68 sulfotransferase family 1A member 3 Homo sapiens 183-186 20607163-7 2010 This relatively high value of conductance for the single Au(tip)-1BP9-Au(substrate) junction is attributed to an increased coupling of the BP unit to the adjacent electrode, i.e. the STM-tip or the Au-substrate. Gold 70-72 sulfotransferase family 1A member 3 Homo sapiens 183-186 20566371-3 2010 The fluorophore product (4-methylumbelliferone, MU) was continuously produced and monitored when SULT1A3 catalyzed dopamine sulfation with PAPS. Hymecromone 25-46 sulfotransferase family 1A member 3 Homo sapiens 97-104 20566371-3 2010 The fluorophore product (4-methylumbelliferone, MU) was continuously produced and monitored when SULT1A3 catalyzed dopamine sulfation with PAPS. Dopamine 115-123 sulfotransferase family 1A member 3 Homo sapiens 97-104 20567786-0 2010 Synthesis and UHV-STM observation of the T(d)-symmetric Lu metallofullerene: Lu2@C76(T(d)). lu metallofullerene 56-75 sulfotransferase family 1A member 3 Homo sapiens 18-21 20715271-1 2010 Self-assembled monolayers of 1,4-dicyanobenzene on Au(111) electrodes are studied by cyclic voltammetry, in-situ STM and ex-situ XPS. 1,4-dicyanobenzene 29-47 sulfotransferase family 1A member 3 Homo sapiens 113-116 20390144-3 2010 STM and LEED data obtained from one monolayer of the NiTPP-dimer on the Ag(111) surface show the formation of three domains which grow along the main crystallographic directions of the substrate. nitpp 53-58 sulfotransferase family 1A member 3 Homo sapiens 0-3 21399340-4 2010 The origin of the extremely large cross-section is ascribed to the modulated electronic states of graphite around the defect based on the STM measurements, which is due to the local breaking of the pi conjugated system of graphite. Graphite 98-106 sulfotransferase family 1A member 3 Homo sapiens 138-141 21399340-4 2010 The origin of the extremely large cross-section is ascribed to the modulated electronic states of graphite around the defect based on the STM measurements, which is due to the local breaking of the pi conjugated system of graphite. Graphite 222-230 sulfotransferase family 1A member 3 Homo sapiens 138-141 20485778-0 2010 Nanopatterning the surface with ordered supramolecular architectures of N(9)-alkylated guanines: STM reveals. n(9)-alkylated guanines 72-95 sulfotransferase family 1A member 3 Homo sapiens 97-100 20485778-1 2010 STM study of the self-assembly at the solid-liquid interface of substituted guanines exposing in the N(9)-position alkyl side chains with different lengths revealed the formation of distinct crystalline nanopatterns. Guanine 76-84 sulfotransferase family 1A member 3 Homo sapiens 0-3 20536126-0 2010 STM tip catalyzed adsorption of thiol molecules at the nanometer scale. Sulfhydryl Compounds 32-37 sulfotransferase family 1A member 3 Homo sapiens 0-3 20205404-6 2010 The predictive potential of the model was additionally illustrated by comparison of the obtained superstructures with the recent STM images that have been recorded for different organic tripod-shaped molecules adsorbed at the liquid/pyrolytic graphite interface. Graphite 243-251 sulfotransferase family 1A member 3 Homo sapiens 129-132 20536142-3 2010 The tip of an STM is used to form one contact, and the substrate the other; the molecules are conjugated oligophenyleneethynylenes (OPEs). poly(phenylene ethynylene) 105-130 sulfotransferase family 1A member 3 Homo sapiens 14-17 20536142-3 2010 The tip of an STM is used to form one contact, and the substrate the other; the molecules are conjugated oligophenyleneethynylenes (OPEs). poly(phenylene ethynylene) 132-136 sulfotransferase family 1A member 3 Homo sapiens 14-17 20586412-0 2010 Molecular assembly and electropolymerization of 3,4-ethylenedioxythiophene on Au(111) single crystal electrode as probed by in situ electrochemical STM in 0.10 M HClO4. 3,4-ethylenedioxythiophene 48-74 sulfotransferase family 1A member 3 Homo sapiens 148-151 20586412-0 2010 Molecular assembly and electropolymerization of 3,4-ethylenedioxythiophene on Au(111) single crystal electrode as probed by in situ electrochemical STM in 0.10 M HClO4. Perchloric Acid 162-167 sulfotransferase family 1A member 3 Homo sapiens 148-151 20586412-1 2010 We have used electrochemical scanning tunneling microscopy (EC-STM) to obtain molecular insights on the adlayer structures and electrochemical polymerization of 3,4-ethylenedioxythiophene (EDOT) on a bare Au(111) single crystal electrode in 0.1 M HClO(4) solution. 3,4-ethylenedioxythiophene 189-193 sulfotransferase family 1A member 3 Homo sapiens 63-66 20586412-3 2010 In situ STM revealed, for the first time, that EDOT molecules can spontaneously form organized adlayers on a bare Au(111) surface with 18 muM concentration of EDOT in aqueous solution. 3,4-ethylenedioxythiophene 47-51 sulfotransferase family 1A member 3 Homo sapiens 8-11 20586412-6 2010 Electropolymerization was also carried out using in situ STM in 0.10 M HClO(4) under potential control. Hypochlorous Acid 71-75 sulfotransferase family 1A member 3 Homo sapiens 57-60 20524617-1 2010 In this communication we provide the first UHV-STM images and STM-based current-voltage (I-V) and orbital mediated tunneling spectroscopy (OMTS) data on a self-assembled porphyrin nanostructure at the single structure level. Porphyrins 170-179 sulfotransferase family 1A member 3 Homo sapiens 47-50 20524617-1 2010 In this communication we provide the first UHV-STM images and STM-based current-voltage (I-V) and orbital mediated tunneling spectroscopy (OMTS) data on a self-assembled porphyrin nanostructure at the single structure level. Porphyrins 170-179 sulfotransferase family 1A member 3 Homo sapiens 62-65 20481458-0 2010 In situ STM observation of the CO adlayer on a Pt(110) electrode in 0.1 M HClO4 solution. Perchloric Acid 74-79 sulfotransferase family 1A member 3 Homo sapiens 8-11 20481458-1 2010 We have obtained the first in situ STM molecular image of a CO adlayer on a Pt(110)-(1 x 1) electrode surface in 0.1 M HClO(4) solution. Hypochlorous Acid 119-123 sulfotransferase family 1A member 3 Homo sapiens 35-38 21393736-1 2010 Co atoms and dimers embedded in a Cu(110)(2 x 1)-O surface oxide are investigated via low-temperature STM/STS experiments and first-principles simulations. Cobalt 0-2 sulfotransferase family 1A member 3 Homo sapiens 102-105 20455538-2 2010 In this work, we employed Electrochemical Scanning Tunneling Microscopy and Spectroscopy (EC-STM, EC-STS) to study the interfacial electron transfer properties of hydroquinone incorporated in a Self Assembled Monolayer on a Au(111) substrate. hydroquinone 163-175 sulfotransferase family 1A member 3 Homo sapiens 93-96 20073524-0 2010 Substrate-induced varied conformation and molecular assemblies: in situ STM observation of beta-substituted oligothiophene adlayers on Au(111). beta-substituted oligothiophene 91-122 sulfotransferase family 1A member 3 Homo sapiens 72-75 20396817-0 2010 Surface morphologies, electronic structures, and Kondo effect of lanthanide(III)-phthalocyanine molecules on Au(111) by using STM, STS and FET properties for next generation devices. Lanthanoid Series Elements 65-75 sulfotransferase family 1A member 3 Homo sapiens 126-129 20396817-0 2010 Surface morphologies, electronic structures, and Kondo effect of lanthanide(III)-phthalocyanine molecules on Au(111) by using STM, STS and FET properties for next generation devices. phthalocyanine 81-95 sulfotransferase family 1A member 3 Homo sapiens 126-129 20073524-0 2010 Substrate-induced varied conformation and molecular assemblies: in situ STM observation of beta-substituted oligothiophene adlayers on Au(111). Gold 135-137 sulfotransferase family 1A member 3 Homo sapiens 72-75 20158258-0 2010 Self-assembly of (S)-glutamic acid on Ag(100): a combined LT-STM and ab initio investigation. Glutamic Acid 17-34 sulfotransferase family 1A member 3 Homo sapiens 61-64 20218692-1 2010 Results from electrochemical studies, in situ STM, and ex situ angle-resolved XPS on self-assembled monolayers (SAMs) of thiazole on Au(111) are reported for the first time. Thiazoles 121-129 sulfotransferase family 1A member 3 Homo sapiens 46-49 20304798-3 2010 In vitro sulfation assays showed alkyl and aryl substitutions to a fused heterocyclic system modeled after beta-naphthol (betaN), based on compounds that interact with the estrogen receptor, rendered several molecules with enhanced specificity for SULT1E1 over SULT1A1*1, SULT1A1*2, SULT1A3, and SULT2A1. 2-naphthol 107-120 sulfotransferase family 1A member 3 Homo sapiens 283-290 20304798-3 2010 In vitro sulfation assays showed alkyl and aryl substitutions to a fused heterocyclic system modeled after beta-naphthol (betaN), based on compounds that interact with the estrogen receptor, rendered several molecules with enhanced specificity for SULT1E1 over SULT1A1*1, SULT1A1*2, SULT1A3, and SULT2A1. 2-naphthol 122-127 sulfotransferase family 1A member 3 Homo sapiens 283-290 20235114-1 2010 The redox behaviour and potential-dependent adsorption structure of heptyl viologen (1,1"-diheptyl-4,4"-bipyridinium dichloride, DHV(2+)) on a Cu(100) electrode was investigated in a chloride-containing electrolyte solution by cyclic voltammetry (CV) and in situ electrochemical scanning tunneling microscopy (EC-STM). 1,1'-diheptyl-4,4'-bipyridinium 68-83 sulfotransferase family 1A member 3 Homo sapiens 313-316 20235114-1 2010 The redox behaviour and potential-dependent adsorption structure of heptyl viologen (1,1"-diheptyl-4,4"-bipyridinium dichloride, DHV(2+)) on a Cu(100) electrode was investigated in a chloride-containing electrolyte solution by cyclic voltammetry (CV) and in situ electrochemical scanning tunneling microscopy (EC-STM). Copper 143-145 sulfotransferase family 1A member 3 Homo sapiens 313-316 20235114-3 2010 STM images obtained in a KCl-containing electrolyte solution disclose a well-ordered c(2x2) chloride adlayer on a Cu(100) electrode surface. Potassium Chloride 25-28 sulfotransferase family 1A member 3 Homo sapiens 0-3 20235114-3 2010 STM images obtained in a KCl-containing electrolyte solution disclose a well-ordered c(2x2) chloride adlayer on a Cu(100) electrode surface. c(2x2) chloride 85-100 sulfotransferase family 1A member 3 Homo sapiens 0-3 20235114-3 2010 STM images obtained in a KCl-containing electrolyte solution disclose a well-ordered c(2x2) chloride adlayer on a Cu(100) electrode surface. Copper 114-116 sulfotransferase family 1A member 3 Homo sapiens 0-3 20235114-4 2010 After injecting DHV(2+) molecules into the KCl electrolyte solution, a highly ordered 2D "dot-array" structure in STM images emerges on the c(2x2)-Cl modified Cu(100) electrode surface. dhv 16-19 sulfotransferase family 1A member 3 Homo sapiens 114-117 20235114-4 2010 After injecting DHV(2+) molecules into the KCl electrolyte solution, a highly ordered 2D "dot-array" structure in STM images emerges on the c(2x2)-Cl modified Cu(100) electrode surface. Potassium Chloride 43-46 sulfotransferase family 1A member 3 Homo sapiens 114-117 20235114-4 2010 After injecting DHV(2+) molecules into the KCl electrolyte solution, a highly ordered 2D "dot-array" structure in STM images emerges on the c(2x2)-Cl modified Cu(100) electrode surface. c(2x2)-cl 140-149 sulfotransferase family 1A member 3 Homo sapiens 114-117 20235114-4 2010 After injecting DHV(2+) molecules into the KCl electrolyte solution, a highly ordered 2D "dot-array" structure in STM images emerges on the c(2x2)-Cl modified Cu(100) electrode surface. Copper 159-161 sulfotransferase family 1A member 3 Homo sapiens 114-117 20235114-7 2010 One-electron reduction of the dications DHV(2+) around -150 mV causes a phase transition from a "dot-array" assembly to a stripe pattern formed by DHV(*+) radical monocations in STM images which has a bilayer structure. dhv 40-43 sulfotransferase family 1A member 3 Homo sapiens 178-181 20235114-7 2010 One-electron reduction of the dications DHV(2+) around -150 mV causes a phase transition from a "dot-array" assembly to a stripe pattern formed by DHV(*+) radical monocations in STM images which has a bilayer structure. dhv 147-150 sulfotransferase family 1A member 3 Homo sapiens 178-181 20306503-0 2010 Synthesis, magnetic properties, and STM spectroscopy of cobalt(II) Cubanes [Co(II) (4)(Cl)(4)(HL)(4)]. Cobalt(2+) 56-66 sulfotransferase family 1A member 3 Homo sapiens 36-39 20056724-7 2010 Based on expression levels SULT1A3 and SULT1B1 also will probably play a role in the sulfo-conjugation of hesperetin in vivo. Parathion 85-90 sulfotransferase family 1A member 3 Homo sapiens 27-34 19747768-7 2010 Cellular localization of SULT1A3 and STS was also assessed by indirect immunofluorescence on paraffin-embedded sections from control and malignant breast tissue clearly showing a correlation of qRT-PCR data with protein expression of these two enzymes. Paraffin 93-101 sulfotransferase family 1A member 3 Homo sapiens 25-32 19916533-5 2010 A submolecular resolution STM image of these domains exhibits distinction between some functional groups and the surrounding intermolecular hydrogen bonds along the [130] or [310] direction. Hydrogen 140-148 sulfotransferase family 1A member 3 Homo sapiens 26-29 20366437-1 2010 The interactions between adsorbates at a solid-liquid interface were studied by video-rate STM for the case of sulfur on Cu(100) electrode surfaces in HCl solution. Sulfur 111-117 sulfotransferase family 1A member 3 Homo sapiens 91-94 20175573-1 2010 The self-assembly of the binary molecular system comprising copper(II) phthalocyanine (CuPc) and copper-hexadecafluoro-phthalocyanine (F(16)CuPc) on graphite has been investigated by in situ low-temperature scanning tunneling microscopy (LT-STM). Graphite 149-157 sulfotransferase family 1A member 3 Homo sapiens 241-244 20058870-2 2010 High-resolution STM images reveal that a [array: see text] arrangement of the FSN SAMs is formed on Au(100). Gold 100-102 sulfotransferase family 1A member 3 Homo sapiens 16-19 19810724-0 2010 STM investigation of temperature-dependent two-dimensional supramolecular architectures of C60 and amino-tetraphenylporphyrin on Ag(110). amino-tetraphenylporphyrin 99-125 sulfotransferase family 1A member 3 Homo sapiens 0-3 19916533-6 2010 In the submolecular resolution STM, it is most reasonably interpreted that intermolecular network between adsorption alanines is connected by N-H(1)...O(2) and N-H(2)...O(2) hydrogen bonds to form each homochiral domain and the bond at the domain boundary is enhanced by scanning tip which is most probably modified. Alanine 117-125 sulfotransferase family 1A member 3 Homo sapiens 31-34 19916533-6 2010 In the submolecular resolution STM, it is most reasonably interpreted that intermolecular network between adsorption alanines is connected by N-H(1)...O(2) and N-H(2)...O(2) hydrogen bonds to form each homochiral domain and the bond at the domain boundary is enhanced by scanning tip which is most probably modified. Hydrogen 174-182 sulfotransferase family 1A member 3 Homo sapiens 31-34 19995071-0 2009 Spectroscopic STM studies of single gold(III) porphyrin molecules. gold(iii) porphyrin 36-55 sulfotransferase family 1A member 3 Homo sapiens 14-17 20067311-0 2010 Direct observation of conformational changes of beta-substituted duodecithiophene on a Au(111)-(square root(3) x 22) substrate using in situ electrochemical STM in 0.1 M HClO4. beta-substituted duodecithiophene 48-81 sulfotransferase family 1A member 3 Homo sapiens 157-160 20067311-0 2010 Direct observation of conformational changes of beta-substituted duodecithiophene on a Au(111)-(square root(3) x 22) substrate using in situ electrochemical STM in 0.1 M HClO4. Perchloric Acid 170-175 sulfotransferase family 1A member 3 Homo sapiens 157-160 20067311-1 2010 The adsorption of hexahexylduodecithiophene (12T) on a Au(111) electrode was investigated by using cyclic voltammetry (CV) and in situ electrochemical scanning tunneling microscopy (EC-STM) in 0.10 M HClO(4). hexahexylduodecithiophene 18-43 sulfotransferase family 1A member 3 Homo sapiens 185-188 21832523-4 2009 Theoretically simulated STM images for Mn/GaAs(110) indicate round protrusions at As sites and Ga sites, the latter being dependent on the Mn adsorption site (i.e. in different atomic layers). Gallium 42-44 sulfotransferase family 1A member 3 Homo sapiens 24-27 19646966-5 2009 Enzyme activities were assessed using the following substrates: 4-nitrophenol for SULT1A1, dopamine for SULT1A3, 17beta-estradiol for SULT1E1, and dehydroepiandrosterone for SULT2A1. Dopamine 91-99 sulfotransferase family 1A member 3 Homo sapiens 104-111 19924324-5 2009 Using XPS and STM we have investigated the formation of the CuCl(2) like surface species and propose that it derives from the unusual reactivity of transient copper adatoms released from the p(2 x 1)O by the exothermic formation of water. cupric chloride 60-67 sulfotransferase family 1A member 3 Homo sapiens 14-17 19924324-5 2009 Using XPS and STM we have investigated the formation of the CuCl(2) like surface species and propose that it derives from the unusual reactivity of transient copper adatoms released from the p(2 x 1)O by the exothermic formation of water. Copper 158-164 sulfotransferase family 1A member 3 Homo sapiens 14-17 19924324-5 2009 Using XPS and STM we have investigated the formation of the CuCl(2) like surface species and propose that it derives from the unusual reactivity of transient copper adatoms released from the p(2 x 1)O by the exothermic formation of water. Water 232-237 sulfotransferase family 1A member 3 Homo sapiens 14-17 19774253-1 2009 In situ STM imaging of Au(100) electrode in 1 M HClO4 + 0.03 M aniline revealed highly ordered aniline adlattices of (2 radical 2 x 4 radical 2)R45 degrees and (radical 10 x radical 10)R18 degrees and polyaniline molecules exhibiting wiggling conformations at potentials negative and positive of 0.95 V (vs. reversible hydrogen electrode), respectively. Gold 23-25 sulfotransferase family 1A member 3 Homo sapiens 8-11 19874050-5 2009 On the basis of the high-resolution STM images, it was tentatively proposed that three types of chiral supramolecular nanostructures were formed by two-dimensional adsorption-induced chiral p-CPAEt species together with lateral hydrogen-bonding interaction (C-H...N[triple bond]C). Hydrogen 228-236 sulfotransferase family 1A member 3 Homo sapiens 36-39 20449033-6 2009 In addition, STM images of oligopyridine and phthalocyanine molecules were simulated based on periodic and local density functional theory calculations. oligopyridine 27-40 sulfotransferase family 1A member 3 Homo sapiens 13-16 20449033-6 2009 In addition, STM images of oligopyridine and phthalocyanine molecules were simulated based on periodic and local density functional theory calculations. phthalocyanine 45-59 sulfotransferase family 1A member 3 Homo sapiens 13-16 19715338-0 2009 EC-STM study of potential-controlled adsorption of substituted pyrimidinethiol on Au(111). pyrimidinethiol 63-78 sulfotransferase family 1A member 3 Homo sapiens 3-6 19715338-0 2009 EC-STM study of potential-controlled adsorption of substituted pyrimidinethiol on Au(111). Gold 82-84 sulfotransferase family 1A member 3 Homo sapiens 3-6 19715338-2 2009 Therefore, in this paper, the adsorption behavior of 4-hydroxy-6-(trifluoromethyl)pyrimidine-2-thiol (HTPT) on a Au(111) surface has been investigated using electrochemical scanning tunneling microscopy (EC-STM). 4-Hydroxy-6-(trifluoromethyl)pyrimidine-2-thiol 53-100 sulfotransferase family 1A member 3 Homo sapiens 207-210 19780556-1 2009 We used STM to observe visible light photo-oxidation reactions of formic acid on the ordered lattice-work structure of a TiO(2)(001) surface for the first time. formic acid 66-77 sulfotransferase family 1A member 3 Homo sapiens 8-11 19777521-2 2009 Herein, we present an ultrahigh-vacuum scanning tunneling microscopy and scanning tunneling spectroscopy (UHV-STM/STS) study of ex situ self-assembled supramolecular dyads consisting of fulleropyrrolidines (PyC(2)C(60)) axially ligated to zinc(II) tetraphenylporphyrin (ZnTPP), self organized on a 4-aminothiophenol (4-ATP) self-assembled monolayer on gold(111). fulleropyrrolidines 186-205 sulfotransferase family 1A member 3 Homo sapiens 110-113 19774253-1 2009 In situ STM imaging of Au(100) electrode in 1 M HClO4 + 0.03 M aniline revealed highly ordered aniline adlattices of (2 radical 2 x 4 radical 2)R45 degrees and (radical 10 x radical 10)R18 degrees and polyaniline molecules exhibiting wiggling conformations at potentials negative and positive of 0.95 V (vs. reversible hydrogen electrode), respectively. Perchloric Acid 48-53 sulfotransferase family 1A member 3 Homo sapiens 8-11 19774253-1 2009 In situ STM imaging of Au(100) electrode in 1 M HClO4 + 0.03 M aniline revealed highly ordered aniline adlattices of (2 radical 2 x 4 radical 2)R45 degrees and (radical 10 x radical 10)R18 degrees and polyaniline molecules exhibiting wiggling conformations at potentials negative and positive of 0.95 V (vs. reversible hydrogen electrode), respectively. aniline 63-70 sulfotransferase family 1A member 3 Homo sapiens 8-11 19774253-1 2009 In situ STM imaging of Au(100) electrode in 1 M HClO4 + 0.03 M aniline revealed highly ordered aniline adlattices of (2 radical 2 x 4 radical 2)R45 degrees and (radical 10 x radical 10)R18 degrees and polyaniline molecules exhibiting wiggling conformations at potentials negative and positive of 0.95 V (vs. reversible hydrogen electrode), respectively. aniline 95-102 sulfotransferase family 1A member 3 Homo sapiens 8-11 19774253-1 2009 In situ STM imaging of Au(100) electrode in 1 M HClO4 + 0.03 M aniline revealed highly ordered aniline adlattices of (2 radical 2 x 4 radical 2)R45 degrees and (radical 10 x radical 10)R18 degrees and polyaniline molecules exhibiting wiggling conformations at potentials negative and positive of 0.95 V (vs. reversible hydrogen electrode), respectively. polyaniline 201-212 sulfotransferase family 1A member 3 Homo sapiens 8-11 19774253-1 2009 In situ STM imaging of Au(100) electrode in 1 M HClO4 + 0.03 M aniline revealed highly ordered aniline adlattices of (2 radical 2 x 4 radical 2)R45 degrees and (radical 10 x radical 10)R18 degrees and polyaniline molecules exhibiting wiggling conformations at potentials negative and positive of 0.95 V (vs. reversible hydrogen electrode), respectively. Hydrogen 319-327 sulfotransferase family 1A member 3 Homo sapiens 8-11 19633186-6 2009 The fully aromatic [11]helicene was studied in detail including the measurement and theoretical calculation of its racemization barrier and its organization on the InSb (001) surface by STM. [11]helicene 19-31 sulfotransferase family 1A member 3 Homo sapiens 186-189 19737018-1 2009 On the basis of high resolution STM images and DFT modeling, we have resolved low- and high-coverage structures of methylthiolate (CH(3)S) self-assembled on the Au(111) surface. methylthiolate 115-129 sulfotransferase family 1A member 3 Homo sapiens 32-35 19792665-2 2009 By combining real-space imaging of scanning tunneling microscopy and spectroscopy (STM+STS) with momentum-space quantitative low-energy electron diffraction (LEED), we have identified the surface plane of cleaved BaFe2As2 crystals as the As terminated Fe-As layer-the plane where superconductivity occurs. Iron 215-217 sulfotransferase family 1A member 3 Homo sapiens 83-86 19792665-4 2009 It is surprising that STM images the different Fe-As orbitals associated with the orthorhombic structure, but not the As atoms in the surface plane. Iron 47-49 sulfotransferase family 1A member 3 Homo sapiens 22-25 19792665-4 2009 It is surprising that STM images the different Fe-As orbitals associated with the orthorhombic structure, but not the As atoms in the surface plane. Arsenic 50-52 sulfotransferase family 1A member 3 Homo sapiens 22-25 19586022-3 2009 In addition, the local electronic structures of Ni-Pd mixed-metal single crystals were directly investigated by using scanning tunneling microscopy (STM) at room temperature and ambient pressure. ni-pd 48-53 sulfotransferase family 1A member 3 Homo sapiens 149-152 21828469-1 2009 A low temperature scanning tunneling microscope (LT-STM) was used to investigate a new superstructure on the cleaved surface of a 2H- NbSe(2) single crystal after introduction of structural defects through bias voltage pulses during tunneling at 4.2 K. A charge density wave (CDW) with a [Formula: see text] reconstruction was observed in the vicinity of the defects and the well-known 3 x 3 CDW was observed far from these defects. Deuterium 130-132 sulfotransferase family 1A member 3 Homo sapiens 52-55 19792522-1 2009 The possibility to modify the adsorption properties of a porous silica/Mo(112) film by controlling its work function has been studied by a combined STM and density-functional theory approach. Silicon Dioxide 64-70 sulfotransferase family 1A member 3 Homo sapiens 148-151 19792529-0 2009 Switching a single spin on metal surfaces by a STM Tip: Ab Initio studies. Metals 27-32 sulfotransferase family 1A member 3 Homo sapiens 47-50 19792529-1 2009 The exchange coupling between single 3d magnetic adatoms (Cr, Mn, Fe, and Co) adsorbed on a Cu(001) surface and a Cr STM tip is studied with ab initio calculations. Chromium 114-116 sulfotransferase family 1A member 3 Homo sapiens 117-120 19588964-2 2009 As revealed by in situ video-STM the formation of this phase starts with lateral displacements of Cu surface atoms from lattice positions, resulting in stripe-like structures, followed by expansion of the surface lattice along the stripe direction. Copper 98-100 sulfotransferase family 1A member 3 Homo sapiens 29-32 19341286-1 2009 Graphene nanosheets produced in the form of stable aqueous dispersions by chemical reduction of graphene oxide and deposited onto graphite substrates have been investigated by atomic force and scanning tunneling microscopy (AFM/STM). Graphite 0-8 sulfotransferase family 1A member 3 Homo sapiens 228-231 19447296-6 2009 Enzymatic assays using the eleven known human cytosolic SULTs revealed SULT1A3 as the major enzyme responsible for the sulfation of both dopamine and 3-methyldopamine. Dopamine 137-145 sulfotransferase family 1A member 3 Homo sapiens 71-78 19447296-6 2009 Enzymatic assays using the eleven known human cytosolic SULTs revealed SULT1A3 as the major enzyme responsible for the sulfation of both dopamine and 3-methyldopamine. 3-methyldopamine 150-166 sulfotransferase family 1A member 3 Homo sapiens 71-78 19447296-7 2009 Kinetic analysis showed that the catalytic efficiency of SULT1A3 with 3-methyldopamine was 1.6 times than that with dopamine. 3-methyldopamine 70-86 sulfotransferase family 1A member 3 Homo sapiens 57-64 19447296-7 2009 Kinetic analysis showed that the catalytic efficiency of SULT1A3 with 3-methyldopamine was 1.6 times than that with dopamine. Dopamine 78-86 sulfotransferase family 1A member 3 Homo sapiens 57-64 19447296-0 2009 Concerted action of the cytosolic sulfotransferase, SULT1A3, and catechol-O-methyltransferase in the metabolism of dopamine in SK-N-MC human neuroblastoma cells. Dopamine 115-123 sulfotransferase family 1A member 3 Homo sapiens 52-59 19447296-0 2009 Concerted action of the cytosolic sulfotransferase, SULT1A3, and catechol-O-methyltransferase in the metabolism of dopamine in SK-N-MC human neuroblastoma cells. sk-n-mc 127-134 sulfotransferase family 1A member 3 Homo sapiens 52-59 19447296-1 2009 Conjugation reactions catalyzed by the cytosolic sulfotransferase, SULT1A3, or catechol-O-methyltransferase (COMT) are known to be involved in the regulation and homeostasis of dopamine and other monoamine neurotransmitters. Dopamine 177-185 sulfotransferase family 1A member 3 Homo sapiens 67-74 19447296-3 2009 The current study aimed to investigate the concerted action of SULT1A3 and COMT in dopamine metabolism. Dopamine 83-91 sulfotransferase family 1A member 3 Homo sapiens 63-70 19341286-9 2009 The unreduced graphene oxide nanosheets could only be imaged by STM at very low tunneling currents (approximately 1 pA), being visualized in some cases with inverted contrast relative to the graphite substrate, a result that was attributed to their extremely low conductivity. graphene oxide 14-28 sulfotransferase family 1A member 3 Homo sapiens 64-67 19364103-1 2009 Isolated Co-phthalocyanine (CoPc) molecules were moved on a monolayer of CoPc on Cu(111) using an STM tip. co-phthalocyanine 9-26 sulfotransferase family 1A member 3 Homo sapiens 98-101 19364103-1 2009 Isolated Co-phthalocyanine (CoPc) molecules were moved on a monolayer of CoPc on Cu(111) using an STM tip. copc 28-32 sulfotransferase family 1A member 3 Homo sapiens 98-101 19366268-5 2009 In the STM observations we can distinguish three (t,t,t,t) conformational isomers, three (t,t,t,c) conformational isomers, and one (t,c,t,c) isomer, which self-assemble into different adlayers with TCDB on a HOPG surface. trimethylaminocarboxyldihydroboran 198-202 sulfotransferase family 1A member 3 Homo sapiens 7-10 21817477-5 2009 In order to investigate the reactivity of graphene we expose graphene islands to a partial pressure of oxygen and following the evolution of the surface by STM during the exposure. Graphite 42-50 sulfotransferase family 1A member 3 Homo sapiens 156-159 19325986-10 2009 STM shows that the morphology of the particle system is largely conserved during NO(2) exposure at 300 K. The reaction is limited to the formation of surface nitrites and nitrates, which are characterized by low thermal stability and completely decompose below 500 K. As no further sintering occurs before decomposition, NO(2) uptake and release is a fully reversible process. Nitrogen Dioxide 81-86 sulfotransferase family 1A member 3 Homo sapiens 0-3 19325986-10 2009 STM shows that the morphology of the particle system is largely conserved during NO(2) exposure at 300 K. The reaction is limited to the formation of surface nitrites and nitrates, which are characterized by low thermal stability and completely decompose below 500 K. As no further sintering occurs before decomposition, NO(2) uptake and release is a fully reversible process. Nitrites 158-166 sulfotransferase family 1A member 3 Homo sapiens 0-3 19325986-10 2009 STM shows that the morphology of the particle system is largely conserved during NO(2) exposure at 300 K. The reaction is limited to the formation of surface nitrites and nitrates, which are characterized by low thermal stability and completely decompose below 500 K. As no further sintering occurs before decomposition, NO(2) uptake and release is a fully reversible process. Nitrates 171-179 sulfotransferase family 1A member 3 Homo sapiens 0-3 19325986-10 2009 STM shows that the morphology of the particle system is largely conserved during NO(2) exposure at 300 K. The reaction is limited to the formation of surface nitrites and nitrates, which are characterized by low thermal stability and completely decompose below 500 K. As no further sintering occurs before decomposition, NO(2) uptake and release is a fully reversible process. Nitrogen Dioxide 321-326 sulfotransferase family 1A member 3 Homo sapiens 0-3 19171676-6 2009 SULT1A1 is known to catalyze the metabolism of small phenols, whereas SULT1A3 sulfates catecholamine neurotransmitters. Sulfates 78-86 sulfotransferase family 1A member 3 Homo sapiens 70-77 19171676-6 2009 SULT1A1 is known to catalyze the metabolism of small phenols, whereas SULT1A3 sulfates catecholamine neurotransmitters. Catecholamines 87-100 sulfotransferase family 1A member 3 Homo sapiens 70-77 19209364-1 2009 The reactions of 3,4,9,10-perylenetetracarboxylic dianhydride with 4,4"-diamino-p-terphenyl and with 2,4,6-tris(4-aminophenyl)-1,3,5-triazine on an Au(111) surface have been followed by low-temperature UHV-STM in the range of 300 to 700 K at coverages of up to one monolayer. 3,4,9,10-perylenetetracarboxylic dianhydride 17-61 sulfotransferase family 1A member 3 Homo sapiens 206-209 19197965-0 2009 Field-emission resonances at tip/alpha,omega-mercaptoalkyl ferrocene/Au interfaces studied by STM. omega-mercaptoalkyl ferrocene 39-68 sulfotransferase family 1A member 3 Homo sapiens 94-97 19197965-0 2009 Field-emission resonances at tip/alpha,omega-mercaptoalkyl ferrocene/Au interfaces studied by STM. Gold 69-71 sulfotransferase family 1A member 3 Homo sapiens 94-97 19350454-3 2009 hSULT1A1 and hSULT1A3 as well as human intestine cytosol can catalyse the sulfation of the investigated flavonoids. Flavonoids 104-114 sulfotransferase family 1A member 3 Homo sapiens 13-21 19350454-5 2009 Hesperetin and eriodictyol are potent inhibitors of purified hSULT1A1, hSULT1A3, hSULT1E1, and hSULT2A1. hesperetin 0-10 sulfotransferase family 1A member 3 Homo sapiens 71-79 19350454-5 2009 Hesperetin and eriodictyol are potent inhibitors of purified hSULT1A1, hSULT1A3, hSULT1E1, and hSULT2A1. eriodictyol 15-26 sulfotransferase family 1A member 3 Homo sapiens 71-79 19350454-6 2009 Catechin and epicatechin inhibited hSULT1A1 and hSULT1A3, but not hSULT1E1 and hSULT2A1. Catechin 0-8 sulfotransferase family 1A member 3 Homo sapiens 48-56 19350454-6 2009 Catechin and epicatechin inhibited hSULT1A1 and hSULT1A3, but not hSULT1E1 and hSULT2A1. Catechin 13-24 sulfotransferase family 1A member 3 Homo sapiens 48-56 19420479-1 2009 We investigated electronic properties of a biochemically synthesized cobalt oxide bionanodot (Co-BND) by means of scanning tunneling microscopy/spectroscopy (STM/STS) and Kelvin-probe force microscopy (KFM). cobalt oxide 69-81 sulfotransferase family 1A member 3 Homo sapiens 158-161 19245268-12 2009 At first, we used C(60) fullerenes as wheels, which allowed the demonstration of a directional rolling mechanism of a nanocar on a gold surface by STM. fullerene C60 18-34 sulfotransferase family 1A member 3 Homo sapiens 147-150 19209364-1 2009 The reactions of 3,4,9,10-perylenetetracarboxylic dianhydride with 4,4"-diamino-p-terphenyl and with 2,4,6-tris(4-aminophenyl)-1,3,5-triazine on an Au(111) surface have been followed by low-temperature UHV-STM in the range of 300 to 700 K at coverages of up to one monolayer. 4,4''-Diamino-p-terphenyl 67-91 sulfotransferase family 1A member 3 Homo sapiens 206-209 19257215-3 2009 Several adsorption structures, e.g., Pd-Pd, Ag-Pd, and Au-Pd complexes, have been prepared in this way and analyzed with the STM and density functional theory. au-pd 55-60 sulfotransferase family 1A member 3 Homo sapiens 125-128 19177646-1 2009 Using UHV-STM investigations and density-functional theory calculations we prove the contribution of Cu-adatoms to the stabilization of a new high-density phase of benzoate molecules on a Cu(110) substrate. cu-adatoms 101-111 sulfotransferase family 1A member 3 Homo sapiens 10-13 19177646-1 2009 Using UHV-STM investigations and density-functional theory calculations we prove the contribution of Cu-adatoms to the stabilization of a new high-density phase of benzoate molecules on a Cu(110) substrate. Benzoates 164-172 sulfotransferase family 1A member 3 Homo sapiens 10-13 19123790-2 2009 A combined theoretical and experimental (STM, photoemission) study of the molecular-scale factors involved in the formation of gap states in TiO(2) is presented. titanium dioxide 141-147 sulfotransferase family 1A member 3 Homo sapiens 41-44 19180615-0 2009 STM insight into hydrogen-bonded bicomponent 1D supramolecular polymers with controlled geometries at the liquid-solid interface. Hydrogen 17-25 sulfotransferase family 1A member 3 Homo sapiens 0-3 19032108-3 2009 Those are attributable to Ge-N dative bonding of pyridine through the lone pair electrons of its N atom, which is consistent with previous STM and theoretical studies. pyridine 49-57 sulfotransferase family 1A member 3 Homo sapiens 139-142 19032108-3 2009 Those are attributable to Ge-N dative bonding of pyridine through the lone pair electrons of its N atom, which is consistent with previous STM and theoretical studies. Nitrogen 29-30 sulfotransferase family 1A member 3 Homo sapiens 139-142 19322772-1 2009 Dynamic surfaces: The conformational transition of 2,6-bis(1-aryl-1,2,3-triazol-4-yl)pyridine (BTP) derivatives, triggered by a change in pH, has been observed with a sub-nm resolution by STM at the solid-liquid interface. 2,6-bis(1-aryl-1,2,3-triazol-4-yl)pyridine 51-93 sulfotransferase family 1A member 3 Homo sapiens 188-191 19322772-1 2009 Dynamic surfaces: The conformational transition of 2,6-bis(1-aryl-1,2,3-triazol-4-yl)pyridine (BTP) derivatives, triggered by a change in pH, has been observed with a sub-nm resolution by STM at the solid-liquid interface. 2,6-bis(1,2,3-triazol-4-yl)pyridine 95-98 sulfotransferase family 1A member 3 Homo sapiens 188-191 19082105-1 2008 Helical double stranded polymers incorporated with a covalently bound chiral ferrocene linker are synthesised and characterized by CD spectra and STM images and molecular dynamics simulations. Polymers 24-32 sulfotransferase family 1A member 3 Homo sapiens 146-149 19049274-1 2008 Using STM, infrared absorption reflection spectroscopy experiments and density functional calculations we show that low temperature adsorption of CO on gold surfaces modified by vacancy islands leads to morphological changes and the formation of nanosized Au particles. Gold 256-258 sulfotransferase family 1A member 3 Homo sapiens 6-9 18980356-0 2008 An STM study on nonionic fluorosurfactant zonyl FSN self-assembly on Au(111): large domains, few defects, and good stability. Zonyl 42-51 sulfotransferase family 1A member 3 Homo sapiens 3-6 18975942-2 2008 Electrochemical scanning tunneling microscopy (EC-STM) images revealed the formation of supramolecularly organized nanostructures of cis-H(4)DCPP(2+) such as dimer, trimer, and tetramer on the (square root(3) x square root(7)) sulfate/bisulfate adlayer, suggesting the importance of both electrostatic interaction between cationic porphyrin core and sulfate/bisulfate adlayer and the hydrogen bond formation between carboxyl groups of the nearest neighbor cationic porphyrins. 4,4-dicarboxy-5-pyridoxylproline 141-145 sulfotransferase family 1A member 3 Homo sapiens 50-53 19260323-7 2008 The level of sTM was increased in patients after 14 d, while puerarin treated patient has lower sTM level than patients with basic treatment (P < 0.05). puerarin 61-69 sulfotransferase family 1A member 3 Homo sapiens 96-99 19260323-8 2008 CONCLUSION: Patients with ACI cotreated with puerarin and aspirin improved the neurological function, decreased the levels of serum vWF and sTM, indicating puerarin with aspirin had the protective effects on the damaged vascular endothelial cells. puerarin 45-53 sulfotransferase family 1A member 3 Homo sapiens 140-143 19260323-8 2008 CONCLUSION: Patients with ACI cotreated with puerarin and aspirin improved the neurological function, decreased the levels of serum vWF and sTM, indicating puerarin with aspirin had the protective effects on the damaged vascular endothelial cells. Aspirin 58-65 sulfotransferase family 1A member 3 Homo sapiens 140-143 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Dopamine 61-69 sulfotransferase family 1A member 3 Homo sapiens 42-49 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Dopamine 61-69 sulfotransferase family 1A member 3 Homo sapiens 51-59 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Water 158-163 sulfotransferase family 1A member 3 Homo sapiens 42-49 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Water 158-163 sulfotransferase family 1A member 3 Homo sapiens 51-59 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Amines 64-69 sulfotransferase family 1A member 3 Homo sapiens 42-49 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Amines 64-69 sulfotransferase family 1A member 3 Homo sapiens 51-59 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Dopamine 236-244 sulfotransferase family 1A member 3 Homo sapiens 42-49 18977225-4 2008 In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. Dopamine 236-244 sulfotransferase family 1A member 3 Homo sapiens 51-59 19260323-8 2008 CONCLUSION: Patients with ACI cotreated with puerarin and aspirin improved the neurological function, decreased the levels of serum vWF and sTM, indicating puerarin with aspirin had the protective effects on the damaged vascular endothelial cells. puerarin 156-164 sulfotransferase family 1A member 3 Homo sapiens 140-143 19260323-8 2008 CONCLUSION: Patients with ACI cotreated with puerarin and aspirin improved the neurological function, decreased the levels of serum vWF and sTM, indicating puerarin with aspirin had the protective effects on the damaged vascular endothelial cells. Aspirin 170-177 sulfotransferase family 1A member 3 Homo sapiens 140-143 18975942-7 2008 In addition, the high-resolution STM clearly distinguished between cis-H(4)DCPP(2+) ion and cis-H(2)DCPP molecule. cis-h(4)dcpp 67-79 sulfotransferase family 1A member 3 Homo sapiens 33-36 18975942-7 2008 In addition, the high-resolution STM clearly distinguished between cis-H(4)DCPP(2+) ion and cis-H(2)DCPP molecule. cis-h(2)dcpp 92-104 sulfotransferase family 1A member 3 Homo sapiens 33-36 18975950-1 2008 We report on the construction of an asymmetric tunneling junction between a Au STM tip and a Au(111)-(1 x 1) substrate electrode modified with the redox-active molecule N-hexyl-N"-(6-thiohexyl)-4,4"-bipyridinium bromide (HS6V6) in an electrochemical environment. Gold 76-78 sulfotransferase family 1A member 3 Homo sapiens 79-82 18975950-1 2008 We report on the construction of an asymmetric tunneling junction between a Au STM tip and a Au(111)-(1 x 1) substrate electrode modified with the redox-active molecule N-hexyl-N"-(6-thiohexyl)-4,4"-bipyridinium bromide (HS6V6) in an electrochemical environment. au(111) 93-100 sulfotransferase family 1A member 3 Homo sapiens 79-82 18975950-1 2008 We report on the construction of an asymmetric tunneling junction between a Au STM tip and a Au(111)-(1 x 1) substrate electrode modified with the redox-active molecule N-hexyl-N"-(6-thiohexyl)-4,4"-bipyridinium bromide (HS6V6) in an electrochemical environment. n-hexyl-n"-(6-thiohexyl)-4,4"-bipyridinium bromide 169-219 sulfotransferase family 1A member 3 Homo sapiens 79-82 18975950-1 2008 We report on the construction of an asymmetric tunneling junction between a Au STM tip and a Au(111)-(1 x 1) substrate electrode modified with the redox-active molecule N-hexyl-N"-(6-thiohexyl)-4,4"-bipyridinium bromide (HS6V6) in an electrochemical environment. hs6v6 221-226 sulfotransferase family 1A member 3 Homo sapiens 79-82 18950238-1 2008 We have studied the atomic-scale structure of the Mo6S6 nanowires using scanning tunneling microscopy and spectroscopy (STM and STS) and density functional theory (DFT). mo6s6 50-55 sulfotransferase family 1A member 3 Homo sapiens 120-123 19206406-6 2008 Arrhenius plots for individual dibutyl sulfide molecules reveal that the torsional barrier to rotation is approximately 1.2 kJ/mol, in good agreement with the temperature at which the molecule"s appearance changes from a linear to a hexagonal shape in the STM images. dibutyl sulfide 31-46 sulfotransferase family 1A member 3 Homo sapiens 256-259 18834127-0 2008 "Naked" iron-5,10,15-triphenylcorrole on Cu(111): observation of chirality on a surface and manipulation of multiple conformational states by STM. iron-5,10,15-triphenylcorrole 8-37 sulfotransferase family 1A member 3 Homo sapiens 142-145 18293307-6 2008 STM simulations reveal that details about both, benzene adsorption geometry and fluorine position, can be only detected at short tip-surface distances. Benzene 48-55 sulfotransferase family 1A member 3 Homo sapiens 0-3 18808190-4 2008 As an example, we consider the STM-induced dissociation of acetylene. Acetylene 59-68 sulfotransferase family 1A member 3 Homo sapiens 31-34 19049071-1 2008 A low-temperature ultrahigh-vacuum scanning tunneling microscope (UHV-STM) was used to image viologen (N-methyl-N"-di (8-mercaptooctyl)-4,4"-bipyridinium; HSC8VC8SH) molecules and to perform local spectroscopic measurements on these molecules. n-methyl-n"-di (8-mercaptooctyl)-4,4"-bipyridinium 103-153 sulfotransferase family 1A member 3 Homo sapiens 70-73 18788809-6 2008 The strategy present in this work not only extends the capability of STM-BJ to create a variety of metal nanowires including magnetic nanowires for further investigations but also provides opportunities to construct metal-molecule-metal junctions with a variety of choices of metals in the junctions. Metals 99-104 sulfotransferase family 1A member 3 Homo sapiens 69-72 18788809-6 2008 The strategy present in this work not only extends the capability of STM-BJ to create a variety of metal nanowires including magnetic nanowires for further investigations but also provides opportunities to construct metal-molecule-metal junctions with a variety of choices of metals in the junctions. Metals 216-221 sulfotransferase family 1A member 3 Homo sapiens 69-72 18788809-6 2008 The strategy present in this work not only extends the capability of STM-BJ to create a variety of metal nanowires including magnetic nanowires for further investigations but also provides opportunities to construct metal-molecule-metal junctions with a variety of choices of metals in the junctions. Metals 216-221 sulfotransferase family 1A member 3 Homo sapiens 69-72 18710227-0 2008 Oriented organic islands and one-dimensional chains on a Au(111) surface fabricated by electrodeposition: an STM study. Gold 57-59 sulfotransferase family 1A member 3 Homo sapiens 109-112 18293307-6 2008 STM simulations reveal that details about both, benzene adsorption geometry and fluorine position, can be only detected at short tip-surface distances. Fluorine 80-88 sulfotransferase family 1A member 3 Homo sapiens 0-3 17706427-1 2008 Cyclodextrin-based aggregates have been widely investigated with microscopies such as STM, AFM, SEM, TEM, and fluorescent microscopy to obtain the direct morphology and structure of samples. Cyclodextrins 0-12 sulfotransferase family 1A member 3 Homo sapiens 86-89 18529035-4 2008 In addition, isomerization of the noncentrosymmetric tris(phthalocyaninato) lutetium triple-decker complex has been revealed directly with STM and further confirmed by theoretical simulation. tris(phthalocyaninato) lutetium triple-decker 53-98 sulfotransferase family 1A member 3 Homo sapiens 139-142 18643522-1 2008 The structural and morphological changes occurring in an ensemble of vapor deposited palladium nanoclusters have been studied after several hydrogenation cycles with x-ray diffraction, extended x-ray-absorption fine structure spectroscopy, Rutherford backscattering spectrometry, and STM. Palladium 85-94 sulfotransferase family 1A member 3 Homo sapiens 284-287 18473073-0 2008 A rigid sublimable naphthalenediimide cyclophane as model compound for UHV STM experiments. naphthalenediimide cyclophane 19-48 sulfotransferase family 1A member 3 Homo sapiens 75-78 19206347-1 2008 Reversible conductance switching in single quinone-oligo(phenylene vinylene) (Q-OPV) molecules was demonstrated using electrochemical STM. quinone-oligo(phenylene vinylene) 43-76 sulfotransferase family 1A member 3 Homo sapiens 134-137 19206347-1 2008 Reversible conductance switching in single quinone-oligo(phenylene vinylene) (Q-OPV) molecules was demonstrated using electrochemical STM. q-opv 78-83 sulfotransferase family 1A member 3 Homo sapiens 134-137 18473073-1 2008 The design, synthesis and characterization of a rigid naphthalenediimide cyclophane as a model compound for ultrahigh vacuum (UHV) STM experiments are described together with first self-assembly investigations on an Au(111) substrate displaying the formation of densely packed parallel rows of molecules. naphthalenediimide cyclophane 54-83 sulfotransferase family 1A member 3 Homo sapiens 131-134 18232020-4 2008 RESULTS: Of 10 heterologously expressed SULT isoforms examined, SULT1A1, SULT1A3/4, SULT1E1, and SULT2A1 all catalyzed the formation of APAP sulfate with K(m) values of 2.4, 1.5, 1.9, and 3.7 mM, respectively. apap sulfate 136-148 sulfotransferase family 1A member 3 Homo sapiens 73-80 18473744-2 2008 SULT1A3 has catecholamines such as dopamine as substrates while SULT 1E1 sulfonates oestrogens. Catecholamines 12-26 sulfotransferase family 1A member 3 Homo sapiens 0-7 18473744-2 2008 SULT1A3 has catecholamines such as dopamine as substrates while SULT 1E1 sulfonates oestrogens. Dopamine 35-43 sulfotransferase family 1A member 3 Homo sapiens 0-7 18473744-6 2008 SULTs 1A3 and 2A1 were less strongly inhibited by flavonoids or isoflavonoids although tricin (3",5"-dimethoxy-4",5,7-trihydroxyflavone is a competitive inhibitor of SULT 1E1 with an inhibition constant of approximately 1 nM. Flavonoids 50-60 sulfotransferase family 1A member 3 Homo sapiens 0-17 18473744-6 2008 SULTs 1A3 and 2A1 were less strongly inhibited by flavonoids or isoflavonoids although tricin (3",5"-dimethoxy-4",5,7-trihydroxyflavone is a competitive inhibitor of SULT 1E1 with an inhibition constant of approximately 1 nM. isoflavonoids 64-77 sulfotransferase family 1A member 3 Homo sapiens 0-17 18473744-6 2008 SULTs 1A3 and 2A1 were less strongly inhibited by flavonoids or isoflavonoids although tricin (3",5"-dimethoxy-4",5,7-trihydroxyflavone is a competitive inhibitor of SULT 1E1 with an inhibition constant of approximately 1 nM. tricin 87-93 sulfotransferase family 1A member 3 Homo sapiens 0-17 18393425-0 2008 STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface. Cholesterol 25-36 sulfotransferase family 1A member 3 Homo sapiens 0-3 18393425-0 2008 STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface. Dimyristoylphosphatidylcholine 59-102 sulfotransferase family 1A member 3 Homo sapiens 0-3 18393425-0 2008 STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface. Dimyristoylphosphatidylcholine 104-108 sulfotransferase family 1A member 3 Homo sapiens 0-3 18393425-0 2008 STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface. Cholesterol 110-121 sulfotransferase family 1A member 3 Homo sapiens 0-3 18393425-0 2008 STM studies of fusion of cholesterol suspensions and mixed 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol vesicles onto a Au(111) electrode surface. Gold 138-140 sulfotransferase family 1A member 3 Homo sapiens 0-3 18379081-9 2008 Enzymatic assays revealed that, five (SULT1A1, SULT1A2, SULT1A3, SULT1C4, and SULT1E1) of eleven known human SULTs tested could use CEs and methoxyestrogens (MEs) as substrates, with SULT1E1 displaying the strongest sulfating activity. Estrogens, Catechol 132-135 sulfotransferase family 1A member 3 Homo sapiens 56-63 18379081-9 2008 Enzymatic assays revealed that, five (SULT1A1, SULT1A2, SULT1A3, SULT1C4, and SULT1E1) of eleven known human SULTs tested could use CEs and methoxyestrogens (MEs) as substrates, with SULT1E1 displaying the strongest sulfating activity. 2-(N-morpholino)ethanesulfonic acid 158-161 sulfotransferase family 1A member 3 Homo sapiens 56-63 18348225-3 2008 Under the electric field produced by the STM tip, the relatively weakly bound Au surface atoms along the discommensuration lines become mobile due to the strong bond to 4-ATP, while the tendency of the porphyrins towards self-assembly result in a collective motion of gold clusters. Gold 78-80 sulfotransferase family 1A member 3 Homo sapiens 41-44 18348225-3 2008 Under the electric field produced by the STM tip, the relatively weakly bound Au surface atoms along the discommensuration lines become mobile due to the strong bond to 4-ATP, while the tendency of the porphyrins towards self-assembly result in a collective motion of gold clusters. 4-aminothiophenol 169-174 sulfotransferase family 1A member 3 Homo sapiens 41-44 18352741-1 2008 Low-temperature STM measurements combined with density functional theory calculations are employed to study the adsorption of gold on alumina/NiAl(110). Aluminum Oxide 134-141 sulfotransferase family 1A member 3 Homo sapiens 16-19 18232020-7 2008 CONCLUSIONS: The results of this study lead to the hypothesis that genetic variation in SULT1A3/4 represents a risk factor for the development of gastroschisis in the offspring of mothers exposed to APAP early in pregnancy. Acetaminophen 199-203 sulfotransferase family 1A member 3 Homo sapiens 88-95 18076172-1 2008 Recent STM molecular break-junction experiments have revealed multiple series of peaks in the conductance histograms of alkanedithiols. alkanedithiols 120-134 sulfotransferase family 1A member 3 Homo sapiens 7-10 18247438-0 2008 Electrosynthesis of poly(para)phenylene in an ionic liquid: cyclic voltammetry and in situ STM/tunnelling spectroscopy studies. poly-para-phenylene 20-39 sulfotransferase family 1A member 3 Homo sapiens 91-94 18247438-6 2008 The first in situ STM results show that the electropolymerization of benzene in the ionic liquid can be probed on the nanoscale and the band gap of the prepared polymer can be determined. Benzene 69-76 sulfotransferase family 1A member 3 Homo sapiens 18-21 18247438-6 2008 The first in situ STM results show that the electropolymerization of benzene in the ionic liquid can be probed on the nanoscale and the band gap of the prepared polymer can be determined. Polymers 51-58 sulfotransferase family 1A member 3 Homo sapiens 18-21 18352579-0 2008 Nondestructive room-temperature adsorption of 2,4,6-tri(2"-thienyl)-1,3,5-triazine on a Si-B interface: high-resolution STM imaging and molecular modeling. 2,4,6-tri(2"-thienyl)-1,3,5-triazine 46-82 sulfotransferase family 1A member 3 Homo sapiens 120-123 18041859-2 2007 The base-electrode interaction is modeled using a nucleo-base-functionalized STM probe that is pulled away from a nucleoside monolayer. Nucleosides 114-124 sulfotransferase family 1A member 3 Homo sapiens 77-80 17929849-0 2007 In situ STM study of potential-driven transitions in the film of a cationic surfactant adsorbed on a Au(111) electrode surface. Gold 101-103 sulfotransferase family 1A member 3 Homo sapiens 8-11 17929849-1 2007 Electrochemical scanning tunneling microscopy (EC-STM) has been employed to study the structure of a film formed by cationic surfactant N-decyl-N,N,N-trimethylammonium triflate (DeTATf) adsorbed on the Au(111) electrode surface. N,N,N-Trimethyldecan-1-aminium trifluoromethanesulfonate 136-176 sulfotransferase family 1A member 3 Homo sapiens 50-53 17929849-1 2007 Electrochemical scanning tunneling microscopy (EC-STM) has been employed to study the structure of a film formed by cationic surfactant N-decyl-N,N,N-trimethylammonium triflate (DeTATf) adsorbed on the Au(111) electrode surface. detatf 178-184 sulfotransferase family 1A member 3 Homo sapiens 50-53 17876860-5 2007 The grapefruit constituent, quercetin, completely inhibited SULT1A1, while quercetin and naringin both partially inhibited SULT1A3. Quercetin 75-84 sulfotransferase family 1A member 3 Homo sapiens 123-130 17876860-5 2007 The grapefruit constituent, quercetin, completely inhibited SULT1A1, while quercetin and naringin both partially inhibited SULT1A3. naringin 89-97 sulfotransferase family 1A member 3 Homo sapiens 123-130 17876860-7 2007 The tea constituents, (-)-epicatechin gallate and (-)-epigallocatechin gallate, both almost completely inhibited SULT1A1 and SULT1A3. epicatechin gallate 22-45 sulfotransferase family 1A member 3 Homo sapiens 125-132 17876860-7 2007 The tea constituents, (-)-epicatechin gallate and (-)-epigallocatechin gallate, both almost completely inhibited SULT1A1 and SULT1A3. epigallocatechin gallate 50-78 sulfotransferase family 1A member 3 Homo sapiens 125-132 19213313-1 2008 The interactions of nitrate with Cu(100) and Cu(111) in acidic solution are studied by cyclic voltammetry (CV) and in situ electrochemical scanning tunneling microscopy (EC-STM). Nitrates 20-27 sulfotransferase family 1A member 3 Homo sapiens 173-176 19213313-3 2008 EC-STM images show that the terrace of both Cu(111) and Cu(100) are atomically flat at potentials more negative than -0.7 V. The Cu(100) surface exhibits flat terraces throughout the entire cathodic potential range. Copper 44-46 sulfotransferase family 1A member 3 Homo sapiens 3-6 19213313-3 2008 EC-STM images show that the terrace of both Cu(111) and Cu(100) are atomically flat at potentials more negative than -0.7 V. The Cu(100) surface exhibits flat terraces throughout the entire cathodic potential range. Copper 56-58 sulfotransferase family 1A member 3 Homo sapiens 3-6 19213313-3 2008 EC-STM images show that the terrace of both Cu(111) and Cu(100) are atomically flat at potentials more negative than -0.7 V. The Cu(100) surface exhibits flat terraces throughout the entire cathodic potential range. Copper 56-58 sulfotransferase family 1A member 3 Homo sapiens 3-6 17908235-0 2007 Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3. Serotonin 13-22 sulfotransferase family 1A member 3 Homo sapiens 85-92 17908235-0 2007 Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3. Dopamine 27-35 sulfotransferase family 1A member 3 Homo sapiens 85-92 17908235-3 2007 A systematic study using 11 known human cytosolic SULTs revealed SULT1A3 as the responsible enzyme for the sulfation of 7-hydroxyserotonin and 6-hydroxydopamine. 7-hydroxyserotonin 120-138 sulfotransferase family 1A member 3 Homo sapiens 65-72 17908235-3 2007 A systematic study using 11 known human cytosolic SULTs revealed SULT1A3 as the responsible enzyme for the sulfation of 7-hydroxyserotonin and 6-hydroxydopamine. Oxidopamine 143-160 sulfotransferase family 1A member 3 Homo sapiens 65-72 17908235-4 2007 The pH-dependence and kinetic constants of SULT1A3 with 7-hydroxyserotonin or 6-hydroxydopamine as substrate were determined. 7-hydroxyserotonin 56-74 sulfotransferase family 1A member 3 Homo sapiens 43-50 17908235-4 2007 The pH-dependence and kinetic constants of SULT1A3 with 7-hydroxyserotonin or 6-hydroxydopamine as substrate were determined. Oxidopamine 78-95 sulfotransferase family 1A member 3 Homo sapiens 43-50 17908235-8 2007 Upon transfection of the cells with siRNAs targeted at SULT1A3, diminishment of the SULT1A3 protein and concomitantly the sulfating activity toward these hydroxylated monoamines was observed. monoamines 167-177 sulfotransferase family 1A member 3 Homo sapiens 55-62 17908235-8 2007 Upon transfection of the cells with siRNAs targeted at SULT1A3, diminishment of the SULT1A3 protein and concomitantly the sulfating activity toward these hydroxylated monoamines was observed. monoamines 167-177 sulfotransferase family 1A member 3 Homo sapiens 84-91 17908235-10 2007 By serving as substrates for SULT1A3, these hydroxylated monoamines may interfere with the homeostasis of endogenous serotonin and dopamine. monoamines 57-67 sulfotransferase family 1A member 3 Homo sapiens 29-36 17908235-10 2007 By serving as substrates for SULT1A3, these hydroxylated monoamines may interfere with the homeostasis of endogenous serotonin and dopamine. Serotonin 117-126 sulfotransferase family 1A member 3 Homo sapiens 29-36 17908235-10 2007 By serving as substrates for SULT1A3, these hydroxylated monoamines may interfere with the homeostasis of endogenous serotonin and dopamine. Dopamine 131-139 sulfotransferase family 1A member 3 Homo sapiens 29-36 17803325-1 2007 This work presents characteristics of Pt deposits on Au(111) obtained by the use of spontaneous deposition and investigated by electrochemical scanning tunneling microscopy (EC-STM). Gold 53-55 sulfotransferase family 1A member 3 Homo sapiens 177-180 17956109-1 2007 NMR and STM studies revealed that the hydrazide-quinolinone-based building block 5 exhibited a monomer-dimer-polymer equilibrium, while its acyclic analogue 6, due to conformational flexibility, exhibited a more complicated mode of aggregation and formed a gel in dichloromethane/hexane. Quinolones 48-59 sulfotransferase family 1A member 3 Homo sapiens 8-11 17692935-3 2007 Thus, post-training administration of 8-OHDPAT (agonist for 5-HT(1A/7) receptors) only at 0.250 and 0.500 mg/kg impaired both STM and LTM. 8-Hydroxy-2-(di-n-propylamino)tetralin 38-46 sulfotransferase family 1A member 3 Homo sapiens 126-129 17692935-4 2007 CGS12066 (agonist for 5-HT(1B)) produced biphasic affects, at 5.0 mg/kg impaired STM but at 1.0 and 10.0 mg/kg, respectively, improved or impaired LTM. CGS 12066B 0-8 sulfotransferase family 1A member 3 Homo sapiens 81-84 17692935-6 2007 Both, STM and LTM were impaired by either mCPP (mainly agonist for 5-HT(2C) receptors) or mesulergine (mainly antagonist for 5-HT(2C) receptors) lower dose. 1-(3-chlorophenyl)piperazine 42-46 sulfotransferase family 1A member 3 Homo sapiens 6-9 17692935-6 2007 Both, STM and LTM were impaired by either mCPP (mainly agonist for 5-HT(2C) receptors) or mesulergine (mainly antagonist for 5-HT(2C) receptors) lower dose. mesulergine 90-101 sulfotransferase family 1A member 3 Homo sapiens 6-9 17692935-9 2007 The higher dose of fluoxetine (a 5-HT uptake inhibitor) improved both STM and LTM. Fluoxetine 19-29 sulfotransferase family 1A member 3 Homo sapiens 70-73 17803325-2 2007 On such prepared and STM characterized Au(111)/Pt surfaces, we studied electrocatalytic oxidation of formic acid and methanol. Gold 39-41 sulfotransferase family 1A member 3 Homo sapiens 21-24 17803325-2 2007 On such prepared and STM characterized Au(111)/Pt surfaces, we studied electrocatalytic oxidation of formic acid and methanol. Platinum 47-49 sulfotransferase family 1A member 3 Homo sapiens 21-24 17803325-2 2007 On such prepared and STM characterized Au(111)/Pt surfaces, we studied electrocatalytic oxidation of formic acid and methanol. formic acid 101-112 sulfotransferase family 1A member 3 Homo sapiens 21-24 17891604-5 2007 Recent studies have revealed that the sulfation of nitrotyrosine occurs in cells under oxidative/nitrative stress, and have pinpointed the SULT1A3 as the responsible SULT enzyme. 3-nitrotyrosine 51-64 sulfotransferase family 1A member 3 Homo sapiens 139-146 17891604-6 2007 In this review, we summarized the available information concerning the biochemistry of nitrotyrosine sulfation and the effects of genetic polymorphisms on the nitrotyrosine sulfating activity of SULT1A3. 3-nitrotyrosine 159-172 sulfotransferase family 1A member 3 Homo sapiens 195-202 17622126-7 2007 STM measurement of 2 in the Cu(100) surface revealed that it takes several discrete conformations with respect to the relative orientation of neighboring diporphyrins. Copper 28-30 sulfotransferase family 1A member 3 Homo sapiens 0-3 17561347-1 2007 We report the STM observation of single diarylethene derivatives (DD) embedded into alkylthiol self-assembled monolayers (SAM) on Au(111). diarylethene 40-52 sulfotransferase family 1A member 3 Homo sapiens 14-17 17561347-1 2007 We report the STM observation of single diarylethene derivatives (DD) embedded into alkylthiol self-assembled monolayers (SAM) on Au(111). dd 66-68 sulfotransferase family 1A member 3 Homo sapiens 14-17 17561347-1 2007 We report the STM observation of single diarylethene derivatives (DD) embedded into alkylthiol self-assembled monolayers (SAM) on Au(111). alkylthiol 84-94 sulfotransferase family 1A member 3 Homo sapiens 14-17 17561347-1 2007 We report the STM observation of single diarylethene derivatives (DD) embedded into alkylthiol self-assembled monolayers (SAM) on Au(111). Gold 130-132 sulfotransferase family 1A member 3 Homo sapiens 14-17 17622126-7 2007 STM measurement of 2 in the Cu(100) surface revealed that it takes several discrete conformations with respect to the relative orientation of neighboring diporphyrins. diporphyrins 154-166 sulfotransferase family 1A member 3 Homo sapiens 0-3 18019136-0 2007 STM investigation of substitute effect on oligothiophene adlayer at Au(111) substrate. oligothiophene 42-56 sulfotransferase family 1A member 3 Homo sapiens 0-3 18019136-1 2007 Molecular adlayers of a series of oligothiophenes with carboxylic groups and alkyl substitutes, DTDA, TTDA, QTDA, and PTDA, are investigated by STM at Au(111) surface. oligothiophenes 34-49 sulfotransferase family 1A member 3 Homo sapiens 144-147 17655297-1 2007 Nitrate adsorption and reduction on Cu(100) in acidic solution is studied by electrochemical methods, in situ electrochemical scanning tunneling microscopy (EC-STM), surface enhanced Raman spectroscopy (SERS), and density functional theory (DFT) calculations. Nitrates 0-7 sulfotransferase family 1A member 3 Homo sapiens 160-163 17655297-2 2007 Electrochemical results show that reduction of nitrate starts at -0.3 V vs Ag/AgCl and reaches maximum value at -0.58 V. Over the entire potential region interrogated adlayers composed of nitrate, nitrite, or other intermediates are observed by using in situ STM. Nitrates 47-54 sulfotransferase family 1A member 3 Homo sapiens 259-262 17628085-7 2007 In particular, atomic-scale STM imaging suggested a change from a defected, but essentially graphitic, surface in the first regime to an amorphous carbon surface in the second regime. Carbon 147-153 sulfotransferase family 1A member 3 Homo sapiens 28-31 17654760-0 2007 STM vizualization of thiol-containing peptide dendrimers on Au(111). Sulfhydryl Compounds 21-26 sulfotransferase family 1A member 3 Homo sapiens 0-3 17579737-0 2007 In situ STM investigation of spinodal decomposition and surface alloying during underpotential deposition of Cd on Au(111) from an ionic liquid. Cadmium 109-111 sulfotransferase family 1A member 3 Homo sapiens 8-11 17548063-0 2007 Regioselective sulfonation of dopamine by SULT1A3 in vitro provides a molecular explanation for the preponderance of dopamine-3-O-sulfate in human blood circulation. Dopamine 30-38 sulfotransferase family 1A member 3 Homo sapiens 42-49 17548063-0 2007 Regioselective sulfonation of dopamine by SULT1A3 in vitro provides a molecular explanation for the preponderance of dopamine-3-O-sulfate in human blood circulation. dopamine 3-O-sulfate 117-137 sulfotransferase family 1A member 3 Homo sapiens 42-49 17548063-1 2007 SULT1A3 is an enzyme that catalyzes the sulfonation of many endogenous and exogenous phenols and catechols. Phenols 85-92 sulfotransferase family 1A member 3 Homo sapiens 0-7 17548063-1 2007 SULT1A3 is an enzyme that catalyzes the sulfonation of many endogenous and exogenous phenols and catechols. Catechols 97-106 sulfotransferase family 1A member 3 Homo sapiens 0-7 17548063-2 2007 The most important endogenous substrate is dopamine (DA), which is often used as a probe substrate for SULT1A3. Dopamine 43-51 sulfotransferase family 1A member 3 Homo sapiens 103-110 17548063-2 2007 The most important endogenous substrate is dopamine (DA), which is often used as a probe substrate for SULT1A3. Dopamine 53-55 sulfotransferase family 1A member 3 Homo sapiens 103-110 17548063-8 2007 We determined the enzyme kinetic parameters for formation of DA-3-O-sulfate and DA-4-O-sulfate using purified recombinant human SULT1A3. dopamine 3-O-sulfate 61-75 sulfotransferase family 1A member 3 Homo sapiens 128-135 17548063-8 2007 We determined the enzyme kinetic parameters for formation of DA-3-O-sulfate and DA-4-O-sulfate using purified recombinant human SULT1A3. dopamine 4-O-sulfate 80-94 sulfotransferase family 1A member 3 Homo sapiens 128-135 17548063-11 2007 These results are in accordance with the observation that DA-3-O-sulfate is more abundant in human blood than DA-4-O-sulfate and that in the crystal structure of SULT1A3 with dopamine bound to the active site, the 3-hydroxy group is aligned to form hydrogen bonds with catalytic residues of the enzyme. dopamine 3-O-sulfate 58-72 sulfotransferase family 1A member 3 Homo sapiens 162-169 17548063-11 2007 These results are in accordance with the observation that DA-3-O-sulfate is more abundant in human blood than DA-4-O-sulfate and that in the crystal structure of SULT1A3 with dopamine bound to the active site, the 3-hydroxy group is aligned to form hydrogen bonds with catalytic residues of the enzyme. dopamine 4-O-sulfate 110-124 sulfotransferase family 1A member 3 Homo sapiens 162-169 17548063-11 2007 These results are in accordance with the observation that DA-3-O-sulfate is more abundant in human blood than DA-4-O-sulfate and that in the crystal structure of SULT1A3 with dopamine bound to the active site, the 3-hydroxy group is aligned to form hydrogen bonds with catalytic residues of the enzyme. Dopamine 175-183 sulfotransferase family 1A member 3 Homo sapiens 162-169 17548063-11 2007 These results are in accordance with the observation that DA-3-O-sulfate is more abundant in human blood than DA-4-O-sulfate and that in the crystal structure of SULT1A3 with dopamine bound to the active site, the 3-hydroxy group is aligned to form hydrogen bonds with catalytic residues of the enzyme. Hydrogen 249-257 sulfotransferase family 1A member 3 Homo sapiens 162-169 17677710-0 2007 Atomic row doubling in the STM images of Cu(014)-O obtained with MnNi tips. Copper 41-43 sulfotransferase family 1A member 3 Homo sapiens 27-30 17002600-0 2007 Generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible. nitrotyrosine O-sulfate 26-49 sulfotransferase family 1A member 3 Homo sapiens 122-129 17464396-0 2007 Copper sulfide nanostripe patterns at the Au(111)/electrolyte interface studied by in situ STM. cupric sulfide 0-14 sulfotransferase family 1A member 3 Homo sapiens 91-94 17530069-1 2007 Fibres of [Ru(2)Br(micro-O(2)CEt)4]n polymer have been isolated on different surfaces under specific conditions, and morphologically characterised by AFM and STM, showing an unexpected helical internal structure. [ru(2)br(micro-o(2)cet)4]n polymer 10-44 sulfotransferase family 1A member 3 Homo sapiens 158-161 17204552-12 2007 T1AM, the most active thyronamine pharmacologically, was associated with the greatest SULT activity of the thyronamines tested in the liver pool and in both the expressed SULT1A3 and SULT1E1 preparations. T1AM 0-4 sulfotransferase family 1A member 3 Homo sapiens 171-178 17269652-2 2007 The self-assembled monolayer of PAHs was investigated by STM and was used in the electrochemical detection of nitroaromatic compounds (NACs). Polycyclic Aromatic Hydrocarbons 32-36 sulfotransferase family 1A member 3 Homo sapiens 57-60 17263340-6 2007 Orientational control of the scaffold protein STM, a triply mutated form of the stable intracellular protein inhibitor stefin A is achieved with a surface cysteine residue, which leads to the presentation of the scaffold recognition surface to solution. Cysteine 155-163 sulfotransferase family 1A member 3 Homo sapiens 46-49 17368430-3 2007 As previously reported ketamine (glutamatergic antagonist) and two well-known amnesic drugs, scopolamine (cholinergic antagonist) and dizocilpine (NMDA antagonist) impaired STM but not LTM; dizocilpine even improved the latter. Ketamine 23-31 sulfotransferase family 1A member 3 Homo sapiens 173-176 17368430-3 2007 As previously reported ketamine (glutamatergic antagonist) and two well-known amnesic drugs, scopolamine (cholinergic antagonist) and dizocilpine (NMDA antagonist) impaired STM but not LTM; dizocilpine even improved the latter. Scopolamine 93-104 sulfotransferase family 1A member 3 Homo sapiens 173-176 17368430-3 2007 As previously reported ketamine (glutamatergic antagonist) and two well-known amnesic drugs, scopolamine (cholinergic antagonist) and dizocilpine (NMDA antagonist) impaired STM but not LTM; dizocilpine even improved the latter. Dizocilpine Maleate 134-145 sulfotransferase family 1A member 3 Homo sapiens 173-176 17368430-4 2007 Since ketamine produces hallucinations and impairs memory in humans, we address the question if well-known antipsychotic haloperidol and clozapine might affect STM deficit. Clozapine 137-146 sulfotransferase family 1A member 3 Homo sapiens 160-163 17368430-5 2007 Indeed, systemic administration of clozapine<haloperidol reversed the ketamine-STM deficit. Clozapine 35-44 sulfotransferase family 1A member 3 Homo sapiens 82-85 17368430-5 2007 Indeed, systemic administration of clozapine<haloperidol reversed the ketamine-STM deficit. Leu-Thr 45-47 sulfotransferase family 1A member 3 Homo sapiens 82-85 17368430-5 2007 Indeed, systemic administration of clozapine<haloperidol reversed the ketamine-STM deficit. Haloperidol 48-59 sulfotransferase family 1A member 3 Homo sapiens 82-85 17368430-5 2007 Indeed, systemic administration of clozapine<haloperidol reversed the ketamine-STM deficit. Ketamine 73-81 sulfotransferase family 1A member 3 Homo sapiens 82-85 17368430-7 2007 The ketamine STM-induced deficit was blocked by 8-OHDPAT (5-HT(1A/7) agonist) and SB-399885 (a 5-HT(6) antagonist) but not by 5-HT(1B), 5-HT(2) and 5-HT(7) antagonists, thus implicating 5-HT(1A/7) and 5-HT(6) receptors. Ketamine 4-12 sulfotransferase family 1A member 3 Homo sapiens 13-16 17368430-7 2007 The ketamine STM-induced deficit was blocked by 8-OHDPAT (5-HT(1A/7) agonist) and SB-399885 (a 5-HT(6) antagonist) but not by 5-HT(1B), 5-HT(2) and 5-HT(7) antagonists, thus implicating 5-HT(1A/7) and 5-HT(6) receptors. 8-Hydroxy-2-(di-n-propylamino)tetralin 48-56 sulfotransferase family 1A member 3 Homo sapiens 13-16 17253654-1 2007 The monolayer growth of pyrimido-pentaphenylbenzene (NPB) on Cu(111) is investigated by means of low-temperature scanning tunneling microscopy (LT-STM). pyrimido-pentaphenylbenzene 24-51 sulfotransferase family 1A member 3 Homo sapiens 147-150 17241047-0 2007 STM study on 2D molecular assemblies of luminescent quinacridone derivatives: structure fine-tuned by introducing bulky substitutes and co-adsorption with monofunctional/bifunctional acid. quinacridone 52-64 sulfotransferase family 1A member 3 Homo sapiens 0-3 17002600-6 2007 Of the 11 enzymes tested, only SULT1A3 displayed sulfating activity toward nitrotyrosine. 3-nitrotyrosine 75-88 sulfotransferase family 1A member 3 Homo sapiens 31-38 17002600-7 2007 The pH-dependence and kinetic constants of SULT1A3 with nitrotyrosine or dopamine as substrate were determined. 3-nitrotyrosine 56-69 sulfotransferase family 1A member 3 Homo sapiens 43-50 17002600-7 2007 The pH-dependence and kinetic constants of SULT1A3 with nitrotyrosine or dopamine as substrate were determined. Dopamine 73-81 sulfotransferase family 1A member 3 Homo sapiens 43-50 17129057-0 2006 Molecular adsorption at well-defined electrode surfaces: hydroquinone on Pd(111) studied by EC-STM. hydroquinone 57-69 sulfotransferase family 1A member 3 Homo sapiens 95-98 17280227-1 2006 Stark-shifted image-potential states were measured with an STM tip for benzene adsorbed on a Cu(111) surface. Benzene 71-78 sulfotransferase family 1A member 3 Homo sapiens 59-62 17149917-0 2006 X-ray diffraction and STM study of reactive surfaces under electrochemical control: Cl and I on Cu(100). Copper 96-98 sulfotransferase family 1A member 3 Homo sapiens 22-25 17129057-1 2006 The interaction of hydroquinone (H2Q) with well-defined Pd(111) surfaces at preselected potentials in dilute H2SO4 has been studied by molecule-resolved electrochemical scanning tunneling microscopy (EC-STM). hydroquinone 19-31 sulfotransferase family 1A member 3 Homo sapiens 203-206 17129057-1 2006 The interaction of hydroquinone (H2Q) with well-defined Pd(111) surfaces at preselected potentials in dilute H2SO4 has been studied by molecule-resolved electrochemical scanning tunneling microscopy (EC-STM). (2~{R})-4-[6-[4-[1-(hydroxymethyl)cyclopropyl]buta-1,3-diynyl]-3-oxidanylidene-1~{H}-pyrrolo[1,2-c]imidazol-2-yl]-2-methyl-2-methylsulfonyl-~{N}-oxidanyl-butanamide 33-36 sulfotransferase family 1A member 3 Homo sapiens 203-206 17155753-3 2006 By desorbing this hydrogen atom with the STM tip, the interaction of the molecule with the surface is modified such that it becomes transformed into a multistable device with four stable states having switching yields increased by almost 2 orders of magnitude. Hydrogen 18-26 sulfotransferase family 1A member 3 Homo sapiens 41-44 17125315-2 2006 STM images, collected at 77 K, revealed an unreconstructed 1 x 1 structure for the chlorination layer, consistent with what has been observed for the gas phase chlorination of H-terminated Si(111). Silicon 189-191 sulfotransferase family 1A member 3 Homo sapiens 0-3 17090013-0 2006 Electric field-induced isomerization of azobenzene by STM. azobenzene 40-50 sulfotransferase family 1A member 3 Homo sapiens 54-57 17155271-2 2006 Based on STM measurements and density-functional theory calculations, a new model for the low-coverage self-assembled monolayer of alkanethiolate on the Au(111) surface is developed, which involves the adsorbate complexes incorporating Au adatoms. alkanethiolate 131-145 sulfotransferase family 1A member 3 Homo sapiens 9-12 17155558-2 2006 Large scale STM images are employed to quantify the layer population, i.e., the fraction of the surface area covered by different Pb thicknesses, directly in the real space as a function of temperature. Lead 130-132 sulfotransferase family 1A member 3 Homo sapiens 12-15 17155577-1 2006 Electron stimulated desorption of cyclopentene from the Si(100)-(2 x 1) surface is studied experimentally with cryogenic UHV STM and theoretically with transport, electronic structure, and dynamical calculations. Cyclopentanes 34-46 sulfotransferase family 1A member 3 Homo sapiens 125-128 17155577-1 2006 Electron stimulated desorption of cyclopentene from the Si(100)-(2 x 1) surface is studied experimentally with cryogenic UHV STM and theoretically with transport, electronic structure, and dynamical calculations. si(100) 56-63 sulfotransferase family 1A member 3 Homo sapiens 125-128 17048940-0 2006 Methanethiolate adsorption site on Au(111): a combined STM/DFT study at the single-molecule level. methylmercaptan 0-15 sulfotransferase family 1A member 3 Homo sapiens 55-58 17048940-0 2006 Methanethiolate adsorption site on Au(111): a combined STM/DFT study at the single-molecule level. Gold 35-37 sulfotransferase family 1A member 3 Homo sapiens 55-58 17048940-1 2006 The chemisorptive bonding of methanethiolate (CH(3)S) on the Au(111) surface has been investigated at a single-molecule level using low-temperature scanning tunneling microscopy (LT-STM) and density functional theory (DFT). methylmercaptan 29-44 sulfotransferase family 1A member 3 Homo sapiens 182-185 17048940-1 2006 The chemisorptive bonding of methanethiolate (CH(3)S) on the Au(111) surface has been investigated at a single-molecule level using low-temperature scanning tunneling microscopy (LT-STM) and density functional theory (DFT). methyl radical 46-53 sulfotransferase family 1A member 3 Homo sapiens 182-185 17048940-2 2006 The CH(3)S species were produced by STM-tip-induced dissociation of methanethiol (CH(3)SH) or dimethyl disulfide (CH(3)SSCH(3)) at 5 K. The adsorption site of an isolated CH(3)S species was assigned by comparing the experimental and calculated STM images. methylmercaptan 68-80 sulfotransferase family 1A member 3 Homo sapiens 36-39 17048940-2 2006 The CH(3)S species were produced by STM-tip-induced dissociation of methanethiol (CH(3)SH) or dimethyl disulfide (CH(3)SSCH(3)) at 5 K. The adsorption site of an isolated CH(3)S species was assigned by comparing the experimental and calculated STM images. dimethyl disulfide 94-112 sulfotransferase family 1A member 3 Homo sapiens 36-39 17034175-1 2006 Low-temperature STM observations of the low-coverage chemisorption behavior of iodobenzene on Cu(110) are presented at two annealing temperatures. iodobenzene 79-90 sulfotransferase family 1A member 3 Homo sapiens 16-19 17034175-1 2006 Low-temperature STM observations of the low-coverage chemisorption behavior of iodobenzene on Cu(110) are presented at two annealing temperatures. Copper 94-96 sulfotransferase family 1A member 3 Homo sapiens 16-19 17034175-3 2006 An STM tip-induced dissociation reaction is used to determine that the individual units in the chains are composed of pairs of iodobenzene molecules. iodobenzene 127-138 sulfotransferase family 1A member 3 Homo sapiens 3-6 16984169-1 2006 We evidence by STM that 2-naphthalenethiol self-assembled monolayers formed at the n-tetradecane/Au(111) interface coexist as two structural phases which both possess molecules into two different orientations (standing and lying). 2-naphthalenethiol 24-42 sulfotransferase family 1A member 3 Homo sapiens 15-18 17002376-3 2006 In a background of 10 Torr of benzene, STM is able to image small ordered regions corresponding to the c(2 radical3 x 3)rect structure in which each molecule is chemisorbed at a bridge site. Benzene 30-37 sulfotransferase family 1A member 3 Homo sapiens 39-42 16984169-1 2006 We evidence by STM that 2-naphthalenethiol self-assembled monolayers formed at the n-tetradecane/Au(111) interface coexist as two structural phases which both possess molecules into two different orientations (standing and lying). n-tetradecane 83-96 sulfotransferase family 1A member 3 Homo sapiens 15-18 16952267-4 2006 The structure of Os deposits on Pt(111) was characterized and quantified by in situ STM and stripping voltammetry. Osmium 17-19 sulfotransferase family 1A member 3 Homo sapiens 84-87 16922536-0 2006 Homo- and heteroassemblies of lactim/lactam recognition patterns on highly ordered pyrolytic graphite: An STM investigation. Lactams 37-43 sulfotransferase family 1A member 3 Homo sapiens 106-109 17028707-4 2006 In situ STM shows many small pits in the dense adlayers uniformly spread over the surface, which is a typical feature of self-assembled monolayers (SAMs) of alkanethiols. SAMS Peptide 148-152 sulfotransferase family 1A member 3 Homo sapiens 8-11 17028707-4 2006 In situ STM shows many small pits in the dense adlayers uniformly spread over the surface, which is a typical feature of self-assembled monolayers (SAMs) of alkanethiols. alkanethiols 157-169 sulfotransferase family 1A member 3 Homo sapiens 8-11 16922536-0 2006 Homo- and heteroassemblies of lactim/lactam recognition patterns on highly ordered pyrolytic graphite: An STM investigation. Graphite 93-101 sulfotransferase family 1A member 3 Homo sapiens 106-109 16800507-0 2006 Role of conformation in the electronic properties of chemisorbed pyridine on Cu(110): an STM/STS study. pyridine 65-73 sulfotransferase family 1A member 3 Homo sapiens 89-92 16800507-1 2006 Pyridine was chemisorbed on Cu(110) at 10 K and observed using STM at 5 K as dosed and after annealing to temperatures between 20 and 300 K. At very low coverage, two molecular species with different apparent heights are observed to coexist. pyridine 0-8 sulfotransferase family 1A member 3 Homo sapiens 63-66 16673444-0 2006 From a lamellar to hexagonal self-assembly of bis(4,4"-(m,m"-di(dodecyloxy)phenyl)-2,2"-difluoro-1,3,2-dioxaborin) molecules: a trans-to-cis-isomerization-induced structural transition studied with STM. bis(4,4"-(m,m"-di(dodecyloxy)phenyl)-2,2"-difluoro-1,3,2-dioxaborin) 46-114 sulfotransferase family 1A member 3 Homo sapiens 198-201 16768498-4 2006 These complexes assemble into ordered arrays at the interface of 1-phenyloctane and the highly oriented pyrolytic graphite surface, owing to the affinity of the long alkyl chains toward the surface, as revealed by means of scanning tunneling microscopy (STM) with molecular resolution. n-octylbenzene 65-79 sulfotransferase family 1A member 3 Homo sapiens 254-257 16768498-4 2006 These complexes assemble into ordered arrays at the interface of 1-phenyloctane and the highly oriented pyrolytic graphite surface, owing to the affinity of the long alkyl chains toward the surface, as revealed by means of scanning tunneling microscopy (STM) with molecular resolution. Graphite 114-122 sulfotransferase family 1A member 3 Homo sapiens 254-257 16803324-1 2006 An intriguing growth morphology of Pb islands on a Si(111) surface is observed in our STM experiments: the growth of a Pb layer on Pb islands with unstable heights starts from the periphery and moves towards the center, while the nucleation of the next layer on stable Pb islands starts away from the periphery. Lead 35-37 sulfotransferase family 1A member 3 Homo sapiens 86-89 16803324-1 2006 An intriguing growth morphology of Pb islands on a Si(111) surface is observed in our STM experiments: the growth of a Pb layer on Pb islands with unstable heights starts from the periphery and moves towards the center, while the nucleation of the next layer on stable Pb islands starts away from the periphery. Silicon 51-53 sulfotransferase family 1A member 3 Homo sapiens 86-89 16803324-1 2006 An intriguing growth morphology of Pb islands on a Si(111) surface is observed in our STM experiments: the growth of a Pb layer on Pb islands with unstable heights starts from the periphery and moves towards the center, while the nucleation of the next layer on stable Pb islands starts away from the periphery. Lead 119-121 sulfotransferase family 1A member 3 Homo sapiens 86-89 16803324-1 2006 An intriguing growth morphology of Pb islands on a Si(111) surface is observed in our STM experiments: the growth of a Pb layer on Pb islands with unstable heights starts from the periphery and moves towards the center, while the nucleation of the next layer on stable Pb islands starts away from the periphery. Lead 119-121 sulfotransferase family 1A member 3 Homo sapiens 86-89 16803324-1 2006 An intriguing growth morphology of Pb islands on a Si(111) surface is observed in our STM experiments: the growth of a Pb layer on Pb islands with unstable heights starts from the periphery and moves towards the center, while the nucleation of the next layer on stable Pb islands starts away from the periphery. Lead 119-121 sulfotransferase family 1A member 3 Homo sapiens 86-89 16732637-2 2006 The statistical analysis of the conductance values show that the alpha,omega-alkanedithiol molecule trapped in the STM break junction can adopt two distinct geometries that result in "lower" and "higher" conductivity values. alpha,omega-alkanedithiol 65-90 sulfotransferase family 1A member 3 Homo sapiens 115-118 16708048-10 2006 CONCLUSIONS: In conclusion, we demonstrated that NAT1, SULT1A1 and SULT1A3 are present in human prostate and that both enzyme classes significantly contribute to the activation of N-hydroxylated heterocyclic amines to DNA-damaging species in this tissue. Amines 208-214 sulfotransferase family 1A member 3 Homo sapiens 67-74 16732637-5 2006 Moreover when the STM tip is polarized to electrochemical potential preventing a chemical reaction between the terminal -SH group and Au, only "lower" conductivity values are observed for alpha,omega-alkaneditiols. Gold 134-136 sulfotransferase family 1A member 3 Homo sapiens 18-21 16732637-5 2006 Moreover when the STM tip is polarized to electrochemical potential preventing a chemical reaction between the terminal -SH group and Au, only "lower" conductivity values are observed for alpha,omega-alkaneditiols. alpha,omega-alkaneditiols 188-213 sulfotransferase family 1A member 3 Homo sapiens 18-21 26626686-5 2006 Energetic criteria show also that the STM tip (made from Pt and Ir alloys) immersed into a bromine solution may contain only dissociated bromine atoms that bind strongly with the surface Pt atoms. Bromine 91-98 sulfotransferase family 1A member 3 Homo sapiens 38-41 26626686-5 2006 Energetic criteria show also that the STM tip (made from Pt and Ir alloys) immersed into a bromine solution may contain only dissociated bromine atoms that bind strongly with the surface Pt atoms. Bromine 137-144 sulfotransferase family 1A member 3 Homo sapiens 38-41 26626686-5 2006 Energetic criteria show also that the STM tip (made from Pt and Ir alloys) immersed into a bromine solution may contain only dissociated bromine atoms that bind strongly with the surface Pt atoms. Platinum 57-59 sulfotransferase family 1A member 3 Homo sapiens 38-41 16548552-0 2006 STM study of mixed alkanethiol/biphenylthiol self-assembled monolayers on Au(111). Gold 74-76 sulfotransferase family 1A member 3 Homo sapiens 0-3 16551059-1 2006 Recently, we reported STM images of the methylated Si(111) surface [prepared through chlorination-alkylation of the Si(111)-H surface] taken at 4.7 K, indicating that the torsion angle of the methyl group with respect to the subsurface silicon layer is phi = 23 +/- 3 degrees . Silicon 51-53 sulfotransferase family 1A member 3 Homo sapiens 22-25 16551059-1 2006 Recently, we reported STM images of the methylated Si(111) surface [prepared through chlorination-alkylation of the Si(111)-H surface] taken at 4.7 K, indicating that the torsion angle of the methyl group with respect to the subsurface silicon layer is phi = 23 +/- 3 degrees . Silicon 116-118 sulfotransferase family 1A member 3 Homo sapiens 22-25 16551059-1 2006 Recently, we reported STM images of the methylated Si(111) surface [prepared through chlorination-alkylation of the Si(111)-H surface] taken at 4.7 K, indicating that the torsion angle of the methyl group with respect to the subsurface silicon layer is phi = 23 +/- 3 degrees . Silicon 236-243 sulfotransferase family 1A member 3 Homo sapiens 22-25 16548552-0 2006 STM study of mixed alkanethiol/biphenylthiol self-assembled monolayers on Au(111). alkanethiol/biphenylthiol 19-44 sulfotransferase family 1A member 3 Homo sapiens 0-3 16548552-8 2006 The decay constant beta for the phenylene groups is deduced from the apparent STM heights of the inserted BP4 islands compared to the STM heights of the C12 closely packed monolayers. Phenylephrine 32-41 sulfotransferase family 1A member 3 Homo sapiens 78-81 16608279-1 2006 Current-voltage characteristics measured using STM on fullerene-like WS2 nanoparticles show zero-bias current and contain segments in which the tunneling current flows opposite to the applied bias voltage. Fullerenes 54-63 sulfotransferase family 1A member 3 Homo sapiens 47-50 16548552-8 2006 The decay constant beta for the phenylene groups is deduced from the apparent STM heights of the inserted BP4 islands compared to the STM heights of the C12 closely packed monolayers. Phenylephrine 32-41 sulfotransferase family 1A member 3 Homo sapiens 134-137 16853029-1 2005 The adsorption of methanethiol and n-propanethiol on the Au(111) surface has been studied by temperature-programmed desorption (TPD), Auger electron spectroscopy (AES), and low-temperature scanning tunneling microscopy (LT-STM). methylmercaptan 18-30 sulfotransferase family 1A member 3 Homo sapiens 223-226 16460059-0 2006 Influence of halogen substituents on the self-assembly of oligothiophenes--a combined STM and theoretical approach. oligothiophenes 58-73 sulfotransferase family 1A member 3 Homo sapiens 86-89 16460082-6 2006 The effect of hydrogen bonds in self-assembled molecules of N,N"-dialkylurea CH3-(CH2)m-NHCONH-(CH2)n-CH3 (m + n = 14) [7 (n = 2)] was visualized by STM at the octylbenzene/graphite interface. n-octylbenzene 160-172 sulfotransferase family 1A member 3 Homo sapiens 149-152 16460082-6 2006 The effect of hydrogen bonds in self-assembled molecules of N,N"-dialkylurea CH3-(CH2)m-NHCONH-(CH2)n-CH3 (m + n = 14) [7 (n = 2)] was visualized by STM at the octylbenzene/graphite interface. Graphite 173-181 sulfotransferase family 1A member 3 Homo sapiens 149-152 16461835-4 2006 The transfer function from STM to AP was identified by a white noise system identification method in 12 sevoflurane-anesthetized patients undergoing orthopedic surgery involving the cervical vertebrae, and the feedback correction factors were determined with a numerical simulation to enable the BBS to quickly and stably attenuate an external disturbance on AP. Sevoflurane 104-115 sulfotransferase family 1A member 3 Homo sapiens 27-30 16486600-1 2006 Direct in situ studies of the surface diffusion of isolated adsorbates at an electrochemical interface by high-speed scanning tunneling microscopy (video STM) are presented for sulfide adsorbates on Cu(100) in HCl solution. Sulfides 177-184 sulfotransferase family 1A member 3 Homo sapiens 154-157 16486601-2 2006 Remarkable details, corresponding to the passage of phasons through the tunnel junction, are detected by the STM within the short span between two atoms comprising an individual Si dimer. Silicon 178-180 sulfotransferase family 1A member 3 Homo sapiens 109-112 16486501-1 2006 A d-wave, Eliashberg analysis of break-junction and STM tunneling spectra on Bi2Sr2CaCu2O(8+delta) (Bi2212) reveals that the spectral dip feature is directly linked to strong electronic coupling to a narrow boson spectrum, evidenced by a large peak in alpha2F(omega). boson 207-212 sulfotransferase family 1A member 3 Homo sapiens 52-55 16512369-3 2006 Here we report the use of a logarithmic current-to-voltage converter to examine a wide range of currents in an STM break junction study of octanedithiol, clearly showing both the gold-quantum wire regime and the single molecule conductance regime. octanedithiol 139-152 sulfotransferase family 1A member 3 Homo sapiens 111-114 16375360-0 2005 In situ STM study of potential-dependent height change of a tetrathiafulvalene derivative embedded in alkanethiol self-assembled monolayers on Au(111). tetrathiafulvalene 60-78 sulfotransferase family 1A member 3 Homo sapiens 8-11 16375360-0 2005 In situ STM study of potential-dependent height change of a tetrathiafulvalene derivative embedded in alkanethiol self-assembled monolayers on Au(111). alkanethiol 102-113 sulfotransferase family 1A member 3 Homo sapiens 8-11 16375360-0 2005 In situ STM study of potential-dependent height change of a tetrathiafulvalene derivative embedded in alkanethiol self-assembled monolayers on Au(111). Gold 143-145 sulfotransferase family 1A member 3 Homo sapiens 8-11 16261236-1 2005 Thiol- and thiophene-functionalized SWNTs prepared via the reaction of a substituted amine with fluoronanotubes show similar levels of sidewall functionalization, however, the use of Au nanoparticles as chemical markers for AFM gives misleading results for substituent distribution since STM shows the thiol substituents grouped in bands while the thiophene substituents uniformly distributed along the SWNTs. Sulfhydryl Compounds 0-5 sulfotransferase family 1A member 3 Homo sapiens 288-291 16261236-1 2005 Thiol- and thiophene-functionalized SWNTs prepared via the reaction of a substituted amine with fluoronanotubes show similar levels of sidewall functionalization, however, the use of Au nanoparticles as chemical markers for AFM gives misleading results for substituent distribution since STM shows the thiol substituents grouped in bands while the thiophene substituents uniformly distributed along the SWNTs. Thiophenes 11-20 sulfotransferase family 1A member 3 Homo sapiens 288-291 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. formic acid 98-105 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. (2r,3s,5r,7s)-2-(Pyridin-3-Yl)-1-Azatricyclo[3.3.1.1~3,7~]decane 130-133 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. formic acid 147-154 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. Oxygen 161-167 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. Oxygen 189-195 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. formic acid 147-154 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. formic acid 147-154 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. Oxygen 189-195 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. formic acid 147-154 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. Oxygen 189-195 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. Oxygen 189-195 sulfotransferase family 1A member 3 Homo sapiens 11-14 16853423-3 2005 Successive STM observations revealed transformations among the three configurations, i.e., bridge formate on a 5-fold coordinated Ti4+ row, bridge formate on an oxygen vacancy site with an oxygen atom of formate and on a 5-fold coordinated Ti4+ ion and with the other formate oxygen atom, and a monodentate formate on an oxygen vacancy site with an oxygen atom of formate. formic acid 147-154 sulfotransferase family 1A member 3 Homo sapiens 11-14 16375442-14 2005 Larger Ti deposits produce TiO2 nanoclusters on top of the different monolayer films, as supported both by XPS and STM data. Titanium 7-9 sulfotransferase family 1A member 3 Homo sapiens 115-118 16375442-14 2005 Larger Ti deposits produce TiO2 nanoclusters on top of the different monolayer films, as supported both by XPS and STM data. titanium dioxide 27-31 sulfotransferase family 1A member 3 Homo sapiens 115-118 16853724-0 2005 Weak hydrogen bonds as a structural motif for two-dimensional assemblies of oligopyridines on highly oriented pyrolytic graphite: an STM investigation. Hydrogen 5-13 sulfotransferase family 1A member 3 Homo sapiens 133-136 16853724-0 2005 Weak hydrogen bonds as a structural motif for two-dimensional assemblies of oligopyridines on highly oriented pyrolytic graphite: an STM investigation. oligopyridines 76-90 sulfotransferase family 1A member 3 Homo sapiens 133-136 16853724-0 2005 Weak hydrogen bonds as a structural motif for two-dimensional assemblies of oligopyridines on highly oriented pyrolytic graphite: an STM investigation. Graphite 120-128 sulfotransferase family 1A member 3 Homo sapiens 133-136 16853724-1 2005 We present the STM investigation of four different oligopyridines at the liquid/highly oriented pyrolytic graphite interface. oligopyridines 51-65 sulfotransferase family 1A member 3 Homo sapiens 15-18 16853724-1 2005 We present the STM investigation of four different oligopyridines at the liquid/highly oriented pyrolytic graphite interface. Graphite 106-114 sulfotransferase family 1A member 3 Homo sapiens 15-18 16083857-0 2005 Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3"-phosphoadenosine 5"-phosphate. Dopamine 68-76 sulfotransferase family 1A member 3 Homo sapiens 44-51 16083857-0 2005 Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3"-phosphoadenosine 5"-phosphate. adenosine 3'-phosphate-5'-phosphate 81-113 sulfotransferase family 1A member 3 Homo sapiens 44-51 16083857-1 2005 The human sulfotransferase, SULT1A3, catalyzes specifically the sulfonation of monoamines such as dopamine, epinephrine, and norepinephrine. monoamines 79-89 sulfotransferase family 1A member 3 Homo sapiens 28-35 16083857-1 2005 The human sulfotransferase, SULT1A3, catalyzes specifically the sulfonation of monoamines such as dopamine, epinephrine, and norepinephrine. Dopamine 98-106 sulfotransferase family 1A member 3 Homo sapiens 28-35 16083857-1 2005 The human sulfotransferase, SULT1A3, catalyzes specifically the sulfonation of monoamines such as dopamine, epinephrine, and norepinephrine. Epinephrine 108-119 sulfotransferase family 1A member 3 Homo sapiens 28-35 16083857-1 2005 The human sulfotransferase, SULT1A3, catalyzes specifically the sulfonation of monoamines such as dopamine, epinephrine, and norepinephrine. Norepinephrine 125-139 sulfotransferase family 1A member 3 Homo sapiens 28-35 16083857-2 2005 SULT1A3 also has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is preferentially toward their D-form enantiomers and can be stimulated dramatically by Mn2+. Dihydroxyphenylalanine 26-52 sulfotransferase family 1A member 3 Homo sapiens 0-7 16083857-2 2005 SULT1A3 also has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is preferentially toward their D-form enantiomers and can be stimulated dramatically by Mn2+. Dihydroxyphenylalanine 54-58 sulfotransferase family 1A member 3 Homo sapiens 0-7 16083857-2 2005 SULT1A3 also has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is preferentially toward their D-form enantiomers and can be stimulated dramatically by Mn2+. Tyrosine 60-68 sulfotransferase family 1A member 3 Homo sapiens 0-7 16083857-2 2005 SULT1A3 also has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is preferentially toward their D-form enantiomers and can be stimulated dramatically by Mn2+. Manganese(2+) 181-185 sulfotransferase family 1A member 3 Homo sapiens 0-7 16083857-3 2005 To further our understanding of the molecular basis for the unique substrate specificity of this enzyme, we solved the crystal structure of human SULT1A3, complexed with dopamine and 3"-phosphoadenosine 5"-phosphate, at 2.6 A resolution and carried out autodocking analysis with D-Dopa. Dopamine 170-178 sulfotransferase family 1A member 3 Homo sapiens 146-153 16083857-3 2005 To further our understanding of the molecular basis for the unique substrate specificity of this enzyme, we solved the crystal structure of human SULT1A3, complexed with dopamine and 3"-phosphoadenosine 5"-phosphate, at 2.6 A resolution and carried out autodocking analysis with D-Dopa. adenosine 3'-phosphate-5'-phosphate 183-215 sulfotransferase family 1A member 3 Homo sapiens 146-153 16083857-3 2005 To further our understanding of the molecular basis for the unique substrate specificity of this enzyme, we solved the crystal structure of human SULT1A3, complexed with dopamine and 3"-phosphoadenosine 5"-phosphate, at 2.6 A resolution and carried out autodocking analysis with D-Dopa. D-Dopa 279-285 sulfotransferase family 1A member 3 Homo sapiens 146-153 16083857-4 2005 The structure of SULT1A3 enzyme-ligand complex clearly showed that residue Glu146 can form electrostatic interaction with dopamine and may play a pivotal role in the stereoselectivity and sulfating activity. DL-Glutamic acid 75-81 sulfotransferase family 1A member 3 Homo sapiens 17-24 16083857-4 2005 The structure of SULT1A3 enzyme-ligand complex clearly showed that residue Glu146 can form electrostatic interaction with dopamine and may play a pivotal role in the stereoselectivity and sulfating activity. Dopamine 122-130 sulfotransferase family 1A member 3 Homo sapiens 17-24 16083857-5 2005 On the other hand, residue Asp86 appeared to be critical to the Mn2+-stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3, in addition to a supporting role in the stereoselectivity and sulfating activity. Manganese(2+) 64-68 sulfotransferase family 1A member 3 Homo sapiens 124-131 16083857-5 2005 On the other hand, residue Asp86 appeared to be critical to the Mn2+-stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3, in addition to a supporting role in the stereoselectivity and sulfating activity. Dihydroxyphenylalanine 88-92 sulfotransferase family 1A member 3 Homo sapiens 124-131 16083857-5 2005 On the other hand, residue Asp86 appeared to be critical to the Mn2+-stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3, in addition to a supporting role in the stereoselectivity and sulfating activity. Tyrosine 93-101 sulfotransferase family 1A member 3 Homo sapiens 124-131 16078151-0 2005 Inhibitory effects of various beverages on ritodrine sulfation by recombinant human sulfotransferase isoforms SULT1A1 and SULT1A3. Ritodrine 43-52 sulfotransferase family 1A member 3 Homo sapiens 122-129 16042446-0 2005 STM study on quinacridone derivative assemblies: modulation of the two-dimensional structure by coadsorption with dicarboxylic acids. quinacridone 13-25 sulfotransferase family 1A member 3 Homo sapiens 0-3 16042446-0 2005 STM study on quinacridone derivative assemblies: modulation of the two-dimensional structure by coadsorption with dicarboxylic acids. Dicarboxylic Acids 114-132 sulfotransferase family 1A member 3 Homo sapiens 0-3 16196902-4 2005 Complex surface reconstructions as reported in recent STM and LEED studies are observed only for cooling and H2 dosing. Hydrogen 109-111 sulfotransferase family 1A member 3 Homo sapiens 54-57 16078151-6 2005 RESULTS: Sulfation of ritodrine by SULT1A3 was much higher than that by SULT1A1, suggesting that the bioavailability of ritodrine may be limited by intestinal SULT1A3. Ritodrine 120-129 sulfotransferase family 1A member 3 Homo sapiens 159-166 16078151-7 2005 The ritodrine sulfation activities of SULT1A1 and SULT1A3 were significantly inhibited by all beverages examined at a concentration of 10%. Ritodrine 4-13 sulfotransferase family 1A member 3 Homo sapiens 50-57 16078151-4 2005 METHODS: We investigated ritodrine sulfation by using recombinant human sulfotransferase (SULT) 1A1 and SULT1A3 in an in vitro study. Ritodrine 25-34 sulfotransferase family 1A member 3 Homo sapiens 104-111 16078151-6 2005 RESULTS: Sulfation of ritodrine by SULT1A3 was much higher than that by SULT1A1, suggesting that the bioavailability of ritodrine may be limited by intestinal SULT1A3. Ritodrine 22-31 sulfotransferase family 1A member 3 Homo sapiens 35-42 16078151-6 2005 RESULTS: Sulfation of ritodrine by SULT1A3 was much higher than that by SULT1A1, suggesting that the bioavailability of ritodrine may be limited by intestinal SULT1A3. Ritodrine 22-31 sulfotransferase family 1A member 3 Homo sapiens 159-166 16078151-6 2005 RESULTS: Sulfation of ritodrine by SULT1A3 was much higher than that by SULT1A1, suggesting that the bioavailability of ritodrine may be limited by intestinal SULT1A3. Ritodrine 120-129 sulfotransferase family 1A member 3 Homo sapiens 35-42 15954778-8 2005 STM studies of analogous SAMs on Au(111) gave a detailed picture of the structure and dynamics of mixed monolayers of this type. SAMS Peptide 25-29 sulfotransferase family 1A member 3 Homo sapiens 0-3 15861482-0 2005 Use of specific functionalised tips with STM: a new identification method of ester groups and their molecular structure in self-assembled overlayers. Esters 77-82 sulfotransferase family 1A member 3 Homo sapiens 41-44 16009282-7 2005 RESULTS: The sulfation rate of dopamine (SULT1A3) was 3-fold higher in fetal than adult liver whereas the sulfation rate of 4-nitrophenol (SULT1A1) was one order of magnitude lower in fetal than adult liver. Dopamine 31-39 sulfotransferase family 1A member 3 Homo sapiens 41-48 16178232-0 2005 Formation of TiO2 nanoparticles by reactive-layer-assisted deposition and characterization by XPS and STM. titanium dioxide 13-17 sulfotransferase family 1A member 3 Homo sapiens 102-105 16178245-1 2005 STM imaging on graphite of the S-enantiomer of a chiral diacetylene isophthalic acid derivative reveals that molecular chirality is not expressed in the monolayer due to a specific molecular conformation preventing the stereogenic center to transfer its chiral information. Graphite 15-23 sulfotransferase family 1A member 3 Homo sapiens 0-3 16178245-1 2005 STM imaging on graphite of the S-enantiomer of a chiral diacetylene isophthalic acid derivative reveals that molecular chirality is not expressed in the monolayer due to a specific molecular conformation preventing the stereogenic center to transfer its chiral information. diacetylene isophthalic acid 56-84 sulfotransferase family 1A member 3 Homo sapiens 0-3 16178256-3 2005 Here we introduce a single-molecule device concept based on a class of robust redox active transition metal (Os(II)/(III)) complexes inserted between the working electrode and tip in an electrochemical scanning tunneling microscope (in situ STM). Metals 102-107 sulfotransferase family 1A member 3 Homo sapiens 241-244 16178256-3 2005 Here we introduce a single-molecule device concept based on a class of robust redox active transition metal (Os(II)/(III)) complexes inserted between the working electrode and tip in an electrochemical scanning tunneling microscope (in situ STM). os(ii) 109-115 sulfotransferase family 1A member 3 Homo sapiens 241-244 15954778-8 2005 STM studies of analogous SAMs on Au(111) gave a detailed picture of the structure and dynamics of mixed monolayers of this type. Gold 33-35 sulfotransferase family 1A member 3 Homo sapiens 0-3 15954778-9 2005 The STM images showed that the catalyst-bearing thiolates are distributed statistically on the surface and that the ordered structure of the n-octanethiolate SAM can be retained during incorporation of the catalyst-bearing thiols using the place-exchange methodology. thiolates 48-57 sulfotransferase family 1A member 3 Homo sapiens 4-7 15954778-9 2005 The STM images showed that the catalyst-bearing thiolates are distributed statistically on the surface and that the ordered structure of the n-octanethiolate SAM can be retained during incorporation of the catalyst-bearing thiols using the place-exchange methodology. n-octanethiol 141-157 sulfotransferase family 1A member 3 Homo sapiens 4-7 15954778-9 2005 The STM images showed that the catalyst-bearing thiolates are distributed statistically on the surface and that the ordered structure of the n-octanethiolate SAM can be retained during incorporation of the catalyst-bearing thiols using the place-exchange methodology. Sulfhydryl Compounds 223-229 sulfotransferase family 1A member 3 Homo sapiens 4-7 15917928-1 2005 We have obtained the first in situ STM atomic images of a CO adlayer on a Pt(100)-(1 x 1) electrode in 0.1 M HClO(4) solution, exhibiting a phase transition from c(6 x 2)-10CO to c(4 x 2)-6CO at E > 0.3 V vs. RHE. Hypochlorous Acid 109-113 sulfotransferase family 1A member 3 Homo sapiens 35-38 15929889-3 2005 At concentrations > 0.15 microM, 3-OH-BaP inhibited its own sulfonation in cytosol fractions that were genotyped for SULT1A1 variants, as well as with expressed SULT1A1*1, SULT1A1*2, and SULT1E1, but not with SULT1A3 or SULT1B1. 3-hydroxybenzo(a)pyrene 36-44 sulfotransferase family 1A member 3 Homo sapiens 212-219 16852381-0 2005 An STM investigation of sulfur and alkoxide adsorption on Ni(100). Sulfur 24-30 sulfotransferase family 1A member 3 Homo sapiens 3-6 16852381-1 2005 The effect of sulfur on alkoxide formation and decomposition on the Ni(100) surface has been investigated with STM and LEED. Sulfur 14-20 sulfotransferase family 1A member 3 Homo sapiens 111-114 16852381-1 2005 The effect of sulfur on alkoxide formation and decomposition on the Ni(100) surface has been investigated with STM and LEED. ni(100) 68-75 sulfotransferase family 1A member 3 Homo sapiens 111-114 16852381-2 2005 At low coverage sulfur adsorbs into a p(2 x 2) structure, in agreement with LEED measurements and previous STM results. Sulfur 16-22 sulfotransferase family 1A member 3 Homo sapiens 107-110 16852381-5 2005 STM measurements of the evolution of the sulfur-covered surface with D(2)S(g) adsorption are suggestive of sulfur nucleation and growth at multiple sites on the surface. Sulfur 41-47 sulfotransferase family 1A member 3 Homo sapiens 0-3 16852381-5 2005 STM measurements of the evolution of the sulfur-covered surface with D(2)S(g) adsorption are suggestive of sulfur nucleation and growth at multiple sites on the surface. Sulfur 107-113 sulfotransferase family 1A member 3 Homo sapiens 0-3 15929889-12 2005 The OH-PCBs tested were generally poor inhibitors of SULT1A3- and SULT1B1-dependent activity with 3-OH-BaP. oh-pcbs 4-11 sulfotransferase family 1A member 3 Homo sapiens 53-60 15929889-12 2005 The OH-PCBs tested were generally poor inhibitors of SULT1A3- and SULT1B1-dependent activity with 3-OH-BaP. 3-hydroxybenzo(a)pyrene 98-106 sulfotransferase family 1A member 3 Homo sapiens 53-60 15847549-2 2005 The finite level structure is assumed to have strong binding properties with the metallic substrate, and the bias between the STM tip and the hybrid metal-molecule interface has both an ac and a dc component. Actinium 170-172 sulfotransferase family 1A member 3 Homo sapiens 126-129 16852150-0 2005 The reactive chemisorption of alkyl iodides at Cu(110) and Ag(111) surfaces: a combined STM and XPS study. alkyl iodides 30-43 sulfotransferase family 1A member 3 Homo sapiens 88-91 16852150-1 2005 The chemisorption of methyl and phenyl iodide has been studied at Cu(110) and Ag(111) surfaces at 290 K with STM and XPS. methyl and phenyl iodide 21-45 sulfotransferase family 1A member 3 Homo sapiens 109-112 16852150-5 2005 The STM images show the phenyl groups as bright features approximately 0.7 nm in diameter and 0.11 nm above the iodine adlayer, reaching a maximum surface concentration after approximately 6 Langmuir exposure. Iodine 112-118 sulfotransferase family 1A member 3 Homo sapiens 4-7 16852066-1 2005 A morphological variation of Au(111) covered with irreversibly adsorbed Sb was investigated with cyclic voltammetry and EC-STM. Gold 29-31 sulfotransferase family 1A member 3 Homo sapiens 123-126 16852066-1 2005 A morphological variation of Au(111) covered with irreversibly adsorbed Sb was investigated with cyclic voltammetry and EC-STM. Antimony 72-74 sulfotransferase family 1A member 3 Homo sapiens 123-126 15697277-1 2005 We have shown that STM-tip-induced chain polymerization of 10,12-tricosadiynoic acid (TCDA) in a self-organized monolayer at the liquid-solid interface of TCDA on highly oriented pyrolytic graphite is possible. 10,12-tricosadiynoic acid 59-84 sulfotransferase family 1A member 3 Homo sapiens 19-22 15748705-0 2005 Involvement of SULT1A3 in elevated sulfation of 4-hydroxypropranolol in Hep G2 cells pretreated with beta-naphthoflavone. 4-hydroxypropranolol 48-68 sulfotransferase family 1A member 3 Homo sapiens 15-22 15748705-0 2005 Involvement of SULT1A3 in elevated sulfation of 4-hydroxypropranolol in Hep G2 cells pretreated with beta-naphthoflavone. beta-Naphthoflavone 101-120 sulfotransferase family 1A member 3 Homo sapiens 15-22 15748705-5 2005 SULT1A3 and -1E1 exhibited an enantioselectivity of 4-OH-R-PL sulfation>4-OH-S-PL sulfation, which agreed with that of BNF-pretreated Hep G2 cells as well as of nontreated cells, whereas SULT1A1 and -1B1 showed a reversed enantioselectivity (R<S). 4-oh-r-pl 52-61 sulfotransferase family 1A member 3 Homo sapiens 0-16 15748705-5 2005 SULT1A3 and -1E1 exhibited an enantioselectivity of 4-OH-R-PL sulfation>4-OH-S-PL sulfation, which agreed with that of BNF-pretreated Hep G2 cells as well as of nontreated cells, whereas SULT1A1 and -1B1 showed a reversed enantioselectivity (R<S). 4-oh-s-pl 75-84 sulfotransferase family 1A member 3 Homo sapiens 0-16 15748705-6 2005 In kinetic studies of 4-OH-PL sulfations by four kinds of human SULT isoforms, apparent K(m) values for SULT1A3 were the lowest, and the parameters were close to those of Hep G2 cytosolic fractions. 4-oh-pl 22-29 sulfotransferase family 1A member 3 Homo sapiens 104-111 15755826-11 2005 CONCLUSIONS: Each intervention (dietary counseling or n-3 PUFA supplements) reduced sTM and sICAM-1 concentrations, indicating decreased endothelial activation. Nitrogen 19-20 sulfotransferase family 1A member 3 Homo sapiens 84-87 15755826-11 2005 CONCLUSIONS: Each intervention (dietary counseling or n-3 PUFA supplements) reduced sTM and sICAM-1 concentrations, indicating decreased endothelial activation. 3 pufa 56-62 sulfotransferase family 1A member 3 Homo sapiens 84-87 15748705-8 2005 These results suggest that the induction of SULT1A3 is mainly responsible for the elevated 4-OH-PL sulfation activities following the pretreatment of Hep G2 cells with BNF. 4-oh-pl 91-98 sulfotransferase family 1A member 3 Homo sapiens 44-51 15697277-1 2005 We have shown that STM-tip-induced chain polymerization of 10,12-tricosadiynoic acid (TCDA) in a self-organized monolayer at the liquid-solid interface of TCDA on highly oriented pyrolytic graphite is possible. 10,12-tricosadiynoic acid 86-90 sulfotransferase family 1A member 3 Homo sapiens 19-22 15697277-1 2005 We have shown that STM-tip-induced chain polymerization of 10,12-tricosadiynoic acid (TCDA) in a self-organized monolayer at the liquid-solid interface of TCDA on highly oriented pyrolytic graphite is possible. 10,12-tricosadiynoic acid 155-159 sulfotransferase family 1A member 3 Homo sapiens 19-22 15697277-1 2005 We have shown that STM-tip-induced chain polymerization of 10,12-tricosadiynoic acid (TCDA) in a self-organized monolayer at the liquid-solid interface of TCDA on highly oriented pyrolytic graphite is possible. Graphite 189-197 sulfotransferase family 1A member 3 Homo sapiens 19-22 15697282-1 2005 STM investigations of three N-alkyl fatty acid amide molecules have been carried out to get information of their molecular arrangement on a highly oriented pyrolytic graphite surface. n-alkyl fatty acid amide 28-52 sulfotransferase family 1A member 3 Homo sapiens 0-3 15697282-1 2005 STM investigations of three N-alkyl fatty acid amide molecules have been carried out to get information of their molecular arrangement on a highly oriented pyrolytic graphite surface. Graphite 166-174 sulfotransferase family 1A member 3 Homo sapiens 0-3 15521727-0 2004 Photochemical attachment of organic monolayers onto H-terminated Si(111): radical chain propagation observed via STM studies. Silicon 65-67 sulfotransferase family 1A member 3 Homo sapiens 113-116 15880500-1 2005 STM tips made from antiferromagnetic MnNi have been used to investigate the atomic structure of the (001) and (111) surfaces of Fe3O4. ferryl iron 128-133 sulfotransferase family 1A member 3 Homo sapiens 0-3 15996335-9 2005 As sTM is excreted by the kidney we also measured plasma level of creatinine and its clearance. Creatinine 66-76 sulfotransferase family 1A member 3 Homo sapiens 3-6 15654867-6 2005 We show that intra-LA infusions of the MAPK kinase (MEK) inhibitor U0126, a manipulation which inhibits activation of ERK-MAPK, impairs postreactivation long-term memory (PR-LTM) but leaves the postreactivation short-term memory (PR-STM) intact. U 0126 67-72 sulfotransferase family 1A member 3 Homo sapiens 233-236 16095049-8 2005 In multivariate regression analyses, tPAag remained significantly associated with the presence of CVD (p = 0.03), sE-selectin with diabetes (p=0.004), sTM with hypertension (p = 0.02) and sVCAM-1, sICAM-1 and sTM with smoking, (p = 0.01, p < 0.001, p < 0.001, respectively). tpaag 37-42 sulfotransferase family 1A member 3 Homo sapiens 151-154 16095049-8 2005 In multivariate regression analyses, tPAag remained significantly associated with the presence of CVD (p = 0.03), sE-selectin with diabetes (p=0.004), sTM with hypertension (p = 0.02) and sVCAM-1, sICAM-1 and sTM with smoking, (p = 0.01, p < 0.001, p < 0.001, respectively). tpaag 37-42 sulfotransferase family 1A member 3 Homo sapiens 209-212 15601102-1 2004 Density functional calculations are performed to identify features observed in STM experiments after phosphine (PH3) dosing of the Si(001) surface. phosphine 101-110 sulfotransferase family 1A member 3 Homo sapiens 79-82 15601102-1 2004 Density functional calculations are performed to identify features observed in STM experiments after phosphine (PH3) dosing of the Si(001) surface. PH.3 112-115 sulfotransferase family 1A member 3 Homo sapiens 79-82 15601102-2 2004 On the basis of a comprehensive survey of possible structures, energetics, and simulated STM images, three prominent STM features are assigned to structures containing surface bound PH2, PH, and P, respectively. ph2 182-185 sulfotransferase family 1A member 3 Homo sapiens 89-92 15601102-2 2004 On the basis of a comprehensive survey of possible structures, energetics, and simulated STM images, three prominent STM features are assigned to structures containing surface bound PH2, PH, and P, respectively. ph2 182-185 sulfotransferase family 1A member 3 Homo sapiens 117-120 16399348-4 2005 SULT1A3 is the major catecholamine sulfonating form, which is consistent with it being expressed principally in the gastrointestinal tract. Catecholamines 21-34 sulfotransferase family 1A member 3 Homo sapiens 0-7 15281911-11 2004 If the expression levels in tissues are additionally taken into account, SULT1A3 might be the predominant form for the sulphonation of ethanol in vivo, although a robust estimate requires further studies. Ethanol 135-142 sulfotransferase family 1A member 3 Homo sapiens 73-80 15506724-1 2004 The rational design of catechol bis-amides rendered molecular structures that fold into beta-turn mimics at the interface of HOPG and 1-octanol as demonstrated by STM. catechol bis-amides 23-42 sulfotransferase family 1A member 3 Homo sapiens 163-166 15506724-1 2004 The rational design of catechol bis-amides rendered molecular structures that fold into beta-turn mimics at the interface of HOPG and 1-octanol as demonstrated by STM. 1-Octanol 134-143 sulfotransferase family 1A member 3 Homo sapiens 163-166 15483196-8 2004 Moreover, when estrone (which selectively inhibits expressed SULT1E1 and SULT1A3) was included in intestinal incubations, the high-affinity component of the Eadie-Hofstee plot for EE sulfation was inhibited, converting the plot from biphasic to monophasic. Estrone 15-22 sulfotransferase family 1A member 3 Homo sapiens 73-80 15531517-5 2004 Apparent K(m) values for SULT1A1 and SULT1A3 activities with the model substrates p-nitrophenol and dopamine were 0.58 +/- 0.04 and 11.3 +/- 1.3 microm, respectively. 4-nitrophenol 82-95 sulfotransferase family 1A member 3 Homo sapiens 37-44 15531517-5 2004 Apparent K(m) values for SULT1A1 and SULT1A3 activities with the model substrates p-nitrophenol and dopamine were 0.58 +/- 0.04 and 11.3 +/- 1.3 microm, respectively. Dopamine 100-108 sulfotransferase family 1A member 3 Homo sapiens 37-44 15358107-1 2004 Sulfotransferase (SULT) 1A3 catalyzes the sulfate conjugation of catecholamines. Sulfates 42-49 sulfotransferase family 1A member 3 Homo sapiens 0-27 15525007-1 2004 STM investigations of vicinal Si(111) surfaces etched in KOH solutions under controlled flow conditions show that step bunching instability is due to inhomogeneities that develop in the etchant as the result of highly step-site-specific etching reactions. Silicon 30-32 sulfotransferase family 1A member 3 Homo sapiens 0-3 15525007-1 2004 STM investigations of vicinal Si(111) surfaces etched in KOH solutions under controlled flow conditions show that step bunching instability is due to inhomogeneities that develop in the etchant as the result of highly step-site-specific etching reactions. potassium hydroxide 57-60 sulfotransferase family 1A member 3 Homo sapiens 0-3 15502831-2 2004 Here we show that we can change the diffusion coefficient of the complex organic molecule known as Violet Lander (VL, C(108)H(104)) on Cu(110) by two orders of magnitude by using the STM at low temperatures to switch between two adsorption configurations that differ only in the molecular orientation with respect to the substrate lattice. Copper 135-137 sulfotransferase family 1A member 3 Homo sapiens 183-186 15358107-1 2004 Sulfotransferase (SULT) 1A3 catalyzes the sulfate conjugation of catecholamines. Catecholamines 65-79 sulfotransferase family 1A member 3 Homo sapiens 0-27 15323727-2 2004 Atomic scale STM images show significant magnetic contrast corresponding to variations in the local surface states induced by oxygen vacancies. Oxygen 126-132 sulfotransferase family 1A member 3 Homo sapiens 13-16 15087475-8 2004 No human ST1D ortholog was detected at both mRNA and protein levels, although ST1A5 selectively catalyzing parent amine sulfation was detected in human kidney. Amines 114-119 sulfotransferase family 1A member 3 Homo sapiens 78-83 15487807-4 2004 The IC50 value of mefenamic acid for human liver phenol sulfotransferase (SULT 1A1) was 0.02 microM and for human liver catechol sulfotransferase (SULT1A3) 76 microM with a SULT 1A3/SULT1A1 ratio for the IC50 of 3,800. Mefenamic Acid 18-32 sulfotransferase family 1A member 3 Homo sapiens 147-154 15487807-4 2004 The IC50 value of mefenamic acid for human liver phenol sulfotransferase (SULT 1A1) was 0.02 microM and for human liver catechol sulfotransferase (SULT1A3) 76 microM with a SULT 1A3/SULT1A1 ratio for the IC50 of 3,800. Mefenamic Acid 18-32 sulfotransferase family 1A member 3 Homo sapiens 173-181 15144814-3 2004 Here, the electrochemical and physical properties of hydroquinone adsorbed on hematite surfaces at pH 2.5-3 were investigated with cyclic voltammetry (CV), electrochemical-scanning tunneling microscopy (EC-STM), and X-ray photoelectron spectroscopy (XPS). hydroquinone 53-65 sulfotransferase family 1A member 3 Homo sapiens 206-209 15323996-3 2004 Based on our results, we propose that STM images and photoemission experiments may detect specific changes induced by water on both the structural and electronic properties of SiC(001) surfaces. Water 118-123 sulfotransferase family 1A member 3 Homo sapiens 38-41 15199569-0 2004 Visualization of local valence structures in quasi-one-dimensional halogen-bridged complexes [Ni(1-x)Pd(x)(chxn)(2)Br]Br(2) by STM. Halogens 67-74 sulfotransferase family 1A member 3 Homo sapiens 127-130 15144814-5 2004 The EC-STM results indicate that hydroquinone sometimes forms an ordered monolayer with approximately 1.1 QH(2)/nm(2), but can be fairly disordered (especially when viewed at larger scales). hydroquinone 33-45 sulfotransferase family 1A member 3 Homo sapiens 7-10 14871892-2 2004 Human SULT1A3 has been shown to be the major sulfotransferase that sulfonates dopamine. Dopamine 78-86 sulfotransferase family 1A member 3 Homo sapiens 6-13 14871892-11 2004 We also propose, based on modeling and kinetic studies, that substrate inhibition by dopamine in SULT1A3 is caused by binding of two dopamine molecules in the active site. Dopamine 85-93 sulfotransferase family 1A member 3 Homo sapiens 97-104 14871892-11 2004 We also propose, based on modeling and kinetic studies, that substrate inhibition by dopamine in SULT1A3 is caused by binding of two dopamine molecules in the active site. Dopamine 133-141 sulfotransferase family 1A member 3 Homo sapiens 97-104 14871892-7 2004 For SULT1A3, substrate inhibition is found for dopamine but not with pNP. Dopamine 47-55 sulfotransferase family 1A member 3 Homo sapiens 4-11 15069479-1 2004 The evaporation of solutions of dendron-functionalised 2,2"-bipyridines on a graphite surface gives highly ordered monolayers; near atomic resolution STM imaging has allowed a detailed conformational analysis to be made. dendron 32-39 sulfotransferase family 1A member 3 Homo sapiens 150-153 15069479-1 2004 The evaporation of solutions of dendron-functionalised 2,2"-bipyridines on a graphite surface gives highly ordered monolayers; near atomic resolution STM imaging has allowed a detailed conformational analysis to be made. 2,2'-Dipyridyl 55-71 sulfotransferase family 1A member 3 Homo sapiens 150-153 15069479-1 2004 The evaporation of solutions of dendron-functionalised 2,2"-bipyridines on a graphite surface gives highly ordered monolayers; near atomic resolution STM imaging has allowed a detailed conformational analysis to be made. Graphite 77-85 sulfotransferase family 1A member 3 Homo sapiens 150-153 12898345-0 2003 L-DOPA biotransformation: correlations of dosage, erythrocyte catechol O-methyltransferase and platelet SULT1A3 activities with metabolic pathways in Parkinsonian patients. Levodopa 0-6 sulfotransferase family 1A member 3 Homo sapiens 104-111 15089492-4 2004 Here, using STM, we show that on Si(100) many intrinsically repulsive adsorbates cluster to form surface patches even at low surface coverages. Silicon 33-35 sulfotransferase family 1A member 3 Homo sapiens 12-15 14525459-1 2003 We report a systematic experimental investigation of the mechanism of desorption of chlorobenzene molecules from the Si(111)-(7 x 7) surface induced by the STM at room temperature. chlorobenzene 84-97 sulfotransferase family 1A member 3 Homo sapiens 156-159 14525459-1 2003 We report a systematic experimental investigation of the mechanism of desorption of chlorobenzene molecules from the Si(111)-(7 x 7) surface induced by the STM at room temperature. Silicon 117-119 sulfotransferase family 1A member 3 Homo sapiens 156-159 14703820-1 2003 Geometrical structures of chain porphyrin arrays adsorbed on Cu(100) are observed by STM: a bridge-like bent structure for meso-meso singly linked orthogonal hexamer, whereas a rigid planar and one-dimensionally stacked structure for meso-meso, beta-beta, beta-beta triply-linked hexamer. meso-meso 123-132 sulfotransferase family 1A member 3 Homo sapiens 85-88 14680218-1 2003 Triptycene molecular orientation has been tuned with a STM tip at a Cu(111) surface in solution from flat, to tilt, to vertical. triptycene 0-10 sulfotransferase family 1A member 3 Homo sapiens 55-58 14595405-3 2003 Here we present high-speed scanning tunnelling microscopy (video-STM) observations of the dynamic behaviour of five-atom-wide, hexagonally ordered strings of Au atoms embedded in the square lattice of the Au(100)-(1x1) surface that reveal quasi-collective lateral motion of these strings perpendicular to as well as along the string direction. Gold 158-160 sulfotransferase family 1A member 3 Homo sapiens 65-68 14622112-1 2003 Sulfotransferase (SULT) 1A3 catalyzes the sulfate conjugation of catecholamines and structurally related drugs. Sulfates 42-49 sulfotransferase family 1A member 3 Homo sapiens 0-27 14622112-1 2003 Sulfotransferase (SULT) 1A3 catalyzes the sulfate conjugation of catecholamines and structurally related drugs. Catecholamines 65-79 sulfotransferase family 1A member 3 Homo sapiens 0-27 14611320-1 2003 Ab initio total energy calculations reveal benzene-dithiolate molecules on a gold surface, contacted by a monatomic gold STM tip to have two classes of low-energy conformations with differing symmetries. Benzene 43-50 sulfotransferase family 1A member 3 Homo sapiens 121-124 14611320-1 2003 Ab initio total energy calculations reveal benzene-dithiolate molecules on a gold surface, contacted by a monatomic gold STM tip to have two classes of low-energy conformations with differing symmetries. dithiolate 51-61 sulfotransferase family 1A member 3 Homo sapiens 121-124 14502490-3 2003 The evaluated SULT1A3 substrate data set consisted of 95 different substituted phenols, catechols, catecholamines, steroids, and related structures for which the K(m) values were available. Phenols 79-86 sulfotransferase family 1A member 3 Homo sapiens 14-21 14502490-3 2003 The evaluated SULT1A3 substrate data set consisted of 95 different substituted phenols, catechols, catecholamines, steroids, and related structures for which the K(m) values were available. Catechols 88-97 sulfotransferase family 1A member 3 Homo sapiens 14-21 14502490-3 2003 The evaluated SULT1A3 substrate data set consisted of 95 different substituted phenols, catechols, catecholamines, steroids, and related structures for which the K(m) values were available. Catecholamines 99-113 sulfotransferase family 1A member 3 Homo sapiens 14-21 14502490-3 2003 The evaluated SULT1A3 substrate data set consisted of 95 different substituted phenols, catechols, catecholamines, steroids, and related structures for which the K(m) values were available. Steroids 115-123 sulfotransferase family 1A member 3 Homo sapiens 14-21 12707753-0 2003 EC STM investigations of corrosion due to chloride solutions on thin CrN coatings. Chlorides 42-50 sulfotransferase family 1A member 3 Homo sapiens 3-6 12739671-1 2003 The synthesis, isolation and STM imaging on graphite of the cis and trans isomers of a TTF reveal isomer-dependent packing, and constitutes a way to study the non-covalent interactions at play in these systems. Graphite 44-52 sulfotransferase family 1A member 3 Homo sapiens 29-32 12535561-0 2003 STM observation of steps and terraces on tungsten (211) surface. Tungsten 41-49 sulfotransferase family 1A member 3 Homo sapiens 0-3 12707753-0 2003 EC STM investigations of corrosion due to chloride solutions on thin CrN coatings. corrin 69-72 sulfotransferase family 1A member 3 Homo sapiens 3-6 12707753-4 2003 They were investigated in electrochemical scanning tunnelling microscopy (EC STM) by cyclic voltammetry in 1 mol L(-1) NaCl. Sodium Chloride 119-123 sulfotransferase family 1A member 3 Homo sapiens 77-80 12603161-1 2003 The molecular orientation, spatial distribution, and thermal behavior of the powerful chiral catalyst modifier precursor (S)-naphthylethylamine adsorbed on Pt[111] have been studied by NEXAFS, XPS, STM, and temperature programmed reaction. (s)-naphthylethylamine 121-143 sulfotransferase family 1A member 3 Homo sapiens 198-201 12822536-6 2003 Analysis of these strains revealed: 1. the proportion of multiresistant strains STM DT104 of the total number of isolated STM strains increased from 7% in 2000 to 11.5% in 2001, 2. the territory in the CR where these multiresistant strains were found expanded, 3. the relationship of proportions of the most frequently detected STM phagotypes in the human population changes: in 2000 this ratio was balanced, in 2001 the ratio of phagotype DT104 is roughly three times higher than of DT 141, 4. analysis of all STM strains from the environment and animals indicates that the frequency of STM DT104 is 73%. Thymidine 84-86 sulfotransferase family 1A member 3 Homo sapiens 80-83 12822536-6 2003 Analysis of these strains revealed: 1. the proportion of multiresistant strains STM DT104 of the total number of isolated STM strains increased from 7% in 2000 to 11.5% in 2001, 2. the territory in the CR where these multiresistant strains were found expanded, 3. the relationship of proportions of the most frequently detected STM phagotypes in the human population changes: in 2000 this ratio was balanced, in 2001 the ratio of phagotype DT104 is roughly three times higher than of DT 141, 4. analysis of all STM strains from the environment and animals indicates that the frequency of STM DT104 is 73%. Thymidine 84-86 sulfotransferase family 1A member 3 Homo sapiens 122-125 12822536-6 2003 Analysis of these strains revealed: 1. the proportion of multiresistant strains STM DT104 of the total number of isolated STM strains increased from 7% in 2000 to 11.5% in 2001, 2. the territory in the CR where these multiresistant strains were found expanded, 3. the relationship of proportions of the most frequently detected STM phagotypes in the human population changes: in 2000 this ratio was balanced, in 2001 the ratio of phagotype DT104 is roughly three times higher than of DT 141, 4. analysis of all STM strains from the environment and animals indicates that the frequency of STM DT104 is 73%. Thymidine 84-86 sulfotransferase family 1A member 3 Homo sapiens 122-125 12822536-6 2003 Analysis of these strains revealed: 1. the proportion of multiresistant strains STM DT104 of the total number of isolated STM strains increased from 7% in 2000 to 11.5% in 2001, 2. the territory in the CR where these multiresistant strains were found expanded, 3. the relationship of proportions of the most frequently detected STM phagotypes in the human population changes: in 2000 this ratio was balanced, in 2001 the ratio of phagotype DT104 is roughly three times higher than of DT 141, 4. analysis of all STM strains from the environment and animals indicates that the frequency of STM DT104 is 73%. Thymidine 84-86 sulfotransferase family 1A member 3 Homo sapiens 122-125 12822536-6 2003 Analysis of these strains revealed: 1. the proportion of multiresistant strains STM DT104 of the total number of isolated STM strains increased from 7% in 2000 to 11.5% in 2001, 2. the territory in the CR where these multiresistant strains were found expanded, 3. the relationship of proportions of the most frequently detected STM phagotypes in the human population changes: in 2000 this ratio was balanced, in 2001 the ratio of phagotype DT104 is roughly three times higher than of DT 141, 4. analysis of all STM strains from the environment and animals indicates that the frequency of STM DT104 is 73%. Thymidine 84-86 sulfotransferase family 1A member 3 Homo sapiens 122-125 12745871-11 2003 Curcumin inhibited human SULT1A3, and the inhibition was studied in five liver specimens with an IC(50) of 4324 +/- 1026 nM. Curcumin 0-8 sulfotransferase family 1A member 3 Homo sapiens 25-32 12603161-7 2003 When NEA and methyl pyruvate are coadsorbed in the presence of H(a), STM reveals entities that could correspond to a 1:1 docking complex between the prochiral reactant and the chiral modifier. N-Nitroso-N-ethylaniline 5-8 sulfotransferase family 1A member 3 Homo sapiens 69-72 12603161-7 2003 When NEA and methyl pyruvate are coadsorbed in the presence of H(a), STM reveals entities that could correspond to a 1:1 docking complex between the prochiral reactant and the chiral modifier. methyl pyruvate 13-28 sulfotransferase family 1A member 3 Homo sapiens 69-72 12603161-7 2003 When NEA and methyl pyruvate are coadsorbed in the presence of H(a), STM reveals entities that could correspond to a 1:1 docking complex between the prochiral reactant and the chiral modifier. histidinoalanine 63-67 sulfotransferase family 1A member 3 Homo sapiens 69-72 12558577-1 2003 PURPOSE: To evaluate the effects of sulthiame (Ospolot; STM) monotherapy compared with placebo on the EEG in children with benign childhood epilepsy with centrotemporal spikes (BECTS). sulthiame 36-45 sulfotransferase family 1A member 3 Homo sapiens 56-59 12641227-8 2003 SAM molecules can also be removed from the tip apex by application of a negative sample bias (-2.0 V for 0.5-10 min) making it possible to alternate between conventional STM images and STM images with chemically enhanced contrasts. S-Adenosylmethionine 0-3 sulfotransferase family 1A member 3 Homo sapiens 170-173 12641227-8 2003 SAM molecules can also be removed from the tip apex by application of a negative sample bias (-2.0 V for 0.5-10 min) making it possible to alternate between conventional STM images and STM images with chemically enhanced contrasts. S-Adenosylmethionine 0-3 sulfotransferase family 1A member 3 Homo sapiens 185-188 12619410-0 2003 The characterisation of supported platinum nanoparticles on carbon used for enantioselective hydrogenation: a combined electrochemical-STM approach. Platinum 34-42 sulfotransferase family 1A member 3 Homo sapiens 135-138 12619410-0 2003 The characterisation of supported platinum nanoparticles on carbon used for enantioselective hydrogenation: a combined electrochemical-STM approach. Carbon 60-66 sulfotransferase family 1A member 3 Homo sapiens 135-138 12424257-4 2003 Through the characterization of chimeric PSTs where these two regions were exchanged between them, it was demonstrated that variable Region II of SULT1A3 is required for the stereospecificity of its Dopa/tyrosine-sulfating activity, whereas variable Region I of SULT1A3 is required for the stimulation by Mn(2+) of this activity. Tyrosine 204-212 sulfotransferase family 1A member 3 Homo sapiens 146-153 12424257-0 2003 Structure-function relationships in the stereospecific and manganese-dependent 3,4-dihydroxyphenylalanine/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase, SULT1A3. Tyrosine 106-114 sulfotransferase family 1A member 3 Homo sapiens 183-190 12424257-1 2003 The human monoamine-form phenol sulfotransferase (PST), SULT1A3, has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is stereospecific for their d-form enantiomers and can be stimulated dramatically by Mn(2+). monoamine 10-19 sulfotransferase family 1A member 3 Homo sapiens 56-63 12424257-1 2003 The human monoamine-form phenol sulfotransferase (PST), SULT1A3, has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is stereospecific for their d-form enantiomers and can be stimulated dramatically by Mn(2+). Dihydroxyphenylalanine 78-104 sulfotransferase family 1A member 3 Homo sapiens 56-63 12424257-1 2003 The human monoamine-form phenol sulfotransferase (PST), SULT1A3, has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is stereospecific for their d-form enantiomers and can be stimulated dramatically by Mn(2+). Dihydroxyphenylalanine 106-110 sulfotransferase family 1A member 3 Homo sapiens 56-63 12424257-1 2003 The human monoamine-form phenol sulfotransferase (PST), SULT1A3, has a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is stereospecific for their d-form enantiomers and can be stimulated dramatically by Mn(2+). Tyrosine 112-120 sulfotransferase family 1A member 3 Homo sapiens 56-63 12929419-2 2003 Highly-ordered adlayers both for the metal-free state and the complex were visualized by in-situ STM with sub-molecular visualization. Metals 37-42 sulfotransferase family 1A member 3 Homo sapiens 97-100 12424257-4 2003 Through the characterization of chimeric PSTs where these two regions were exchanged between them, it was demonstrated that variable Region II of SULT1A3 is required for the stereospecificity of its Dopa/tyrosine-sulfating activity, whereas variable Region I of SULT1A3 is required for the stimulation by Mn(2+) of this activity. Dihydroxyphenylalanine 199-203 sulfotransferase family 1A member 3 Homo sapiens 146-153 12424257-5 2003 Further studies using point-mutated SULT1A3s mutated at amino acid residues in these two regions and deletional mutants missing residues 84-86 and 84-90 implicate residue Glu-146 (in variable Region II of SULT1A3), as well as the presence of residues 84-90 of variable Region I, in the stereospecificity in the absence of Mn(2+). Glutamic Acid 171-174 sulfotransferase family 1A member 3 Homo sapiens 205-212 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Aspartic Acid 8-11 sulfotransferase family 1A member 3 Homo sapiens 40-47 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Aspartic Acid 8-11 sulfotransferase family 1A member 3 Homo sapiens 150-157 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Manganese(2+) 88-94 sulfotransferase family 1A member 3 Homo sapiens 40-47 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Manganese(2+) 88-94 sulfotransferase family 1A member 3 Homo sapiens 150-157 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Dihydroxyphenylalanine 114-118 sulfotransferase family 1A member 3 Homo sapiens 40-47 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Dihydroxyphenylalanine 114-118 sulfotransferase family 1A member 3 Homo sapiens 150-157 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Tyrosine 119-127 sulfotransferase family 1A member 3 Homo sapiens 40-47 12424257-6 2003 Residue Asp-86 (in variable Region I of SULT1A3), on the other hand, is critical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3. Tyrosine 119-127 sulfotransferase family 1A member 3 Homo sapiens 150-157 12424257-7 2003 A model is proposed, with reference to the reported x-ray crystal structure of SULT1A3, to explain how the normal role of SULT1A3 in dopamine regulation may be subverted in the presence of Mn(2+). Dopamine 133-141 sulfotransferase family 1A member 3 Homo sapiens 79-86 12424257-7 2003 A model is proposed, with reference to the reported x-ray crystal structure of SULT1A3, to explain how the normal role of SULT1A3 in dopamine regulation may be subverted in the presence of Mn(2+). Dopamine 133-141 sulfotransferase family 1A member 3 Homo sapiens 122-129 12225042-1 2002 The persistence behavior for fluctuating steps on the Si(111)-(sqrt[3]xsqrt[3])R30 degrees -Al surface was determined by analyzing time-dependent STM images for temperatures between 770 and 970 K. Using the standard persistence definition, the measured persistence probability displays power-law decay with an exponent of theta=0.77+/-0.03. Silicon 54-56 sulfotransferase family 1A member 3 Homo sapiens 146-149 12513174-1 2002 Recent STM experiments on Bi2Sr2Ca2Cu3O10 observed sharp bound states associated with Zn and Ni impurities, as previously predicted theoretically. Zinc 86-88 sulfotransferase family 1A member 3 Homo sapiens 7-10 12452692-1 2002 The adsorption mode of cinchonidine on Cu(111) was directly obtained by in situ STM. cinchonidine 23-35 sulfotransferase family 1A member 3 Homo sapiens 80-83 12452692-1 2002 The adsorption mode of cinchonidine on Cu(111) was directly obtained by in situ STM. Copper 39-41 sulfotransferase family 1A member 3 Homo sapiens 80-83 12402313-4 2002 Wild-type ST1A3*1 ((213)Arg) alleles were slightly overrepresented in nonsmoking urothelial cancer patients (82.6% vs. 69.7%) and in smoking cancer patients (76.7% and 74.3%) compared to a variant ST1A3*2 ((213)His) allele. Arginine 24-27 sulfotransferase family 1A member 3 Homo sapiens 10-15 12402313-4 2002 Wild-type ST1A3*1 ((213)Arg) alleles were slightly overrepresented in nonsmoking urothelial cancer patients (82.6% vs. 69.7%) and in smoking cancer patients (76.7% and 74.3%) compared to a variant ST1A3*2 ((213)His) allele. Arginine 24-27 sulfotransferase family 1A member 3 Homo sapiens 197-202 12402313-6 2002 Recombinant ST1A3*1 enzyme showed a tendency of catalyzing higher in vitro 3"-phosphoadenosine 5"-phosphosulfate-dependent DNA adduct formation than ST1A3*2 (2.84 +/- 0.49 and 2.22 +/- 0.11 adducts/10(8) nucleotides). Phosphoadenosine Phosphosulfate 75-112 sulfotransferase family 1A member 3 Homo sapiens 12-17 12402313-7 2002 Combined analyses of different alleles of carcinogenic aromatic amine-activating phase II enzymes were applied to urothelial cancer risk for the first time and showed the highest risk combination of ST1A3 and NAT2 alleles. aromatic amine 55-69 sulfotransferase family 1A member 3 Homo sapiens 199-204 12430426-1 2002 Poly(dA).Poly(dT) molecules up to 1000 base pairs (bp) have been synthesized using enzymatic reaction, and characterization by STM observation shows that the DNA has no defects in the duplex structure. Poly T 9-17 sulfotransferase family 1A member 3 Homo sapiens 127-130 12552528-4 2003 When chemically modified tips were used for STM measurements, contrast enhancements at specific regions in the STM images occurred on the basis of hydrogen bond and metal-coordination interactions. Hydrogen 147-155 sulfotransferase family 1A member 3 Homo sapiens 44-47 12552528-4 2003 When chemically modified tips were used for STM measurements, contrast enhancements at specific regions in the STM images occurred on the basis of hydrogen bond and metal-coordination interactions. Hydrogen 147-155 sulfotransferase family 1A member 3 Homo sapiens 111-114 12552528-4 2003 When chemically modified tips were used for STM measurements, contrast enhancements at specific regions in the STM images occurred on the basis of hydrogen bond and metal-coordination interactions. Metals 165-170 sulfotransferase family 1A member 3 Homo sapiens 44-47 12552528-4 2003 When chemically modified tips were used for STM measurements, contrast enhancements at specific regions in the STM images occurred on the basis of hydrogen bond and metal-coordination interactions. Metals 165-170 sulfotransferase family 1A member 3 Homo sapiens 111-114 12564743-7 2003 The rate of apomorphine sulfation correlated with the activity of SULT1A1 (r = 0.989; p = 0.002) and SULT1A3 (r = 0.973; p = 0.005). Apomorphine 12-23 sulfotransferase family 1A member 3 Homo sapiens 101-108 12440891-1 2002 We report single-molecule level STM observations of chiral complexes generated by the assembly of achiral components at a metal surface. Metals 122-127 sulfotransferase family 1A member 3 Homo sapiens 32-35 12440891-2 2002 Following co-deposition of iron atoms and 1,3,5-tricarboxylic benzoic acid (trimesic acid, TMA) on Cu(100) in ultrahigh vaccum, TMA molecules react with the metal centers, and metal-ligand interactions stabilize R and S chiral complexes which are clearly distinguished by STM. Iron 27-31 sulfotransferase family 1A member 3 Homo sapiens 272-275 12440891-2 2002 Following co-deposition of iron atoms and 1,3,5-tricarboxylic benzoic acid (trimesic acid, TMA) on Cu(100) in ultrahigh vaccum, TMA molecules react with the metal centers, and metal-ligand interactions stabilize R and S chiral complexes which are clearly distinguished by STM. 1,3,5-tricarboxylic benzoic acid 42-74 sulfotransferase family 1A member 3 Homo sapiens 272-275 12440891-2 2002 Following co-deposition of iron atoms and 1,3,5-tricarboxylic benzoic acid (trimesic acid, TMA) on Cu(100) in ultrahigh vaccum, TMA molecules react with the metal centers, and metal-ligand interactions stabilize R and S chiral complexes which are clearly distinguished by STM. trimesic acid 76-89 sulfotransferase family 1A member 3 Homo sapiens 272-275 12167648-7 2002 Here we report that long chain acyl-CoAs are more potent inhibitors of bSULT1A1 and also of human dopamine sulfotransferase (SULT1A3) when compared with unesterified CoA and short chain-length acyl-CoAs. Acyl Coenzyme A 31-40 sulfotransferase family 1A member 3 Homo sapiens 125-132 12206822-2 2002 We previously showed the sulfoconjugation of bisphenol A catalyzed by a human thermostable phenol sulfotransferase, ST1A3. bisphenol A 45-56 sulfotransferase family 1A member 3 Homo sapiens 116-121 12225042-1 2002 The persistence behavior for fluctuating steps on the Si(111)-(sqrt[3]xsqrt[3])R30 degrees -Al surface was determined by analyzing time-dependent STM images for temperatures between 770 and 970 K. Using the standard persistence definition, the measured persistence probability displays power-law decay with an exponent of theta=0.77+/-0.03. Aluminum 92-94 sulfotransferase family 1A member 3 Homo sapiens 146-149 12227564-1 2002 Atomically resolved in situ STM images are presented for an underpotentially deposited (upd) cadmium layer on a Cu(111) electrode from a 10(-4) M CdCl2/10(-2) M HCl solution. Cadmium 93-100 sulfotransferase family 1A member 3 Homo sapiens 28-31 12188658-0 2002 Long-range self-assembly of a polyunsaturated linear organosilane at the n-tetradecane/Au(111) interface studied by STM. n-tetradecane 73-86 sulfotransferase family 1A member 3 Homo sapiens 116-119 12188658-2 2002 Molecular resolution STM images recorded at the liquid-solid interface between gold and tetradecane reveal a long-range and densely packed hexagonal lattice with a ( radical3 x radical3)R30 degrees -like structure commensurate against gold adlattice. n-tetradecane 88-99 sulfotransferase family 1A member 3 Homo sapiens 21-24 11814364-0 2002 The ATP/metallothionein interaction: NMR and STM. Adenosine Triphosphate 4-7 sulfotransferase family 1A member 3 Homo sapiens 45-48 12120309-1 2002 The formation of a Pt skin layer with predominantly (111)-oriented facets induced by dissolution of Fe atoms in a Pt-Fe alloy for fuel cell applications is investigated for the first time by using in situ electrochemical STM in 0.1 M HClO4 solution. Platinum 19-21 sulfotransferase family 1A member 3 Homo sapiens 221-224 11792184-1 2002 The immobilization of thiol-derivatized DNA on a Au (111) single crystal surface by self-assembly has been investigated by electrochemical scanning tunneling microscopy (EC-STM). Sulfhydryl Compounds 22-27 sulfotransferase family 1A member 3 Homo sapiens 173-176 11815407-12 2002 Curcumin was sulfated by human phenol sulfotransferase isoenzymes SULT1A1 and SULT1A3. Curcumin 0-8 sulfotransferase family 1A member 3 Homo sapiens 78-85 12124314-0 2002 Phenol sulfotransferase, ST1A3, as the main enzyme catalyzing sulfation of troglitazone in human liver. Troglitazone 75-87 sulfotransferase family 1A member 3 Homo sapiens 25-30 12124314-2 2002 Experiments using the recombinant sulfotransferases and human liver cytosols indicated that phenol sulfotransferase (ST1A3) and estrogen sulfotransferase (ST1E4) were the sulfotransferases most active toward troglitazone. Troglitazone 208-220 sulfotransferase family 1A member 3 Homo sapiens 117-122 12124314-3 2002 Immunoblot analyses indicated that hepatic content of ST1A3 is about 13 times higher than that of ST1E4, suggesting that ST1A3 is mainly responsible for the sulfation of troglitazone in the liver. Troglitazone 170-182 sulfotransferase family 1A member 3 Homo sapiens 54-59 12124314-3 2002 Immunoblot analyses indicated that hepatic content of ST1A3 is about 13 times higher than that of ST1E4, suggesting that ST1A3 is mainly responsible for the sulfation of troglitazone in the liver. Troglitazone 170-182 sulfotransferase family 1A member 3 Homo sapiens 121-126 12162854-11 2002 Apomorphine sulfation was correlated with SULT1A1 activity in the liver (r(2) = 0.363, p = 0.005) and duodenum (r(2) = 0.494, p = 0.0005), but it did not correlate with SULT1A3 activity both in the liver and duodenum. Apomorphine 0-11 sulfotransferase family 1A member 3 Homo sapiens 169-176 11981900-14 2002 2: STM image (819x819 nm2) of a monolayer of [Cu.3]+ on Au(111) on mica. Gold 56-58 sulfotransferase family 1A member 3 Homo sapiens 3-6 11981900-14 2002 2: STM image (819x819 nm2) of a monolayer of [Cu.3]+ on Au(111) on mica. mica 67-71 sulfotransferase family 1A member 3 Homo sapiens 3-6 12227564-1 2002 Atomically resolved in situ STM images are presented for an underpotentially deposited (upd) cadmium layer on a Cu(111) electrode from a 10(-4) M CdCl2/10(-2) M HCl solution. Copper 112-114 sulfotransferase family 1A member 3 Homo sapiens 28-31 12227564-1 2002 Atomically resolved in situ STM images are presented for an underpotentially deposited (upd) cadmium layer on a Cu(111) electrode from a 10(-4) M CdCl2/10(-2) M HCl solution. Cadmium Chloride 146-151 sulfotransferase family 1A member 3 Homo sapiens 28-31 12227564-1 2002 Atomically resolved in situ STM images are presented for an underpotentially deposited (upd) cadmium layer on a Cu(111) electrode from a 10(-4) M CdCl2/10(-2) M HCl solution. Hydrochloric Acid 161-164 sulfotransferase family 1A member 3 Homo sapiens 28-31 12227564-4 2002 Furthermore the height modulation was simulated by a hard-sphere model for the Cd overlayer and shows remarkable agreement with the detailed tunneling current density distribution of the measured STM images. Cadmium 79-81 sulfotransferase family 1A member 3 Homo sapiens 196-199 12227574-1 2002 Using electrochemical STM we studied monolayer high Au islands on Au(100) electrodes in sulfuric acid as a function of the electrode potential. Gold 52-54 sulfotransferase family 1A member 3 Homo sapiens 22-25 12227579-7 2002 Hence, in this investigation electrodes with single Pd particles which were deposited from the STM tip onto the substrate are used. Palladium 52-54 sulfotransferase family 1A member 3 Homo sapiens 95-98 11603976-4 2001 Highly ordered domains (as determined from STM imaging) of the enantiomerically pure chiral redox polymers could be prepared via the interfacial reaction, over an HOPG substrate, of the bridging ligand in CH(2)Cl(2) and FeSO(4) in water. redox polymers 92-106 sulfotransferase family 1A member 3 Homo sapiens 43-46 11984005-6 2002 Recombinant STM was expressed in COS-7 cells. carbonyl sulfide 33-36 sulfotransferase family 1A member 3 Homo sapiens 12-15 11984005-7 2002 The substrate and linkage specificity of STM was examined using various oligosaccharides and O-glycosylated proteins as acceptor substrates. Oligosaccharides 72-88 sulfotransferase family 1A member 3 Homo sapiens 41-44 11984005-11 2002 Recombinant STM is an active GalNAc alpha2,6-sialyltransferase with Gal beta 1,3 GalNAc-O-Ser/Thr and (+/- Neu5Ac alpha 2,3) Gal beta 1,3GalNAc-O-Ser/Thr acceptor specificity. N-acetylgalactosaminuronic acid 29-35 sulfotransferase family 1A member 3 Homo sapiens 12-15 11984005-11 2002 Recombinant STM is an active GalNAc alpha2,6-sialyltransferase with Gal beta 1,3 GalNAc-O-Ser/Thr and (+/- Neu5Ac alpha 2,3) Gal beta 1,3GalNAc-O-Ser/Thr acceptor specificity. o-ser 88-93 sulfotransferase family 1A member 3 Homo sapiens 12-15 11984005-11 2002 Recombinant STM is an active GalNAc alpha2,6-sialyltransferase with Gal beta 1,3 GalNAc-O-Ser/Thr and (+/- Neu5Ac alpha 2,3) Gal beta 1,3GalNAc-O-Ser/Thr acceptor specificity. Threonine 94-97 sulfotransferase family 1A member 3 Homo sapiens 12-15 11984005-11 2002 Recombinant STM is an active GalNAc alpha2,6-sialyltransferase with Gal beta 1,3 GalNAc-O-Ser/Thr and (+/- Neu5Ac alpha 2,3) Gal beta 1,3GalNAc-O-Ser/Thr acceptor specificity. neu5ac alpha 2,3) gal beta 1,3galnac-o-ser 107-149 sulfotransferase family 1A member 3 Homo sapiens 12-15 11984005-11 2002 Recombinant STM is an active GalNAc alpha2,6-sialyltransferase with Gal beta 1,3 GalNAc-O-Ser/Thr and (+/- Neu5Ac alpha 2,3) Gal beta 1,3GalNAc-O-Ser/Thr acceptor specificity. Threonine 150-153 sulfotransferase family 1A member 3 Homo sapiens 12-15 11984005-17 2002 Because STM catalyzes the synthesis of O-glycans, cloning and characterization of its substrate specificity will contribute to the understanding of the molecular mechanisms underlying the aberrant glycosylation patterns of O-glycans and the formation of mucin-related antigens in human breast cancers. o-glycans 39-48 sulfotransferase family 1A member 3 Homo sapiens 8-11 11984005-17 2002 Because STM catalyzes the synthesis of O-glycans, cloning and characterization of its substrate specificity will contribute to the understanding of the molecular mechanisms underlying the aberrant glycosylation patterns of O-glycans and the formation of mucin-related antigens in human breast cancers. o-glycans 223-232 sulfotransferase family 1A member 3 Homo sapiens 8-11 11603976-4 2001 Highly ordered domains (as determined from STM imaging) of the enantiomerically pure chiral redox polymers could be prepared via the interfacial reaction, over an HOPG substrate, of the bridging ligand in CH(2)Cl(2) and FeSO(4) in water. (2)cl 207-212 sulfotransferase family 1A member 3 Homo sapiens 43-46 11603976-4 2001 Highly ordered domains (as determined from STM imaging) of the enantiomerically pure chiral redox polymers could be prepared via the interfacial reaction, over an HOPG substrate, of the bridging ligand in CH(2)Cl(2) and FeSO(4) in water. ferrous sulfate 220-227 sulfotransferase family 1A member 3 Homo sapiens 43-46 11603976-4 2001 Highly ordered domains (as determined from STM imaging) of the enantiomerically pure chiral redox polymers could be prepared via the interfacial reaction, over an HOPG substrate, of the bridging ligand in CH(2)Cl(2) and FeSO(4) in water. Water 231-236 sulfotransferase family 1A member 3 Homo sapiens 43-46 23686881-3 2001 STM images show two orientations of an adlayer of 2,2"-bipyridine. 2,2'-Dipyridyl 50-65 sulfotransferase family 1A member 3 Homo sapiens 0-3 11580546-1 2001 Fe nanostripes on W(110) are investigated by Kerr magnetometry and spin-polarized scanning tunneling microscopy (SP-STM). Iron 0-2 sulfotransferase family 1A member 3 Homo sapiens 116-119 11566410-4 2001 The most orderly polymer formed at 912 mg l(-1) initial phenol concentration, current density 32.9 mA cm(-2), NaCl concentration 120 g l(-1) and temperature 25 degrees C. Higher operational parameters yielded disorderly formed aggregates of the polymer in decreasing surface density on STM images. Polymers 17-24 sulfotransferase family 1A member 3 Homo sapiens 286-289 11566410-6 2001 FTIR analysis and enlarged STM image implied the repeating phenol units in the polymer structure. Phenol 59-65 sulfotransferase family 1A member 3 Homo sapiens 27-30 11566410-6 2001 FTIR analysis and enlarged STM image implied the repeating phenol units in the polymer structure. Polymers 79-86 sulfotransferase family 1A member 3 Homo sapiens 27-30 23696532-0 2001 Ordered nanostructures of a [2]catenane through self-assembly at surfaces--an STM study with sub-molecular resolution. [2]catenane 28-39 sulfotransferase family 1A member 3 Homo sapiens 78-81 11531502-1 2001 STM images show that vicinal Au(788) surfaces are made up of a uniform array of (111)-oriented terraces of similar width ( approximately 3.8 nm). Gold 29-31 sulfotransferase family 1A member 3 Homo sapiens 0-3 11485566-4 2001 The site of cleavage in MDP-STM(ACE) was identified by MS as the Arg(374)-Ser(375) bond, corresponding to the Arg(1203)-Ser(1204) secretase cleavage site in somatic ACE. Arginine 65-68 sulfotransferase family 1A member 3 Homo sapiens 28-31 11485566-4 2001 The site of cleavage in MDP-STM(ACE) was identified by MS as the Arg(374)-Ser(375) bond, corresponding to the Arg(1203)-Ser(1204) secretase cleavage site in somatic ACE. Serine 74-77 sulfotransferase family 1A member 3 Homo sapiens 28-31 11485566-4 2001 The site of cleavage in MDP-STM(ACE) was identified by MS as the Arg(374)-Ser(375) bond, corresponding to the Arg(1203)-Ser(1204) secretase cleavage site in somatic ACE. Arginine 110-113 sulfotransferase family 1A member 3 Homo sapiens 28-31 11485566-4 2001 The site of cleavage in MDP-STM(ACE) was identified by MS as the Arg(374)-Ser(375) bond, corresponding to the Arg(1203)-Ser(1204) secretase cleavage site in somatic ACE. Serine 120-123 sulfotransferase family 1A member 3 Homo sapiens 28-31 11485566-5 2001 The release of MDP-STM(ACE) and ACE from the cells was inhibited in an identical manner by batimastat and two other hydroxamic acid-based zinc metallosecretase inhibitors. batimastat 91-101 sulfotransferase family 1A member 3 Homo sapiens 19-22 11478778-6 2001 M-form (SULT1A3) PST showed high activity with the flavonoids but not with the isoflavonoids. Flavonoids 51-61 sulfotransferase family 1A member 3 Homo sapiens 8-15 23696532-2 2001 Large two-dimensional crystals of [2]catenane were formed on HOPG through self-assembly--the picture shows a 15x15 nm(2) STM image of the surface-bound structure. [2]catenane 34-45 sulfotransferase family 1A member 3 Homo sapiens 121-124 11472438-9 2001 Only sTM was significantly lower in patients with both LAC and thrombosis than in patients without both these features after adjustment for serum creatinine concentrations. Creatinine 146-156 sulfotransferase family 1A member 3 Homo sapiens 5-8 11254346-0 2001 Electron-Transfer-Induced Molecular Reorientations: The Benzoquinone/Hydroquinone Reaction at Pd(111)-(square3xsquare3)R30 degrees -I Studied by EC-STM. quinone 56-68 sulfotransferase family 1A member 3 Homo sapiens 148-151 11315838-8 2001 Significant postprandial increases in MG, 3-DG, and D-lactate occurred after the STM. Pyruvaldehyde 38-40 sulfotransferase family 1A member 3 Homo sapiens 81-84 11397879-4 2001 Hepatic SULT1A3 (dopamine) was expressed at high levels early in development, but decreased substantially in late fetal/early neonatal liver and was essentially absent from the adult liver. Dopamine 17-25 sulfotransferase family 1A member 3 Homo sapiens 8-15 11254346-0 2001 Electron-Transfer-Induced Molecular Reorientations: The Benzoquinone/Hydroquinone Reaction at Pd(111)-(square3xsquare3)R30 degrees -I Studied by EC-STM. hydroquinone 69-81 sulfotransferase family 1A member 3 Homo sapiens 148-151 11254346-1 2001 The benzoquinone/hydroquinone (Q/H(2)Q) redox reaction has been studied by electrochemical-scanning tunneling microscopy (EC-STM) at a Pd(111)-(square3xsquare3)R30 degrees -I electrode surface in a solution that contained 10(-4) M H(2)Q in 0.05 M H(2)SO(4); iodine-pretreatment of the Pd(111) surface was to prevent chemisorption of organic-derived species. quinone 4-16 sulfotransferase family 1A member 3 Homo sapiens 125-128 11254346-1 2001 The benzoquinone/hydroquinone (Q/H(2)Q) redox reaction has been studied by electrochemical-scanning tunneling microscopy (EC-STM) at a Pd(111)-(square3xsquare3)R30 degrees -I electrode surface in a solution that contained 10(-4) M H(2)Q in 0.05 M H(2)SO(4); iodine-pretreatment of the Pd(111) surface was to prevent chemisorption of organic-derived species. hydroquinone 17-29 sulfotransferase family 1A member 3 Homo sapiens 125-128 11254346-1 2001 The benzoquinone/hydroquinone (Q/H(2)Q) redox reaction has been studied by electrochemical-scanning tunneling microscopy (EC-STM) at a Pd(111)-(square3xsquare3)R30 degrees -I electrode surface in a solution that contained 10(-4) M H(2)Q in 0.05 M H(2)SO(4); iodine-pretreatment of the Pd(111) surface was to prevent chemisorption of organic-derived species. Palladium 135-137 sulfotransferase family 1A member 3 Homo sapiens 125-128 11254346-4 2001 Unfortunately, at potentials where only Q would be present in solution, I-catalyzed corrosion of the Pd starts to occur, which leads to noise-laden EC-STM images. Palladium 101-103 sulfotransferase family 1A member 3 Homo sapiens 151-154 11508820-0 2001 Fractal analysis of STM images of photochemical polymer of coniferyl alcohol. Polymers 48-55 sulfotransferase family 1A member 3 Homo sapiens 20-23 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. 4-thiopyridine 39-57 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. 4-thiopyridine 59-62 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. zinc(ii) 5,15-bis(4-octadecyloxyphenyl)porphyrin 101-149 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. Metals 168-173 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. Porphyrins 140-149 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. Nickel(2+) 202-212 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-1 2001 STM gold tips chemically modified with 4-mercaptopyridine (4MP) were found capable of discriminating zinc(II) 5,15-bis(4-octadecyloxyphenyl)porphyrin (Por-Zn) from its metal-free porphyrin (Por-2H) and nickel(II) complexes (Por-Ni) in the mixed monolayers of these compounds, spontaneously formed at the solution/graphite interface. Graphite 313-321 sulfotransferase family 1A member 3 Homo sapiens 0-3 11289431-2 2001 The porphyrin centers in STM images observed with 4MP-modified tips exhibited bright spots, while those measured with unmodified tips exhibited the porphyrin centers as dark depressions. 4-thiopyridine 50-53 sulfotransferase family 1A member 3 Homo sapiens 25-28 11181495-6 2001 They showed high affinities toward p-nitrophenol and 6-hydroxymelatonin as found in human ST1A3. 4-nitrophenol 35-48 sulfotransferase family 1A member 3 Homo sapiens 90-95 11181495-6 2001 They showed high affinities toward p-nitrophenol and 6-hydroxymelatonin as found in human ST1A3. 6-hydroxymelatonin 53-71 sulfotransferase family 1A member 3 Homo sapiens 90-95 11181495-7 2001 These forms also showed high activities toward umbelliferone and naringenin, but very low activities toward catecholamines, representative substrates of human ST1A5. Catecholamines 108-122 sulfotransferase family 1A member 3 Homo sapiens 159-164 11508820-0 2001 Fractal analysis of STM images of photochemical polymer of coniferyl alcohol. coniferyl alcohol 59-76 sulfotransferase family 1A member 3 Homo sapiens 20-23 11177855-1 2001 The structural response of the Cu(110) surface to H2 gas pressures ranging from 10(-13) to 1 bar is studied using a novel high-pressure scanning tunneling microscope (HP-STM). Copper 31-33 sulfotransferase family 1A member 3 Homo sapiens 170-173 11465392-2 2001 The aim was to see whether mefenamic acid and salicylic acid had different inhibition profiles for SULT1A1 (substrate: 4-nitrophenol) and SULT1A3 (dopamine) activities and on (-)-salbutamol and minoxidil sulphation rates in the human adult and mid-gestational foetal livers. Mefenamic Acid 27-41 sulfotransferase family 1A member 3 Homo sapiens 138-145 11465392-2 2001 The aim was to see whether mefenamic acid and salicylic acid had different inhibition profiles for SULT1A1 (substrate: 4-nitrophenol) and SULT1A3 (dopamine) activities and on (-)-salbutamol and minoxidil sulphation rates in the human adult and mid-gestational foetal livers. Salicylic Acid 46-60 sulfotransferase family 1A member 3 Homo sapiens 138-145 11465392-7 2001 With mefenamic acid as an inhibitor, the IC50 (microM) for SULT1A1 was 0.2 +/- 0.004 (adult) and 0.01 +/- 0.002 (foetus; p = 0.001); for SULT1A3 it was 76 +/- 6 (adult) and 77 +/- 13 (foetus; p = 0.889); for the rate of ( )-salbutamol sulphation it was 0.07 +/- 0.005 (adult) and not determinable (foetus) and for minoxidil sulphation it was 1.6 +/- 0.7 (adult) and 0.15 +/- 0.04 (foetus; p = 0.076). Mefenamic Acid 5-19 sulfotransferase family 1A member 3 Homo sapiens 137-144 11465392-9 2001 With salicylic acid as an inhibitor, the IC50 (microM) for SULT1A1 was 30 +/- 2 (adult) and 25 +/- 1 (foetus; p = 0.011); for SULT1A3 it was 690 +/- 36 (adult) and 570 +/- 16 (foetus; p = 0.229); for the rate of ( )-salbutamol sulphation it was 93 +/- 11 (adult) and 344 +/- 42 (foetus; p = 0.010); with minoxidil as substrate, the IC50 was not determinable. Salicylic Acid 5-19 sulfotransferase family 1A member 3 Homo sapiens 126-133 11465392-11 2001 In summary, SULT1A1, SULT1A3 and the sulphotransferases towards (-)-salbutamol and minoxidil had measurable activities in the mid-gestational human foetal liver. Albuterol 64-78 sulfotransferase family 1A member 3 Homo sapiens 21-28 11465392-11 2001 In summary, SULT1A1, SULT1A3 and the sulphotransferases towards (-)-salbutamol and minoxidil had measurable activities in the mid-gestational human foetal liver. Minoxidil 83-92 sulfotransferase family 1A member 3 Homo sapiens 21-28 11465392-12 2001 Mefenamic acid was a more potent inhibitor than salicylic acid of both human adult and foetal liver SULT1A1 and SULT1A3 activities. Mefenamic Acid 0-14 sulfotransferase family 1A member 3 Homo sapiens 112-119 11465392-12 2001 Mefenamic acid was a more potent inhibitor than salicylic acid of both human adult and foetal liver SULT1A1 and SULT1A3 activities. Salicylic Acid 48-62 sulfotransferase family 1A member 3 Homo sapiens 112-119 11181440-7 2001 The recent identification in mammary cytosols of detectable sulfotransferase isoforms (SULT1A1 and SULT1A3), which have high catalytic efficiency for activating N:-hydroxylated heterocyclic amines (HCAs, mutagens in cooked meat), offers a more important role for these enzymes in the metabolic activation of genotoxins in the breast. Amines 190-196 sulfotransferase family 1A member 3 Homo sapiens 99-106 11236808-4 2001 Salbutamol is metabolised almost exclusively by sulphotransferase (SULT) 1A3 to an inactive metabolite. Albuterol 0-10 sulfotransferase family 1A member 3 Homo sapiens 48-76 11177815-1 2001 We present a theory for recent STM studies of Zn impurities in the superconductor Bi2Sr2CaCu2O8+delta, using insights from NMR experiments which show that there is a net S = 1/2 moment on the Cu ions near the Zn. Zinc 46-48 sulfotransferase family 1A member 3 Homo sapiens 31-34 11177815-1 2001 We present a theory for recent STM studies of Zn impurities in the superconductor Bi2Sr2CaCu2O8+delta, using insights from NMR experiments which show that there is a net S = 1/2 moment on the Cu ions near the Zn. Copper 90-92 sulfotransferase family 1A member 3 Homo sapiens 31-34 11177815-1 2001 We present a theory for recent STM studies of Zn impurities in the superconductor Bi2Sr2CaCu2O8+delta, using insights from NMR experiments which show that there is a net S = 1/2 moment on the Cu ions near the Zn. Zinc 209-211 sulfotransferase family 1A member 3 Homo sapiens 31-34 11264787-5 2001 The levels of IL-4, IL-6, beta2 -m, sIL-2R, sVCAM-1, sP-selectin, and sE-selectin in SLE patients with elevated sTM levels were higher than those in the SLE patients without elevated sTM levels. se-selectin 70-81 sulfotransferase family 1A member 3 Homo sapiens 112-115 11236808-16 2001 Functionally significant genetic polymorphisms have been identified for beta2-adrenoceptors, SULT1A3 and organic action transporters, all of which affect the disposition or action of levosalbutamol. Levalbuterol 183-197 sulfotransferase family 1A member 3 Homo sapiens 93-100 10375162-3 1999 ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively. 4-nitrophenol 128-141 sulfotransferase family 1A member 3 Homo sapiens 72-77 10608851-2 1999 Humans are one of the few species that produce large amounts of catecholamine sulfates, and they have evolved a specific sulfotransferase, SULT1A3 (M-PST), to catalyze the formation of these conjugates. catecholamine sulfates 64-86 sulfotransferase family 1A member 3 Homo sapiens 139-146 10608851-4 1999 To further our understanding of the molecular basis for the unique substrate selectivity of this enzyme, we have solved the crystal structure of human SULT1A3, complexed with 3"-phosphoadenosine 5"-phosphate (PAP), at 2.5 A resolution and carried out quantitative structure-activity relationship (QSAR) analysis with a series of phenols and catechols. adenosine 3'-phosphate-5'-phosphate 175-207 sulfotransferase family 1A member 3 Homo sapiens 151-158 10608851-4 1999 To further our understanding of the molecular basis for the unique substrate selectivity of this enzyme, we have solved the crystal structure of human SULT1A3, complexed with 3"-phosphoadenosine 5"-phosphate (PAP), at 2.5 A resolution and carried out quantitative structure-activity relationship (QSAR) analysis with a series of phenols and catechols. adenosine 3'-phosphate-5'-phosphate 209-212 sulfotransferase family 1A member 3 Homo sapiens 151-158 10608851-4 1999 To further our understanding of the molecular basis for the unique substrate selectivity of this enzyme, we have solved the crystal structure of human SULT1A3, complexed with 3"-phosphoadenosine 5"-phosphate (PAP), at 2.5 A resolution and carried out quantitative structure-activity relationship (QSAR) analysis with a series of phenols and catechols. Phenols 329-336 sulfotransferase family 1A member 3 Homo sapiens 151-158 10608851-4 1999 To further our understanding of the molecular basis for the unique substrate selectivity of this enzyme, we have solved the crystal structure of human SULT1A3, complexed with 3"-phosphoadenosine 5"-phosphate (PAP), at 2.5 A resolution and carried out quantitative structure-activity relationship (QSAR) analysis with a series of phenols and catechols. Catechols 341-350 sulfotransferase family 1A member 3 Homo sapiens 151-158 10608851-8 1999 We also investigated further the role of Glu(146) in SULT1A3 using site-directed mutagenesis and showed that it plays a key role not only in defining selectivity for dopamine but also in preventing many phenolic xenobiotics from binding to the enzyme. Glutamic Acid 41-44 sulfotransferase family 1A member 3 Homo sapiens 53-60 10608851-8 1999 We also investigated further the role of Glu(146) in SULT1A3 using site-directed mutagenesis and showed that it plays a key role not only in defining selectivity for dopamine but also in preventing many phenolic xenobiotics from binding to the enzyme. Dopamine 166-174 sulfotransferase family 1A member 3 Homo sapiens 53-60 10543947-3 1999 SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. Alkanesulfonates 21-31 sulfotransferase family 1A member 3 Homo sapiens 0-7 10543947-3 1999 SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. Catecholamines 32-46 sulfotransferase family 1A member 3 Homo sapiens 0-7 10543947-3 1999 SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. Dopamine 55-63 sulfotransferase family 1A member 3 Homo sapiens 0-7 10543947-3 1999 SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. Epinephrine 65-75 sulfotransferase family 1A member 3 Homo sapiens 0-7 10543947-3 1999 SULT1A3 specifically sulfonates catecholamines such as dopamine, adrenaline and noradrenaline. Norepinephrine 80-93 sulfotransferase family 1A member 3 Homo sapiens 0-7 10543947-4 1999 The crystal structure of SULT1A3 with a sulfate bound at the active site, has been determined at 2.4 A resolution. Sulfates 40-47 sulfotransferase family 1A member 3 Homo sapiens 25-32 10423517-6 1999 Kinetic parameters for p-nitrophenol for p-nitrophenol sulfation supported the slight decrease in sulfating activities at 4 microM (K(m), 0.82 vs. 1.75 microM; V(max), 13.2 vs. 13.1 nmol/min/nmol SULT, respectively, for ST1A3*1 and *2). 4-nitrophenol 23-36 sulfotransferase family 1A member 3 Homo sapiens 220-225 10423517-6 1999 Kinetic parameters for p-nitrophenol for p-nitrophenol sulfation supported the slight decrease in sulfating activities at 4 microM (K(m), 0.82 vs. 1.75 microM; V(max), 13.2 vs. 13.1 nmol/min/nmol SULT, respectively, for ST1A3*1 and *2). 4-nitrophenol 41-54 sulfotransferase family 1A member 3 Homo sapiens 220-225 10423517-7 1999 p-Nitrophenyl sulfate-dependent 2-naphthol sulfation by ST1A3*2 was 69% of that by ST1A3*1 (p<0.05). 4-nitrophenyl sulfate 0-21 sulfotransferase family 1A member 3 Homo sapiens 56-61 10423517-7 1999 p-Nitrophenyl sulfate-dependent 2-naphthol sulfation by ST1A3*2 was 69% of that by ST1A3*1 (p<0.05). 4-nitrophenyl sulfate 0-21 sulfotransferase family 1A member 3 Homo sapiens 83-88 10423517-7 1999 p-Nitrophenyl sulfate-dependent 2-naphthol sulfation by ST1A3*2 was 69% of that by ST1A3*1 (p<0.05). 2-naphthol 32-42 sulfotransferase family 1A member 3 Homo sapiens 56-61 10423517-7 1999 p-Nitrophenyl sulfate-dependent 2-naphthol sulfation by ST1A3*2 was 69% of that by ST1A3*1 (p<0.05). 2-naphthol 32-42 sulfotransferase family 1A member 3 Homo sapiens 83-88 10423517-9 1999 The lower p-nitrophenol sulfating activity of ST1A3*2 may explain the lower platelet p-nitrophenol sulfation in ST1A3*2 homozygotes. 4-nitrophenol 10-23 sulfotransferase family 1A member 3 Homo sapiens 46-51 10423517-9 1999 The lower p-nitrophenol sulfating activity of ST1A3*2 may explain the lower platelet p-nitrophenol sulfation in ST1A3*2 homozygotes. 4-nitrophenol 10-23 sulfotransferase family 1A member 3 Homo sapiens 112-117 10423517-9 1999 The lower p-nitrophenol sulfating activity of ST1A3*2 may explain the lower platelet p-nitrophenol sulfation in ST1A3*2 homozygotes. 4-nitrophenol 85-98 sulfotransferase family 1A member 3 Homo sapiens 46-51 10423517-9 1999 The lower p-nitrophenol sulfating activity of ST1A3*2 may explain the lower platelet p-nitrophenol sulfation in ST1A3*2 homozygotes. 4-nitrophenol 85-98 sulfotransferase family 1A member 3 Homo sapiens 112-117 10423517-10 1999 Protein instability and ST1A3 gene regulation may be both involved in the polymorphism of p-nitrophenol sulfation in human tissues. 4-nitrophenol 90-103 sulfotransferase family 1A member 3 Homo sapiens 24-29 10336855-5 1999 Here we have validated a number of heterologous expression systems for producing the human dopamine-metabolizing sulfotransferase SULT1A3, including Escherichia coli, Saccharomyces cerevisiae, COS-7, and V79 cells, by comparison of Km values of the recombinant enzyme in cell extracts with enzyme present in human platelets and with recombinant enzyme purified to homogeneity following E. coli expression. Dopamine 91-99 sulfotransferase family 1A member 3 Homo sapiens 130-137 10336855-7 1999 Expression of SULT1A3 was achieved in all cell types, and the Km for dopamine under the conditions applied was approximately 1 microM in all heterologous systems studied, which compared favorably with the value determined with human platelets. Dopamine 69-77 sulfotransferase family 1A member 3 Homo sapiens 14-21 11156440-0 2000 Fractal analysis of STM images of lignin polymer obtained by in vitro synthesis. Lignin 34-40 sulfotransferase family 1A member 3 Homo sapiens 20-23 11017499-0 2000 Bistability in scanning tunneling spectroscopy of Ga-terminated Si(111) Bistable electron transport, a phenomenon usually associated with double-barrier structures, has been observed with a conventional STM junction formed between a metal tip and a Ga-terminated Si(111) surface at 77 K. Large hysteresis loops appear in the current-voltage characteristics when electrons are injected from the tip to the surface. Gallium 50-52 sulfotransferase family 1A member 3 Homo sapiens 203-206 11017499-0 2000 Bistability in scanning tunneling spectroscopy of Ga-terminated Si(111) Bistable electron transport, a phenomenon usually associated with double-barrier structures, has been observed with a conventional STM junction formed between a metal tip and a Ga-terminated Si(111) surface at 77 K. Large hysteresis loops appear in the current-voltage characteristics when electrons are injected from the tip to the surface. Silicon 64-66 sulfotransferase family 1A member 3 Homo sapiens 203-206 11017499-0 2000 Bistability in scanning tunneling spectroscopy of Ga-terminated Si(111) Bistable electron transport, a phenomenon usually associated with double-barrier structures, has been observed with a conventional STM junction formed between a metal tip and a Ga-terminated Si(111) surface at 77 K. Large hysteresis loops appear in the current-voltage characteristics when electrons are injected from the tip to the surface. Metals 233-238 sulfotransferase family 1A member 3 Homo sapiens 203-206 11017499-0 2000 Bistability in scanning tunneling spectroscopy of Ga-terminated Si(111) Bistable electron transport, a phenomenon usually associated with double-barrier structures, has been observed with a conventional STM junction formed between a metal tip and a Ga-terminated Si(111) surface at 77 K. Large hysteresis loops appear in the current-voltage characteristics when electrons are injected from the tip to the surface. Gallium 249-251 sulfotransferase family 1A member 3 Homo sapiens 203-206 11017499-0 2000 Bistability in scanning tunneling spectroscopy of Ga-terminated Si(111) Bistable electron transport, a phenomenon usually associated with double-barrier structures, has been observed with a conventional STM junction formed between a metal tip and a Ga-terminated Si(111) surface at 77 K. Large hysteresis loops appear in the current-voltage characteristics when electrons are injected from the tip to the surface. Silicon 263-265 sulfotransferase family 1A member 3 Homo sapiens 203-206 10508381-0 1999 STM Images of Individual Porphyrin Molecules on Cu(100) and Cu(111) Surfaces. Copper 48-50 sulfotransferase family 1A member 3 Homo sapiens 0-3 10508381-0 1999 STM Images of Individual Porphyrin Molecules on Cu(100) and Cu(111) Surfaces. Copper 60-62 sulfotransferase family 1A member 3 Homo sapiens 0-3 10441143-4 1999 SULT1A1 favors simple phenolic substrates such as p-nitrophenol, whereas SULT1A3 prefers monoamine substrates such as dopamine. monoamine 89-98 sulfotransferase family 1A member 3 Homo sapiens 73-80 10441143-4 1999 SULT1A1 favors simple phenolic substrates such as p-nitrophenol, whereas SULT1A3 prefers monoamine substrates such as dopamine. Dopamine 118-126 sulfotransferase family 1A member 3 Homo sapiens 73-80 10441143-7 1999 The mutation E146A in SULT1A3 resulted in a SULT1A1-like protein with respect to the Michaelis constant for both simple phenols and monoamine compounds. Phenols 120-127 sulfotransferase family 1A member 3 Homo sapiens 22-29 10441143-7 1999 The mutation E146A in SULT1A3 resulted in a SULT1A1-like protein with respect to the Michaelis constant for both simple phenols and monoamine compounds. monoamine 132-141 sulfotransferase family 1A member 3 Homo sapiens 22-29 10441143-8 1999 When comparing the specificity of SULT1A3 toward tyramine with that for p-ethylphenol (which differs from tyramine in having no amine group on the carbon side chain), we saw a 200-fold preference for tyramine. Tyramine 49-57 sulfotransferase family 1A member 3 Homo sapiens 34-41 10441143-8 1999 When comparing the specificity of SULT1A3 toward tyramine with that for p-ethylphenol (which differs from tyramine in having no amine group on the carbon side chain), we saw a 200-fold preference for tyramine. 4-ethylphenol 72-85 sulfotransferase family 1A member 3 Homo sapiens 34-41 10441143-8 1999 When comparing the specificity of SULT1A3 toward tyramine with that for p-ethylphenol (which differs from tyramine in having no amine group on the carbon side chain), we saw a 200-fold preference for tyramine. Tyramine 106-114 sulfotransferase family 1A member 3 Homo sapiens 34-41 10441143-8 1999 When comparing the specificity of SULT1A3 toward tyramine with that for p-ethylphenol (which differs from tyramine in having no amine group on the carbon side chain), we saw a 200-fold preference for tyramine. Amines 52-57 sulfotransferase family 1A member 3 Homo sapiens 34-41 10441143-8 1999 When comparing the specificity of SULT1A3 toward tyramine with that for p-ethylphenol (which differs from tyramine in having no amine group on the carbon side chain), we saw a 200-fold preference for tyramine. Carbon 147-153 sulfotransferase family 1A member 3 Homo sapiens 34-41 10441143-8 1999 When comparing the specificity of SULT1A3 toward tyramine with that for p-ethylphenol (which differs from tyramine in having no amine group on the carbon side chain), we saw a 200-fold preference for tyramine. Tyramine 106-114 sulfotransferase family 1A member 3 Homo sapiens 34-41 10441143-9 1999 The kinetic data obtained with the E146A mutant of SULT1A3 for these two substrates clearly showed that this protein preferred substrates without an amine group attached. Amines 149-154 sulfotransferase family 1A member 3 Homo sapiens 51-58 10441143-10 1999 Second, changing the glutamic acid at position 146 of SULT1A3 to a glutamine, thereby neutralizing the negative charge at this position, resulted in a 360-fold decrease in the specificity constant for dopamine. Glutamic Acid 21-34 sulfotransferase family 1A member 3 Homo sapiens 54-61 10441143-10 1999 Second, changing the glutamic acid at position 146 of SULT1A3 to a glutamine, thereby neutralizing the negative charge at this position, resulted in a 360-fold decrease in the specificity constant for dopamine. Glutamine 67-76 sulfotransferase family 1A member 3 Homo sapiens 54-61 10441143-10 1999 Second, changing the glutamic acid at position 146 of SULT1A3 to a glutamine, thereby neutralizing the negative charge at this position, resulted in a 360-fold decrease in the specificity constant for dopamine. Dopamine 201-209 sulfotransferase family 1A member 3 Homo sapiens 54-61 10441143-11 1999 The results provide strong evidence that residue 146 is crucial in determining the substrate specificity of both SULT1A1 and SULT1A3 and suggest that there is a direct interaction between glutamic acid 146 in SULT1A3 and monoamine substrates. Glutamic Acid 188-201 sulfotransferase family 1A member 3 Homo sapiens 125-132 10441143-11 1999 The results provide strong evidence that residue 146 is crucial in determining the substrate specificity of both SULT1A1 and SULT1A3 and suggest that there is a direct interaction between glutamic acid 146 in SULT1A3 and monoamine substrates. Glutamic Acid 188-201 sulfotransferase family 1A member 3 Homo sapiens 209-216 10441143-11 1999 The results provide strong evidence that residue 146 is crucial in determining the substrate specificity of both SULT1A1 and SULT1A3 and suggest that there is a direct interaction between glutamic acid 146 in SULT1A3 and monoamine substrates. monoamine 221-230 sulfotransferase family 1A member 3 Homo sapiens 125-132 10375162-3 1999 ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively. 4-nitrophenol 128-141 sulfotransferase family 1A member 3 Homo sapiens 79-84 10386253-5 1999 The sulphotransferase isoenzyme responsible for production of DA sulphate in humans (SULT1A3) has been cloned and shown to be expressed in large quantities in the gastro-intestinal tract, but not in liver. da sulphate 62-73 sulfotransferase family 1A member 3 Homo sapiens 85-92 10199779-4 1999 The apparent Km values of 3,3"-T2 and T3 [at 50 micromol/L 3"-phosphoadenosine-5"-phosphosulfate (PAPS)] were 1.02 and 54.9 micromol/L for liver cytosol, 0.64 and 27.8 micromol/L for kidney cytosol, 0.14 and 29.1 micromol/L for SULT1A1, and 33 and 112 micromol/L for SULT1A3, respectively. 3,3'-diiodothyronine 26-33 sulfotransferase family 1A member 3 Homo sapiens 267-274 10199779-8 1999 These results indicate similar substrate specificities for iodothyronine sulfation by native human liver and kidney sulfotransferases and recombinant SULT1A1 and SULT1A3. iodothyronine 59-72 sulfotransferase family 1A member 3 Homo sapiens 162-169 10090207-1 1999 Water adsorption measured by STM. Water 0-5 sulfotransferase family 1A member 3 Homo sapiens 29-32 10090207-2 1999 When operating scanning probe microscopes, like STM or AFM, under ambient conditions, the presence of water on the sample and the tip always plays an important role. Water 102-107 sulfotransferase family 1A member 3 Homo sapiens 48-51 10090207-3 1999 The water not only influences the structure of the sample itself, but also the imaging process; in the case of the STM using a wet etched w-tip, by interfering with the electron transfer process, and in the case of the AFM, due to the capillary forces in the micro Newton range that dominate the tip surface interaction forces. Water 4-9 sulfotransferase family 1A member 3 Homo sapiens 115-118 10090207-4 1999 In this paper, the distribution and the amount of adsorbed water on different surfaces is investigated with the help of the STM, which can provide information by imaging and by current/distance spectroscopy. Water 59-64 sulfotransferase family 1A member 3 Homo sapiens 124-127 9882633-1 1999 Human aryl sulphotransferase (HAST) 1, HAST3, HAST4 and HAST4v share greater than 90% sequence identity, but vary markedly in their ability to catalyse the sulphonation of dopamine and p-nitrophenol. Dopamine 172-180 sulfotransferase family 1A member 3 Homo sapiens 30-34 9882633-1 1999 Human aryl sulphotransferase (HAST) 1, HAST3, HAST4 and HAST4v share greater than 90% sequence identity, but vary markedly in their ability to catalyse the sulphonation of dopamine and p-nitrophenol. Dopamine 172-180 sulfotransferase family 1A member 3 Homo sapiens 39-44 9882633-1 1999 Human aryl sulphotransferase (HAST) 1, HAST3, HAST4 and HAST4v share greater than 90% sequence identity, but vary markedly in their ability to catalyse the sulphonation of dopamine and p-nitrophenol. 4-nitrophenol 185-198 sulfotransferase family 1A member 3 Homo sapiens 30-34 9882633-1 1999 Human aryl sulphotransferase (HAST) 1, HAST3, HAST4 and HAST4v share greater than 90% sequence identity, but vary markedly in their ability to catalyse the sulphonation of dopamine and p-nitrophenol. 4-nitrophenol 185-198 sulfotransferase family 1A member 3 Homo sapiens 39-44 9882633-5 1999 A single amino acid change in HAST1 (A146E) was able to change the specificity for p-nitrophenol to that of HAST3. 4-nitrophenol 83-96 sulfotransferase family 1A member 3 Homo sapiens 108-113 9882633-8 1999 These findings suggest that a co-ordinated change of multiple amino acids in HAST proteins is needed to alter the substrate specificities of these enzymes towards dopamine, whereas a single amino acid at position 146 determines p-nitrophenol affinity. Dopamine 163-171 sulfotransferase family 1A member 3 Homo sapiens 77-81 9882633-8 1999 These findings suggest that a co-ordinated change of multiple amino acids in HAST proteins is needed to alter the substrate specificities of these enzymes towards dopamine, whereas a single amino acid at position 146 determines p-nitrophenol affinity. 4-nitrophenol 228-241 sulfotransferase family 1A member 3 Homo sapiens 77-81 9855620-2 1998 In humans, catecholamines such as dopamine are extensively sulfated, and a SULT isoform (SULT1A3 or the monoamine-sulfating form of phenolsulfotransferase) has evolved with considerable selectivity for dopamine and other biogenic amines. monoamine 104-113 sulfotransferase family 1A member 3 Homo sapiens 89-96 9855620-2 1998 In humans, catecholamines such as dopamine are extensively sulfated, and a SULT isoform (SULT1A3 or the monoamine-sulfating form of phenolsulfotransferase) has evolved with considerable selectivity for dopamine and other biogenic amines. Dopamine 202-210 sulfotransferase family 1A member 3 Homo sapiens 89-96 9855620-0 1998 A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3. DL-Glutamic acid 21-27 sulfotransferase family 1A member 3 Homo sapiens 101-108 9855620-3 1998 To investigate the molecular basis for this selectivity, we identified a region of SULT1A3, which, we hypothesized, contributes to its preference for biogenic amines, and mutated two amino acids within this domain to the corresponding residues in a closely related but functionally distinct phenol sulfotransferase, SULT1A1 (H143Y and E146A). Amines 159-165 sulfotransferase family 1A member 3 Homo sapiens 83-90 9855620-5 1998 These experiments confirm the functional role of Glu146 in the selectivity of SULT1A3 for biogenic amines and suggest that this region is a key determinant of sulfotransferase substrate specificity. DL-Glutamic acid 49-55 sulfotransferase family 1A member 3 Homo sapiens 78-85 9855620-5 1998 These experiments confirm the functional role of Glu146 in the selectivity of SULT1A3 for biogenic amines and suggest that this region is a key determinant of sulfotransferase substrate specificity. Amines 99-105 sulfotransferase family 1A member 3 Homo sapiens 78-85 9830917-1 1998 STM Healthcare is a division of the Recticel Group which has been actively involved in the production and use of polyurethane foams for the past 40 years, and is now one of Europe"s leading manufacturers of polyurethane foam for insulation, packaging, filtration, aerospace, the automotive and furniture industries, domestic and specialist bedding and seating products. Polyurethanes 113-125 sulfotransferase family 1A member 3 Homo sapiens 0-3 9830917-1 1998 STM Healthcare is a division of the Recticel Group which has been actively involved in the production and use of polyurethane foams for the past 40 years, and is now one of Europe"s leading manufacturers of polyurethane foam for insulation, packaging, filtration, aerospace, the automotive and furniture industries, domestic and specialist bedding and seating products. polyurethane foam 113-130 sulfotransferase family 1A member 3 Homo sapiens 0-3 9566733-7 1998 Partially purified human platelet TL PST tested with minoxidil and dopamine showed identical thermal stabilities and similar responses to the inhibitors 2,6-dichloro-4-nitrophenol (DCNP) and NaCl. Minoxidil 53-62 sulfotransferase family 1A member 3 Homo sapiens 34-40 9566748-6 1998 The observed differences in the ST1A3 and TL-PST mRNA levels were consistent with the differences in p-nitrophenol and dopamine sulfations. 4-nitrophenol 101-114 sulfotransferase family 1A member 3 Homo sapiens 32-37 9566748-6 1998 The observed differences in the ST1A3 and TL-PST mRNA levels were consistent with the differences in p-nitrophenol and dopamine sulfations. 4-nitrophenol 101-114 sulfotransferase family 1A member 3 Homo sapiens 42-48 10904559-0 1998 Water role in STM imaging of organic films. Water 0-5 sulfotransferase family 1A member 3 Homo sapiens 14-17 9723178-6 1998 The STM gene encoding the monoamine neurotransmitter-preferring PST (M-PST) exhibits a lower level of similarity relative to STP1 and STP2. monoamine 26-35 sulfotransferase family 1A member 3 Homo sapiens 4-7 9566748-6 1998 The observed differences in the ST1A3 and TL-PST mRNA levels were consistent with the differences in p-nitrophenol and dopamine sulfations. Dopamine 119-127 sulfotransferase family 1A member 3 Homo sapiens 32-37 9566733-7 1998 Partially purified human platelet TL PST tested with minoxidil and dopamine showed identical thermal stabilities and similar responses to the inhibitors 2,6-dichloro-4-nitrophenol (DCNP) and NaCl. Dopamine 67-75 sulfotransferase family 1A member 3 Homo sapiens 34-40 9566748-6 1998 The observed differences in the ST1A3 and TL-PST mRNA levels were consistent with the differences in p-nitrophenol and dopamine sulfations. Dopamine 119-127 sulfotransferase family 1A member 3 Homo sapiens 42-48 9566733-8 1998 To characterize the activity of TL PST toward minoxidil, several biochemical properties of the enzyme expressed from a human liver cDNA clone were investigated. Minoxidil 46-55 sulfotransferase family 1A member 3 Homo sapiens 32-38 9566748-7 1998 Relative levels of hepatic ST1A3 mRNA were non-normally distributed and correlated significantly with p-nitrophenol sulfation. 4-nitrophenol 102-115 sulfotransferase family 1A member 3 Homo sapiens 27-32 9566748-11 1998 These results suggest that regulation of p-nitrophenol sulfation occurs at the level of gene transcription of ST1A3 which is the major transcript of the three PSULT mRNAs and that a polygenic basis for the apparent genetic polymorphism of sulfation was likely because of the existence of ST1A3 variants. 4-nitrophenol 41-54 sulfotransferase family 1A member 3 Homo sapiens 110-115 21781833-3 1997 Here, we report that another enzyme involved in the metabolism of food-borne carcinogens, sulfotransferase (ST1A3 measured by 2-naphthol activity), may function as a potential protective factor for colon cancer in humans. 2-naphthol 126-136 sulfotransferase family 1A member 3 Homo sapiens 108-113 9566748-11 1998 These results suggest that regulation of p-nitrophenol sulfation occurs at the level of gene transcription of ST1A3 which is the major transcript of the three PSULT mRNAs and that a polygenic basis for the apparent genetic polymorphism of sulfation was likely because of the existence of ST1A3 variants. 4-nitrophenol 41-54 sulfotransferase family 1A member 3 Homo sapiens 288-293 9443824-6 1997 ST1B1 and ST1B2 showed higher affinities for formation of T3 sulfate (apparent Km 40.2 and 63.5 microM, respectively) than did thermostable phenol sulfotransferase ST1A3 (apparent Km 413 microM) or thermolabile phenol sulfotransferase ST1A5 (apparent Km 180 microM). t3 sulfate 58-68 sulfotransferase family 1A member 3 Homo sapiens 164-169 9443824-6 1997 ST1B1 and ST1B2 showed higher affinities for formation of T3 sulfate (apparent Km 40.2 and 63.5 microM, respectively) than did thermostable phenol sulfotransferase ST1A3 (apparent Km 413 microM) or thermolabile phenol sulfotransferase ST1A5 (apparent Km 180 microM). t3 sulfate 58-68 sulfotransferase family 1A member 3 Homo sapiens 235-240 9119390-1 1997 Phenol- and monoamine-metabolizing sulfotransferases (STP and STM, respectively) are members of a superfamily of enzymes that add sulfate to a variety of xenobiotics and endobiotics containing hydroxyl or amino functional groups. Phenol 0-6 sulfotransferase family 1A member 3 Homo sapiens 62-65 9119390-1 1997 Phenol- and monoamine-metabolizing sulfotransferases (STP and STM, respectively) are members of a superfamily of enzymes that add sulfate to a variety of xenobiotics and endobiotics containing hydroxyl or amino functional groups. monoamine 12-21 sulfotransferase family 1A member 3 Homo sapiens 62-65 9119390-1 1997 Phenol- and monoamine-metabolizing sulfotransferases (STP and STM, respectively) are members of a superfamily of enzymes that add sulfate to a variety of xenobiotics and endobiotics containing hydroxyl or amino functional groups. Sulfates 130-137 sulfotransferase family 1A member 3 Homo sapiens 62-65 9119390-1 1997 Phenol- and monoamine-metabolizing sulfotransferases (STP and STM, respectively) are members of a superfamily of enzymes that add sulfate to a variety of xenobiotics and endobiotics containing hydroxyl or amino functional groups. Hydroxyl Radical 193-201 sulfotransferase family 1A member 3 Homo sapiens 62-65 9983127-0 1996 Initial stages of metal encapsulation during epitaxial growth studied by STM: Rh/Ag(100). Metals 18-23 sulfotransferase family 1A member 3 Homo sapiens 73-76 9985920-0 1996 Bias-dependent imaging of the In-terminated InAs(001) (4 x 2)/c(8 x 2) surface by STM: Reconstruction and transitional defect. indium arsenide 44-48 sulfotransferase family 1A member 3 Homo sapiens 82-85 8912648-2 1996 We have previously cloned and sequenced the STM gene encoding the monoamine neurotransmitter-preferring sulfotransferase, M-PST, and a portion of the STP1 gene encoding the phenol-preferring isozyme, P-PST1 (BBRC 205, 1325-1332; Genomics 18, 440-443). monoamine 66-75 sulfotransferase family 1A member 3 Homo sapiens 44-47 9984053-0 1996 Shape of molecular adsorbates in STM images: A theoretical study of benzene on Pt(111). Benzene 68-75 sulfotransferase family 1A member 3 Homo sapiens 33-36 8697101-6 1996 The coding domains of HAST4 and HAST4v were 97 and 94% homologous to previously reported phenol (HAST1) and monoamine (HAST3) sulfonating forms of sulfotransferase, respectively. monoamine 108-117 sulfotransferase family 1A member 3 Homo sapiens 119-124 8859892-0 1996 Instrumental effects on in situ electrochemical STM studies: an investigation of a current surge induced Pd deposit on HOPG. Palladium 105-107 sulfotransferase family 1A member 3 Homo sapiens 48-51 9982590-0 1996 In situ sequential STM imaging of structural changes resulting from the electrodissolution of silver crystal surfaces in aqueous perchloric acid: The roughening kinetics. Perchloric Acid 129-144 sulfotransferase family 1A member 3 Homo sapiens 19-22 9983691-0 1996 Observation of charge enhancement induced by graphite atomic vacancy: A comparative STM and AFM study. Graphite 45-53 sulfotransferase family 1A member 3 Homo sapiens 84-87 9980770-0 1995 Mechanisms of initial alloy formation for Pd on Cu(100) studied by STM. Palladium 42-44 sulfotransferase family 1A member 3 Homo sapiens 67-70 9980770-0 1995 Mechanisms of initial alloy formation for Pd on Cu(100) studied by STM. Copper 48-50 sulfotransferase family 1A member 3 Homo sapiens 67-70 9979822-0 1995 Theory on STM images of Si(001) surface near defects. Silicon 24-26 sulfotransferase family 1A member 3 Homo sapiens 10-13 15048490-5 1995 By means of STM and XPS measurements it was possible to assign these two desorption peaks to the desorption of copper from carbon deposits, which had already been present before the contamination process, and to the desorption of copper from the bare Si surface. Copper 111-117 sulfotransferase family 1A member 3 Homo sapiens 12-15 9981774-0 1995 Phosphine adsorption and decomposition on Si(100) 2 x 1 studied by STM. phosphine 0-9 sulfotransferase family 1A member 3 Homo sapiens 67-70 9981774-0 1995 Phosphine adsorption and decomposition on Si(100) 2 x 1 studied by STM. Silicon 42-44 sulfotransferase family 1A member 3 Homo sapiens 67-70 7733310-6 1995 For PAH, the difference between ModCIM and StM clearance was related to the average PAH clearance by ModCIM and StM (r = 0.78). p-Aminohippuric Acid 4-7 sulfotransferase family 1A member 3 Homo sapiens 112-115 7752059-3 1995 Dopamine, p-nitrophenol and minoxidil were used as substrates for skin and platelet thermolabile (TL PST), thermostable (TS PST) and MNX-ST activities, respectively. Dopamine 0-8 sulfotransferase family 1A member 3 Homo sapiens 98-104 7752059-3 1995 Dopamine, p-nitrophenol and minoxidil were used as substrates for skin and platelet thermolabile (TL PST), thermostable (TS PST) and MNX-ST activities, respectively. 4-nitrophenol 10-23 sulfotransferase family 1A member 3 Homo sapiens 98-104 7752059-3 1995 Dopamine, p-nitrophenol and minoxidil were used as substrates for skin and platelet thermolabile (TL PST), thermostable (TS PST) and MNX-ST activities, respectively. Minoxidil 28-37 sulfotransferase family 1A member 3 Homo sapiens 98-104 7752059-9 1995 Platelet TL PST assayed with minoxidil showed thermal stability and a response to DCNP that were essentially the same as TL PST. Minoxidil 29-38 sulfotransferase family 1A member 3 Homo sapiens 9-15 7752059-9 1995 Platelet TL PST assayed with minoxidil showed thermal stability and a response to DCNP that were essentially the same as TL PST. 2,6-dichloro-4-nitrophenol 82-86 sulfotransferase family 1A member 3 Homo sapiens 9-15 7733310-6 1995 For PAH, the difference between ModCIM and StM clearance was related to the average PAH clearance by ModCIM and StM (r = 0.78). p-Aminohippuric Acid 4-7 sulfotransferase family 1A member 3 Homo sapiens 43-46 7668357-5 1995 YAC and cosmid cloning results have further substantiated the close proximity of STP and a highly related sulfotransferase (STM), encoding the catecholamine-preferring enzyme, to the CLN3 region of chromosome 16p. Catecholamines 143-156 sulfotransferase family 1A member 3 Homo sapiens 124-127 7733310-6 1995 For PAH, the difference between ModCIM and StM clearance was related to the average PAH clearance by ModCIM and StM (r = 0.78). p-Aminohippuric Acid 84-87 sulfotransferase family 1A member 3 Homo sapiens 43-46 7733310-6 1995 For PAH, the difference between ModCIM and StM clearance was related to the average PAH clearance by ModCIM and StM (r = 0.78). p-Aminohippuric Acid 84-87 sulfotransferase family 1A member 3 Homo sapiens 112-115 9974725-0 1994 STM study of surface reconstructions of Si(111):B. Silicon 40-42 sulfotransferase family 1A member 3 Homo sapiens 0-3 7999068-4 1994 Sequencing of these STP-like sequences confirmed that STP is contained within contig 343.1 and maps proximal to FRA16E, and that a related sulphotransferase STM, encoding the catecholamine-sulphating enzyme, is contained within contig 55.4 and maps to the adjacent hybrid interval CY12-CY180A. Catecholamines 175-188 sulfotransferase family 1A member 3 Homo sapiens 157-160 7695637-11 1995 5"-Flanking region(s) of STM contained neither canonical TATA nor CCAAT elements, but they did contain pyrimidine-rich stretches. pyrimidine 103-113 sulfotransferase family 1A member 3 Homo sapiens 25-28 9978925-0 1995 STM study of superstructures formed in the Pd/Si(111) system. Palladium 43-45 sulfotransferase family 1A member 3 Homo sapiens 0-3 9978925-0 1995 STM study of superstructures formed in the Pd/Si(111) system. Silicon 46-48 sulfotransferase family 1A member 3 Homo sapiens 0-3 7724028-7 1995 In the patient group with GFR-StM < 30 ml/min, the 125I-iothalamate plasma concentration increased progressively over time. 125i-iothalamate 54-70 sulfotransferase family 1A member 3 Homo sapiens 30-33 7724028-10 1995 In the two patient groups with GFR-StM > 60 ml/min, the 125I-iothalamate plasma concentration decreased progressively over time. 125i-iothalamate 59-75 sulfotransferase family 1A member 3 Homo sapiens 35-38 7852185-6 1994 Human ST1A2 and ST1A3 mediated the activation of N-OH-PhIP at 5.2- and 6.2-fold higher rates than did rat ST1C1, a main N-hydroxy-2-acetylaminofluorene-activating sulfotransferase, in rat liver. 2-hydroxyamino-1-methyl-6-phenylimidazo(4,5-b)pyridine 49-58 sulfotransferase family 1A member 3 Homo sapiens 16-21 10011515-0 1994 STM study of oxygen on Rh(110). Oxygen 13-19 sulfotransferase family 1A member 3 Homo sapiens 0-3 17830080-0 1994 Observation of Quantum-Size Effects at Room Temperature on Metal Surfaces With STM. Metals 59-64 sulfotransferase family 1A member 3 Homo sapiens 79-82 8093002-11 1994 HAST1 and HAST3 cDNAs were functionally expressed in COS-7 cells and kinetically characterized using the model substrates for P-PST and M-PST, p-nitrophenol and dopamine (3,4-dihydroxyphenethylamine) respectively. carbonyl sulfide 53-56 sulfotransferase family 1A member 3 Homo sapiens 10-15 8093002-11 1994 HAST1 and HAST3 cDNAs were functionally expressed in COS-7 cells and kinetically characterized using the model substrates for P-PST and M-PST, p-nitrophenol and dopamine (3,4-dihydroxyphenethylamine) respectively. 4-nitrophenol 143-156 sulfotransferase family 1A member 3 Homo sapiens 10-15 8093002-11 1994 HAST1 and HAST3 cDNAs were functionally expressed in COS-7 cells and kinetically characterized using the model substrates for P-PST and M-PST, p-nitrophenol and dopamine (3,4-dihydroxyphenethylamine) respectively. Dopamine 161-169 sulfotransferase family 1A member 3 Homo sapiens 10-15 8093002-11 1994 HAST1 and HAST3 cDNAs were functionally expressed in COS-7 cells and kinetically characterized using the model substrates for P-PST and M-PST, p-nitrophenol and dopamine (3,4-dihydroxyphenethylamine) respectively. Dopamine 171-198 sulfotransferase family 1A member 3 Homo sapiens 10-15 8093002-12 1994 COS-expressed HAST1 was shown to be enzymatically active in sulphating p-nitrophenol with high affinity (Km 0.6 microM), whereas dopamine was the preferred substrate for HAST3 (Km 9.7 microM). carbonyl sulfide 0-3 sulfotransferase family 1A member 3 Homo sapiens 170-175 8093002-12 1994 COS-expressed HAST1 was shown to be enzymatically active in sulphating p-nitrophenol with high affinity (Km 0.6 microM), whereas dopamine was the preferred substrate for HAST3 (Km 9.7 microM). Dopamine 129-137 sulfotransferase family 1A member 3 Homo sapiens 170-175 8093002-14 1994 COS-expressed HAST1 and HAST3 displayed inhibition profiles with the ST inhibitor 2,6-dichloro-4-nitrophenol (DCNP), identical with human liver cytosolic P-PST and M-PST activities respectively. 2,6-dichloro-4-nitrophenol 82-108 sulfotransferase family 1A member 3 Homo sapiens 24-29 8093002-14 1994 COS-expressed HAST1 and HAST3 displayed inhibition profiles with the ST inhibitor 2,6-dichloro-4-nitrophenol (DCNP), identical with human liver cytosolic P-PST and M-PST activities respectively. 2,6-dichloro-4-nitrophenol 110-114 sulfotransferase family 1A member 3 Homo sapiens 24-29 10009524-0 1994 STM study on the interactions of C70 with the Si(100)2 x 1 surface. Silicon 46-48 sulfotransferase family 1A member 3 Homo sapiens 0-3 10008422-0 1993 Topographic and spectroscopic analysis of ethylene adsorption on Si(111)7 x 7 by STM and STS. ethylene 42-50 sulfotransferase family 1A member 3 Homo sapiens 81-84 10008422-0 1993 Topographic and spectroscopic analysis of ethylene adsorption on Si(111)7 x 7 by STM and STS. Silicon 65-67 sulfotransferase family 1A member 3 Homo sapiens 81-84 10007620-0 1993 AFM and STM studies of the carbonization and graphitization of polyimide films. polyimide 63-72 sulfotransferase family 1A member 3 Homo sapiens 8-11 8325266-8 1993 Some excellent results which might indicate clinically unknown effects of toluene such as hearing loss, impairments of time discrimination, and improvements of STM were also demonstrated. Toluene 74-81 sulfotransferase family 1A member 3 Homo sapiens 160-163 10009100-0 1993 Variable-temperature STM measurements of step kinetics on Si(001). Silicon 58-60 sulfotransferase family 1A member 3 Homo sapiens 21-24 8223170-6 1993 In conclusion, the method of STM of SAECG using terminal 40 microV/25-250Hz as window onsets offered promise for identification of patients with VTs/VF, and had better clinical applicability than time domain analysis for patients with IVB may not be excluded during STM. saecg 36-41 sulfotransferase family 1A member 3 Homo sapiens 29-32 8223170-6 1993 In conclusion, the method of STM of SAECG using terminal 40 microV/25-250Hz as window onsets offered promise for identification of patients with VTs/VF, and had better clinical applicability than time domain analysis for patients with IVB may not be excluded during STM. saecg 36-41 sulfotransferase family 1A member 3 Homo sapiens 266-269 8109388-7 1993 There are significant potential advantages for imaging biological specimen with the STM as the imaging is done in air and the specimen can be imaged without a metal coating. Metals 159-164 sulfotransferase family 1A member 3 Homo sapiens 84-87 1687013-7 1991 For example, average temperatures that produced 50% inactivation of TL PST, TS PST, and AANST activities, measured with both 0.05 and 1.0 mM 2-NA as substrate, were 35.0, 40.5, 40.3 and 40.5 degrees C, respectively. 2-Naphthylamine 141-145 sulfotransferase family 1A member 3 Homo sapiens 68-74 17801230-0 1992 Extraction and STM Imaging of Spherical Giant Fullerenes. Fullerenes 46-56 sulfotransferase family 1A member 3 Homo sapiens 15-18 17801230-3 1992 The STM images show that the giant fullerenes in these samples are roughly spherical in shape and range in diameter from approximately 1 to 2 nanometers, corresponding to fullerenes containing 60 to 330 atoms. Fullerenes 35-45 sulfotransferase family 1A member 3 Homo sapiens 4-7 1413243-1 1992 We show that domain walls on graphite are very likely to mimic features of extended macromolecules like DNA strands, when imaged with an STM. Graphite 29-37 sulfotransferase family 1A member 3 Homo sapiens 137-140 1687013-8 1991 IC50 values for the inhibition by DCNP of TL PST, TS PST, and AANST, measured with 0.05 and 1.0 mM 2-NA as substrate, were 110, 1.8, 1.3, and 4.0 microM, respectively. 2,6-dichloro-4-nitrophenol 34-38 sulfotransferase family 1A member 3 Homo sapiens 42-48 1687013-8 1991 IC50 values for the inhibition by DCNP of TL PST, TS PST, and AANST, measured with 0.05 and 1.0 mM 2-NA as substrate, were 110, 1.8, 1.3, and 4.0 microM, respectively. 2-Naphthylamine 99-103 sulfotransferase family 1A member 3 Homo sapiens 42-48 34283574-5 2021 The stabilization of the pseudopolymorph was then achieved by using an alternative nanoconfinement strategy, where the domains of the pseudopolymorph could be formed and stabilized by restricting the self-assembly in nanometer-sized shallow compartments produced by STM-based nanolithography carried out on a graphite surface with a high density of covalently bound aryl groups. Graphite 309-317 sulfotransferase family 1A member 3 Homo sapiens 266-269 2288035-4 1990 The effect of the peptide on the polymer condensation is clearly illustrated on the large-scale STM images which reveal a well defined spacing between parallel DNA helices. Polymers 33-40 sulfotransferase family 1A member 3 Homo sapiens 96-99 34596642-6 2021 Importantly, our STM imaging results showed very organized tilted layered structures for meso-AgL2 on highly oriented pyrolytic graphite (HOPG) that are quite similar to its crystalline ones, paving the way for future single molecule manipulations. Graphite 128-136 sulfotransferase family 1A member 3 Homo sapiens 17-20 34505134-3 2021 Following a 21-d adaptation period, total fecal output was collected for 5 d. Dry matter (P < 0.07) and CP (P < 0.06) digestibility tended to be reduced, and NDF (P < 0.04) and acid detergent fiber (ADF) (P < 0.05) digestibility were reduced in STM- vs. HTM-supplemented steers. N-(CARBOXYCARBONYL)-D-PHENYLALANINE 158-161 sulfotransferase family 1A member 3 Homo sapiens 245-248 34505134-13 2021 Results indicate that Cu and Zn from HTM have low solubility in the rumen and appear to be less tightly bound to ruminal solid digesta than Cu and Zn from STM. Zinc 147-149 sulfotransferase family 1A member 3 Homo sapiens 155-158 33587592-0 2021 z-Piezo Pulse-Modulated STM Break Junction: Toward Single-Molecule Rectifiers with Dissimilar Metal Electrodes. Metals 94-99 sulfotransferase family 1A member 3 Homo sapiens 24-27 33587592-2 2021 Herein, we develop a z-piezo pulse-modulated scanning tunneling microscopy break junction (STM-BJ) technique to construct a robust asymmetric junction with different metal electrodes. Metals 166-171 sulfotransferase family 1A member 3 Homo sapiens 91-94 34740292-9 2021 In silico docking simulation was utilized to analyze the inhibition capability of 2"-OH-PCB5, 4"-OH-PCB9, 2"-OH-PCB12 towards SULT1A3.All these results obtained in this study are helpful for further understanding the toxicity of PCBs. 2"-oh-pcb5 82-92 sulfotransferase family 1A member 3 Homo sapiens 126-133 34740292-9 2021 In silico docking simulation was utilized to analyze the inhibition capability of 2"-OH-PCB5, 4"-OH-PCB9, 2"-OH-PCB12 towards SULT1A3.All these results obtained in this study are helpful for further understanding the toxicity of PCBs. 4"-oh-pcb9 94-104 sulfotransferase family 1A member 3 Homo sapiens 126-133 34740292-9 2021 In silico docking simulation was utilized to analyze the inhibition capability of 2"-OH-PCB5, 4"-OH-PCB9, 2"-OH-PCB12 towards SULT1A3.All these results obtained in this study are helpful for further understanding the toxicity of PCBs. 2"-oh-pcb12 106-117 sulfotransferase family 1A member 3 Homo sapiens 126-133 34740292-9 2021 In silico docking simulation was utilized to analyze the inhibition capability of 2"-OH-PCB5, 4"-OH-PCB9, 2"-OH-PCB12 towards SULT1A3.All these results obtained in this study are helpful for further understanding the toxicity of PCBs. Polychlorinated Biphenyls 229-233 sulfotransferase family 1A member 3 Homo sapiens 126-133 34766176-2 2021 Sequential "knock-on" of F-atom products was observed by STM to propagate along the 1D fluorocarbon line. Fluorocarbons 87-99 sulfotransferase family 1A member 3 Homo sapiens 57-60 34757758-1 2021 The dissociation of a single water molecule on a ZnO(1010) surface has been investigated at the atomic level by low temperature STM manipulation combined with DFT calculations. Water 29-34 sulfotransferase family 1A member 3 Homo sapiens 128-131 34757758-1 2021 The dissociation of a single water molecule on a ZnO(1010) surface has been investigated at the atomic level by low temperature STM manipulation combined with DFT calculations. Zinc Oxide 49-52 sulfotransferase family 1A member 3 Homo sapiens 128-131 35343988-0 2022 Nanoscale electrochemical 3D deposition of cobalt with nanosecond voltage pulses in an STM. Cobalt 43-49 sulfotransferase family 1A member 3 Homo sapiens 87-90 34985273-3 2022 STM results show that benzoic acid adsorption displaces a large fraction of Au clusters from the terraces toward their edges. Gold 76-78 sulfotransferase family 1A member 3 Homo sapiens 0-3 35315463-1 2022 We report on the properties of the thin films of the short peptide L-dialanine grown on Cu(100) surfaces and compare them to those of L-alanine by using surface techniques like XPS, IRRAS and STM. l-dialanine 67-78 sulfotransferase family 1A member 3 Homo sapiens 192-195 34985273-2 2022 STM and DFT+U are used to study this phenomenon by monitoring the photoreaction of a prototype hole-scavenger molecule, benzoic acid, over stoichiometric (s) s-TiO2, Au9/s-TiO2, and reduced (r) Au9/r-TiO2. Benzoic Acid 120-132 sulfotransferase family 1A member 3 Homo sapiens 0-3 34985273-3 2022 STM results show that benzoic acid adsorption displaces a large fraction of Au clusters from the terraces toward their edges. Benzoic Acid 22-34 sulfotransferase family 1A member 3 Homo sapiens 0-3 35281274-3 2022 In the initial application of the procedure, yeast cells expressing human SULT1A3 were used for the production of 4"-hydroxypropranolol-4-O-sulfate from 4-hydroxypropranolol. 4"-hydroxypropranolol-4-o-sulfate 114-147 sulfotransferase family 1A member 3 Homo sapiens 74-81 35281274-3 2022 In the initial application of the procedure, yeast cells expressing human SULT1A3 were used for the production of 4"-hydroxypropranolol-4-O-sulfate from 4-hydroxypropranolol. 4-hydroxypropranolol 153-173 sulfotransferase family 1A member 3 Homo sapiens 74-81 35069453-2 2021 The study aimed to investigate the potential inhibitory capability of BPs on four human sulfotransferase isoforms (SULT1A1, SULT1A3, SULT1B1 and SULT1E1) and interpret how to interfere with endocrine hormone metabolism. bps 70-73 sulfotransferase family 1A member 3 Homo sapiens 124-131