PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 24734613-2 2014 Under the excitation of UV light, Na5La(MoO4)4:Tm3+, Na5La(MoO4)4:Tb3+, and Na5La(MoO4)4:Eu3+ exhibit the characteristic emissions of Tm3+ (1D2 --> 3F4, blue), Tb3+ (5D4 --> 7F5, green), and Eu3+ (5D0 --> 7F2, red), respectively. tb3+ 66-70 tropomyosin 3 Homo sapiens 134-137 28063445-6 2017 The optimal concentrations of Dy3+ (1.5 mM) and Tb3+ (0.25 mM) for C13 DNP were found to be less than that of Gd3+ (2 mM). tb3+ 48-52 homeobox C13 Homo sapiens 67-70 28063445-8 2017 Furthermore, when dissolution was employed, Tb3+-doped samples were found to have similar liquid-state C13 NMR signal enhancements compared to samples doped with Gd3+, and both Tb3+ and Dy3+ had a negligible liquid-state nuclear T1 shortening effect which contrasts with the significant reduction in T1 when using Gd3+. tb3+ 44-48 homeobox C13 Homo sapiens 103-106 28063445-9 2017 Our results show that Dy3+ doping and Tb3+ doping have a beneficial impact on C13 DNP both in the solid and liquid states, and that Tb3+ in particular could be used as a potential alternative to Gd3+ in C13 dissolution DNP experiments. tb3+ 38-42 homeobox C13 Homo sapiens 78-81 28063445-9 2017 Our results show that Dy3+ doping and Tb3+ doping have a beneficial impact on C13 DNP both in the solid and liquid states, and that Tb3+ in particular could be used as a potential alternative to Gd3+ in C13 dissolution DNP experiments. tb3+ 132-136 homeobox C13 Homo sapiens 203-206 27934036-5 2016 Using a uniformly 15N-labeled mutant of calbindin D9k loaded with either Tm3+ or Tb3+, reduced R1 and R2 relaxation rates of backbone 15N spins were observed compared with the diamagnetic reference (the same protein loaded with Y3+). tb3+ 81-85 S100 calcium binding protein G Homo sapiens 40-53 27829633-4 2016 Employing such interesting phenomenon, a label-free and time-resolved luminescent strategy for the sensitive detection of EndoV activity was developed based on DNA-enhanced time-resolved luminescence (TRL) of Tb3+. tb3+ 209-213 endonuclease V Homo sapiens 122-127 28451295-2 2017 This sensor is composed of the tandem ZF RNA binding domain of TIS11d functionalized with a luminescent Tb3+ complex on one of the ZFs and a sensitizing antenna on the other. tb3+ 104-108 ZFP36 ring finger protein like 2 Homo sapiens 63-69 27752975-8 2016 In addition, Ce3+/Tb3+-co-doped CaF2 nanocrystals show efficient energy transfer from Ce3+ to Tb3+ ion and strong green luminescence of Tb3+ ion at 541 nm(5D4 7F5). tb3+ 18-22 CCR4-NOT transcription complex subunit 8 Homo sapiens 32-36 27752975-8 2016 In addition, Ce3+/Tb3+-co-doped CaF2 nanocrystals show efficient energy transfer from Ce3+ to Tb3+ ion and strong green luminescence of Tb3+ ion at 541 nm(5D4 7F5). tb3+ 94-98 CCR4-NOT transcription complex subunit 8 Homo sapiens 32-36 27752975-8 2016 In addition, Ce3+/Tb3+-co-doped CaF2 nanocrystals show efficient energy transfer from Ce3+ to Tb3+ ion and strong green luminescence of Tb3+ ion at 541 nm(5D4 7F5). tb3+ 94-98 CCR4-NOT transcription complex subunit 8 Homo sapiens 32-36 20101952-1 2009 LiM (M = Ca, Sr, Ba) BO3 : Tb3+ phosphors were synthesized by solid state reaction. tb3+ 27-31 PDZ and LIM domain 5 Homo sapiens 0-3 25007616-5 2014 The analytical results show that the energy level of 2-FBA matches the lowest excited state energy level of Tb3+ (5D4) better than that of phen. tb3+ 108-112 F-box protein 3 Homo sapiens 55-58 25007616-7 2014 The energy level of triplet state of the first ligand 2-FBA corresponding to the absorption peak 273 nm has poor matching degree with the 5D4 energy level of Tb3+. tb3+ 158-162 F-box protein 3 Homo sapiens 56-59 25007616-9 2014 It illustrates that the energy level of the triplet state of the first ligand 2-FBA corresponding to 252 nm has much better matching degree with the lowest excited state of 5D4 energy level of Tb3+ than that of phen. tb3+ 193-197 F-box protein 3 Homo sapiens 80-83 20101952-7 2009 Effects of activation and charge compensation on the luminescence intensities of LiM (M = Ca, Sr, Ba) BO3 : Tb3+ phosphors were studied, and the results show that the intensities were obviously effected. tb3+ 108-112 PDZ and LIM domain 5 Homo sapiens 81-84 18785925-3 2008 To dissect the relative contributions of key determinants for Ca2+-dependent conformational changes, we report the design of a single-site Ca2+-binding protein (CD2.trigger) created by altering charged residues at an electrostatically sensitive location on the surface of the host protein rat Cluster of Differentiation 2 (CD2).CD2.trigger binds to Tb3+ and Ca2+ with dissociation constants of 0.3 +/- 0.1 and 90 +/- 25 microM, respectively. tb3+ 349-353 Cd2 molecule Rattus norvegicus 161-164 19441364-2 2009 Biological transferrin and lactoferrin proteins formed stable Tb3+ complexes, which exhibited long-lived and green luminescence signals. tb3+ 62-66 transferrin Homo sapiens 11-22 19441364-5 2009 The immobilized biotinylated transferrin-Tb3+ complexes on the micrometer-scaled bead also operated as a pH-responsive luminescent indicator. tb3+ 41-45 transferrin Homo sapiens 29-40 19441364-6 2009 Since the transferrin ligand had rapid Tb3+ complexation/decomplexation process, its Tb3+ complex exhibited pH-responsive luminescence signals even in the presence of Fe3+ cation. tb3+ 39-43 transferrin Homo sapiens 10-21 19441364-6 2009 Since the transferrin ligand had rapid Tb3+ complexation/decomplexation process, its Tb3+ complex exhibited pH-responsive luminescence signals even in the presence of Fe3+ cation. tb3+ 85-89 transferrin Homo sapiens 10-21 18593119-3 2008 Upon interaction of the modified terbium-chelating peptides with the cyclin A substrate recruitment groove, the Tb3+ ion is placed in the vicinity of the Trp217 side chain, which results in efficient intermolecular terbium sensitization and specific long wavelength fluorescent emission from the metal center. tb3+ 112-116 cyclin A2 Homo sapiens 69-77 16765896-8 2006 By exploiting the capability of Tb3+ bound to CLSP to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. tb3+ 32-36 calmodulin like 5 Homo sapiens 46-50 17110158-3 2007 Especially, the UC luminescence was intensified violently with the energy transfer from the Tm3+ ions involves in the Tb3+ excitation. tb3+ 118-122 tropomyosin 3 Homo sapiens 92-95 16751247-2 2006 Changes in DEFET from variously charged Tb3+ -chelates revealed net potentials of -20 mV at the nAChR agonist sites and -14 mV at the entrance to the AChE active site, in physiological ionic strength conditions. tb3+ 40-44 cholinergic receptor nicotinic alpha 4 subunit Homo sapiens 96-101 16751247-2 2006 Changes in DEFET from variously charged Tb3+ -chelates revealed net potentials of -20 mV at the nAChR agonist sites and -14 mV at the entrance to the AChE active site, in physiological ionic strength conditions. tb3+ 40-44 acetylcholinesterase (Cartwright blood group) Homo sapiens 150-154 16751249-2 2006 Freely diffusing Tb3+ -chelates of varying charge constituted a set of energy transfer donors to the acceptor, crystal violet, a noncompetitive antagonist of the nAChR. tb3+ 17-21 cholinergic receptor nicotinic alpha 4 subunit Homo sapiens 162-167 16751249-3 2006 Energy transfer from a neutral Tb3+ -chelate to nAChR-bound crystal violet was reduced 95% relative to the energy transfer to free crystal violet. tb3+ 31-35 cholinergic receptor nicotinic alpha 4 subunit Homo sapiens 48-53 16637598-6 2006 Designed peptides, which contain minimal substrate recognition motifs of the protein kinases PKA, PKC, or the MAP kinase Erk, form complexes with Tb3+ when phosphorylated, showing strong Tb3+ luminescence emission at 544 nm, but show weak luminescence when not phosphorylated. tb3+ 146-150 mitogen-activated protein kinase 1 Homo sapiens 121-124 16637598-6 2006 Designed peptides, which contain minimal substrate recognition motifs of the protein kinases PKA, PKC, or the MAP kinase Erk, form complexes with Tb3+ when phosphorylated, showing strong Tb3+ luminescence emission at 544 nm, but show weak luminescence when not phosphorylated. tb3+ 187-191 mitogen-activated protein kinase 1 Homo sapiens 121-124 16148025-7 2005 The Tb3+ binding constants placed the TSP-1 region affected by N700S polymorphism among other high-affinity Ca2+ binding sites. tb3+ 4-8 thrombospondin 1 Homo sapiens 38-43 16466744-7 2006 Furthermore, bathing crystals with the trivalent calcium ion mimic, Tb3+, results in anomalous scattering data that permit unequivocal localization of terbium ions in each of the proposed type I and type II ion-binding sites of both halves of gelsolin. tb3+ 68-72 gelsolin Homo sapiens 243-251 16581924-5 2006 From the TL spectra and the excitation and emission spectra of photoluminescence for the CaF2 doped activators, it is concluded that the TL of Tb3+ ions is sensitised by the existence of Sm3+ ions. tb3+ 143-147 CCR4-NOT transcription complex subunit 8 Homo sapiens 89-93 16165030-2 2005 Using quinolones-terbium (Tb3+) complex as a fluorescent probe, in the buffer solution of pH 7.8, HSA can remarkably enhance the fluorescence intensity of the quinolones-Tb3+ complex at 545 nm and the enhanced fluorescence intensity of Tb3+ ion is in proportion to the concentration of HSA and quinolone drugs. tb3+ 26-30 albumin Homo sapiens 98-101 16165030-2 2005 Using quinolones-terbium (Tb3+) complex as a fluorescent probe, in the buffer solution of pH 7.8, HSA can remarkably enhance the fluorescence intensity of the quinolones-Tb3+ complex at 545 nm and the enhanced fluorescence intensity of Tb3+ ion is in proportion to the concentration of HSA and quinolone drugs. tb3+ 26-30 albumin Homo sapiens 286-289 16165030-2 2005 Using quinolones-terbium (Tb3+) complex as a fluorescent probe, in the buffer solution of pH 7.8, HSA can remarkably enhance the fluorescence intensity of the quinolones-Tb3+ complex at 545 nm and the enhanced fluorescence intensity of Tb3+ ion is in proportion to the concentration of HSA and quinolone drugs. tb3+ 170-174 albumin Homo sapiens 98-101 16165030-2 2005 Using quinolones-terbium (Tb3+) complex as a fluorescent probe, in the buffer solution of pH 7.8, HSA can remarkably enhance the fluorescence intensity of the quinolones-Tb3+ complex at 545 nm and the enhanced fluorescence intensity of Tb3+ ion is in proportion to the concentration of HSA and quinolone drugs. tb3+ 170-174 albumin Homo sapiens 286-289 16165030-2 2005 Using quinolones-terbium (Tb3+) complex as a fluorescent probe, in the buffer solution of pH 7.8, HSA can remarkably enhance the fluorescence intensity of the quinolones-Tb3+ complex at 545 nm and the enhanced fluorescence intensity of Tb3+ ion is in proportion to the concentration of HSA and quinolone drugs. tb3+ 170-174 albumin Homo sapiens 98-101 16165030-2 2005 Using quinolones-terbium (Tb3+) complex as a fluorescent probe, in the buffer solution of pH 7.8, HSA can remarkably enhance the fluorescence intensity of the quinolones-Tb3+ complex at 545 nm and the enhanced fluorescence intensity of Tb3+ ion is in proportion to the concentration of HSA and quinolone drugs. tb3+ 170-174 albumin Homo sapiens 286-289 15327280-2 2004 As an example, a calcium binding protein (human oncomodulin), in which one of the calcium ions was selectively substituted with Tb3+, is used. tb3+ 128-132 oncomodulin Homo sapiens 48-59 15998051-1 2005 By using Tb3+ as a luminescent probe, we demonstrate that the phosphorylation state of a 14-residue peptide fragment of alpha-synuclein, a protein implicated in Parkinson"s Disease, dramatically affects the metal ion affinity of the peptide. tb3+ 9-13 synuclein alpha Homo sapiens 120-135 15945660-8 2005 In Ce1-x-yZrxTbyO2 there is an unexpected high concentration of Tb3+, which is not seen in TbO2 or Ce1-xTbxO2 and enhances the chemical reactivity of the ternary oxide. tb3+ 64-68 carboxylesterase 1 Homo sapiens 3-6 10556528-1 1999 This work shows that the partial replacement of diamagnetic Ca2+ by paramagnetic Tb3+ in Ca2+/calmodulin systems in solution allows the measurement of interdomain NMR pseudocontact shifts and leads to magnetic alignment of the molecule such that significant residual dipolar couplings can be measured. tb3+ 81-85 calmodulin 1 Homo sapiens 94-104 11075673-8 2000 A decrease in the lifetime of the 5D4 level of Tb3+ with the increase of Pr3+ concentration confirms this. tb3+ 47-51 proteinase 3 Homo sapiens 73-76 10556528-3 1999 Species in which Tb3+ ions are bound to only one domain of calmodulin (the N-domain) and Ca2+ ions to the other (the C-domain) provide convenient systems for measuring these parameters. tb3+ 17-21 calmodulin 1 Homo sapiens 59-69 10556528-5 1999 In addition, the Tb3+ ions bound to the N-domain of calmodulin greatly enhance the magnetic susceptibility anisotropy of the molecule so that a certain degree of alignment is produced due to interaction with the external magnetic field. tb3+ 17-21 calmodulin 1 Homo sapiens 52-62 10052953-8 1999 Additional evidence for the presence of a Trp residue in the PON1 calcium-binding sites was a characteristic fluorescence emission at 545 nm from the PON1-Tb3+ complex and abolishment of that fluorescence upon modification by N-bromosuccinimide. tb3+ 155-159 paraoxonase 1 Homo sapiens 61-65 10052953-8 1999 Additional evidence for the presence of a Trp residue in the PON1 calcium-binding sites was a characteristic fluorescence emission at 545 nm from the PON1-Tb3+ complex and abolishment of that fluorescence upon modification by N-bromosuccinimide. tb3+ 155-159 paraoxonase 1 Homo sapiens 150-154 15818933-1 1999 A series of phosphors containing Ce3+, Tb3+ ions in CaF2 and AlF3 were synthesized in a solution reaction and solid reaction method. tb3+ 39-43 CCR4-NOT transcription complex subunit 8 Homo sapiens 52-56 9723881-2 1998 A quantitative analysis of the interaction of metal ions with bovine Tg was conducted by fluorimetric titration of the protein with Tb3+ ions. tb3+ 132-136 thyroglobulin Bos taurus 69-71 9922166-4 1998 In this work, measurements of Ca2+-induced changes in intrinsic tryptophan fluorescence, and fluorescence energy transfer from tryptophan to Tb3+, reveal a slow conformational change in rat liver MBP (MBP-C) accompanying the binding of either Ca2+ or Tb3+. tb3+ 141-145 mannose binding lectin 2 Rattus norvegicus 196-199 9922166-4 1998 In this work, measurements of Ca2+-induced changes in intrinsic tryptophan fluorescence, and fluorescence energy transfer from tryptophan to Tb3+, reveal a slow conformational change in rat liver MBP (MBP-C) accompanying the binding of either Ca2+ or Tb3+. tb3+ 141-145 mannose binding lectin 2 Rattus norvegicus 201-206 9922166-4 1998 In this work, measurements of Ca2+-induced changes in intrinsic tryptophan fluorescence, and fluorescence energy transfer from tryptophan to Tb3+, reveal a slow conformational change in rat liver MBP (MBP-C) accompanying the binding of either Ca2+ or Tb3+. tb3+ 251-255 mannose binding lectin 2 Rattus norvegicus 196-199 9922166-4 1998 In this work, measurements of Ca2+-induced changes in intrinsic tryptophan fluorescence, and fluorescence energy transfer from tryptophan to Tb3+, reveal a slow conformational change in rat liver MBP (MBP-C) accompanying the binding of either Ca2+ or Tb3+. tb3+ 251-255 mannose binding lectin 2 Rattus norvegicus 201-206 9922166-6 1998 Likewise, addition of EGTA to Ca2+-bound or Tb3+-bound MBP-C causes a decrease in intrinsic tryptophan fluorescence with biphasic kinetics consisting of a burst phase with a rate constant greater than 1 s(-1), followed by a slow phase with a single-exponential rate constant of 0.065 s(-1). tb3+ 44-48 mannose binding lectin 2 Rattus norvegicus 55-60 9922166-9 1998 These data strongly suggest that the binding of either Ca2+ or Tb3+ to MBP-C is coupled to a conformational change that involves the cis-trans isomerization of a peptide bond. tb3+ 63-67 mannose binding lectin 2 Rattus norvegicus 71-76 9824675-3 1998 A high-affinity Tb3+ binding site was identified in the plasma membrane of the C13* cells (n=105+/-2 fmol/cell and Kd=36. tb3+ 16-20 homeobox C13 Homo sapiens 79-82 9824675-8 1998 Formation of the Tb3+-C13*-cisplatin complex does not interfere with the high-affinity binding of Tb3+; cisplatin and Tb3+ bind within 5 to 10 A of each other. tb3+ 17-21 homeobox C13 Homo sapiens 22-25 9723881-4 1998 The fluorescence emission spectrum of Tg excited at 280 nm showed, upon addition of Tb3+ ions, a peak at 546 nm and a marked decrease at 335 nm, indicating an efficient Forster energy transfer between bound Tb3+ ions and closely located Tg intrinsic chromophores. tb3+ 84-88 thyroglobulin Bos taurus 38-40 9723881-4 1998 The fluorescence emission spectrum of Tg excited at 280 nm showed, upon addition of Tb3+ ions, a peak at 546 nm and a marked decrease at 335 nm, indicating an efficient Forster energy transfer between bound Tb3+ ions and closely located Tg intrinsic chromophores. tb3+ 84-88 thyroglobulin Bos taurus 237-239 9723881-4 1998 The fluorescence emission spectrum of Tg excited at 280 nm showed, upon addition of Tb3+ ions, a peak at 546 nm and a marked decrease at 335 nm, indicating an efficient Forster energy transfer between bound Tb3+ ions and closely located Tg intrinsic chromophores. tb3+ 207-211 thyroglobulin Bos taurus 38-40 9723881-5 1998 Titration of Tg with Tb3+ ions, carried out by monitoring the emitted fluorescence at 546 nm, indicated the presence of 13.15 metal binding sites per Tg molecule. tb3+ 21-25 thyroglobulin Bos taurus 13-15 9723881-5 1998 Titration of Tg with Tb3+ ions, carried out by monitoring the emitted fluorescence at 546 nm, indicated the presence of 13.15 metal binding sites per Tg molecule. tb3+ 21-25 thyroglobulin Bos taurus 150-152 9396720-4 1997 The valency of the multivalent cation was not as important, since tervalent lanthanides (Eu3+, Gd3+ and Tb3+) of ionic radius 106-109 pm induced similar levels (50-60%) of helix to those induced by Ca2+ and Cd2+ (ionic radii 109 and 114 pm respectively). tb3+ 104-108 CD2 molecule Homo sapiens 207-210 9242617-2 1997 2"-Deoxy-3"-anthraniloyl adenosine-5-triphosphate (ANT-dATP) coordinated to Tb3+ was used as an environmentally sensitive probe of the nucleotide-binding site of GroEL. tb3+ 76-80 heat shock protein family D (Hsp60) member 1 Homo sapiens 162-167 9398229-3 1997 To gain information about the topography of the CaM-CaD complex, we have carried out fluorescence titrations of CaM with Tb3+ as a substitute for Ca2+ in the presence of wild-type or mutated CaD variants. tb3+ 121-125 calmodulin 2 Gallus gallus 112-115 7772032-7 1995 Spermine displaced Tb3+ and Ruthenium Red from the ATPase, consistent with binding in the stalk region of the ATPase. tb3+ 19-23 dynein axonemal heavy chain 8 Homo sapiens 51-57 8849029-10 1995 ALP hydrolyzes the phosphate ester of fluorosalicylic acid, and the fluorosalicylate produced forms highly fluorescent ternary complexes with Tb(3+)-EDTA, which can be quantified by measuring the Tb3+ fluorescence in a time-resolved mode. tb3+ 196-200 alkaline phosphatase, placental Homo sapiens 0-3 7649174-3 1995 When coordinated to the lanthanide ion Tb3+, Ant-dATP is not hydrolyzed by Hsc70. tb3+ 39-43 solute carrier family 25 member 6 Homo sapiens 45-48 7649174-6 1995 Sensitized luminescence arising from resonance energy transfer from the anthraniloyl group to Tb3+ is substantially enhanced in the presence of Hsc70. tb3+ 94-98 heat shock protein family A (Hsp70) member 8 Homo sapiens 144-149 9242617-3 1997 Tb3+.ANT-dATP recognizes the nucleotide-binding site of GroEL and inhibits ATPase activity. tb3+ 0-4 heat shock protein family D (Hsp60) member 1 Homo sapiens 56-61 9242617-4 1997 Sensitized luminescence, arising from resonance energy transfer from the anthraniloyl moiety to Tb3+, is substantially enhanced in the presence of GroEL. tb3+ 96-100 heat shock protein family D (Hsp60) member 1 Homo sapiens 147-152 9242617-5 1997 Binding of denatured mitochondrial malate dehydrogenase to the apical domain of GroEL causes a red shift in the fluorescence emitted by anthraniloyl and further enhancement in the phosphorescence emitted by Tb3+ upon excitation at 320 nm. tb3+ 207-211 heat shock protein family D (Hsp60) member 1 Homo sapiens 80-85 7522557-2 1994 Tb3+ supported fibrinogen binding to purified GPIIb-IIIa, at lower concentrations than Ca2+, consistent with its higher affinity for cation-binding motifs. tb3+ 0-4 integrin subunit alpha 2b Homo sapiens 46-51 7522557-9 1994 Of the two candidate GPIIIa sequences, 118-131 and 208-221, the former bound Tb3+ and divalent cations with an affinity similar to that of the GPIIb peptides, whereas the latter peptide was not functional. tb3+ 77-81 integrin subunit beta 3 Homo sapiens 21-27 7929166-2 1994 Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum. tb3+ 68-72 ryanodine receptor 1 Homo sapiens 110-128 7929166-2 1994 Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum. tb3+ 68-72 ryanodine receptor 1 Homo sapiens 130-133 7929166-8 1994 About 20% of the bound Tb3+ was not displaced by EGTA or Ca2+; suggesting its "occlusion" in the RyR. tb3+ 23-27 ryanodine receptor 1 Homo sapiens 97-100 7929166-12 1994 The results suggest that RyR/Ca2+ release channel undergoes conformational changes due to Tb3+ binding to the low-affinity Ca2+ binding site, and this binding results in the closing of the Ca2+ release channel. tb3+ 90-94 ryanodine receptor 1 Homo sapiens 25-28 2026250-2 1991 Luminescence of Tb3+ ions bound to a calmodulin fragment has been studied. tb3+ 16-20 calmodulin 1 Rattus norvegicus 37-47 7945790-10 1994 Fluorescence energy transfer measurements between Tb3+ in the strong calcium site to Co2+ in the strong Zn2+ site gave a distance in the range of 14-18 A, which was in excellent agreement with recent crystallographic data for human alpha-lactalbumin [Ren et al. tb3+ 50-54 lactalbumin alpha Homo sapiens 232-249 1643036-3 1992 The dissociation constants for Eu3+ (1.0 +/- 0.2 microM) and Tb3+ (5 +/- 1 microM) from the weak lanthanide binding sites (III and IV, numbered from the amino terminus) of octopus calmodulin were measured using luminescence techniques. tb3+ 61-65 calmodulin Bos taurus 180-190 1643036-7 1992 Forster theory parameters for nonradiative energy transfer between Tyr138 and Tb3+ ions bound at sites III and IV of octopus calmodulin were comprehensively evaluated, including a dynamics simulation of the orientation factor kappa 2. tb3+ 78-82 calmodulin Bos taurus 125-135 1618836-3 1992 The effect of changing the molecular environment around Tb3+ on its luminescence was studied using native Cod III parvalbumin and site-directed mutants of both oncomodulin and calmodulin. tb3+ 56-60 oncomodulin Homo sapiens 160-171 1618836-8 1992 An alternate binding loop, based on Tb3+ binding to model peptides, was inserted into the CD loop of oncomodulin by cassette mutagenesis. tb3+ 36-40 oncomodulin Homo sapiens 101-112 1534084-4 1992 Simultaneously, we directly measured the amount of Tb3+ bound to the ATPase relative to the amount of Ca2+ and found that Tb3+ ions only reduced significantly the amount of Ca2+ bound after a considerable number of Tb3+ ions had bound. tb3+ 51-55 dynein axonemal heavy chain 8 Homo sapiens 69-75 1534084-4 1992 Simultaneously, we directly measured the amount of Tb3+ bound to the ATPase relative to the amount of Ca2+ and found that Tb3+ ions only reduced significantly the amount of Ca2+ bound after a considerable number of Tb3+ ions had bound. tb3+ 122-126 dynein axonemal heavy chain 8 Homo sapiens 69-75 1534084-4 1992 Simultaneously, we directly measured the amount of Tb3+ bound to the ATPase relative to the amount of Ca2+ and found that Tb3+ ions only reduced significantly the amount of Ca2+ bound after a considerable number of Tb3+ ions had bound. tb3+ 122-126 dynein axonemal heavy chain 8 Homo sapiens 69-75 1654822-2 1991 The luminescence of Tb3+ ions bound to gelsolin is markedly enhanced when excited indirectly at 295 nm due to Forster type dipole-dipole energy transfer from neighboring tryptophan residues. tb3+ 20-24 gelsolin Homo sapiens 39-47 1654822-6 1991 Different classes of Tb3+ ion binding sites can also be distinguished by the different Ca2+ ion concentrations needed to displace Tb3+ ions from these sites on gelsolin. tb3+ 21-25 gelsolin Homo sapiens 160-168 1654822-6 1991 Different classes of Tb3+ ion binding sites can also be distinguished by the different Ca2+ ion concentrations needed to displace Tb3+ ions from these sites on gelsolin. tb3+ 130-134 gelsolin Homo sapiens 160-168 1654822-7 1991 It is proposed that the occupancy of one class of Tb3+ ion binding sites on gelsolin causes a conformational change in gelsolin which then allows a second class of cryptic Tb3+ ion binding sites to be expressed. tb3+ 50-54 gelsolin Homo sapiens 76-84 1654822-7 1991 It is proposed that the occupancy of one class of Tb3+ ion binding sites on gelsolin causes a conformational change in gelsolin which then allows a second class of cryptic Tb3+ ion binding sites to be expressed. tb3+ 50-54 gelsolin Homo sapiens 119-127 1654822-7 1991 It is proposed that the occupancy of one class of Tb3+ ion binding sites on gelsolin causes a conformational change in gelsolin which then allows a second class of cryptic Tb3+ ion binding sites to be expressed. tb3+ 172-176 gelsolin Homo sapiens 76-84 1654822-7 1991 It is proposed that the occupancy of one class of Tb3+ ion binding sites on gelsolin causes a conformational change in gelsolin which then allows a second class of cryptic Tb3+ ion binding sites to be expressed. tb3+ 172-176 gelsolin Homo sapiens 119-127 1567990-3 1992 Specifically, the distance between Tb3+ bound at the Ca2+ site and Co2+ bound to the Zn2+ (Cu2+) binding site was 10.3 +/- 0.9 A. Lastly, the effects of Cu2+ on the physico-chemical properties of parvalbumin were studied by measuring the accessibility of protein thiol groups to 5,5"-dithio bis(2-nitrobenzoic acid) and by its affinity for the fluorescent probe 4,4"-bis[1-(phenylamino)-8-naphthalene sulfonic acid] dipotassium salt. tb3+ 35-39 parvalbumin Homo sapiens 196-207 34358784-2 2022 In this work, guanosine monophosphate (GMP), terbium ion (Tb3+) and zeolitic imidazolate framework-8 (ZIF-8) are self-assembled to form a ZIF-8@GMP-Tb nanocomplex, which can be utilized as a ratiometric fluorescent probe to monitor alkaline phosphatase (ALP) activity. tb3+ 58-62 alkaline phosphatase, placental Homo sapiens 232-252 1863267-2 1991 The binding of Tb3+ to calmodulin was followed by an increase in Tb3+ fluorescence at 545 nm. tb3+ 15-19 calmodulin 1 Homo sapiens 23-33 1863267-2 1991 The binding of Tb3+ to calmodulin was followed by an increase in Tb3+ fluorescence at 545 nm. tb3+ 65-69 calmodulin 1 Homo sapiens 23-33 1863267-3 1991 The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation. tb3+ 92-96 calmodulin 1 Homo sapiens 43-53 1863267-3 1991 The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation. tb3+ 157-161 calmodulin 1 Homo sapiens 43-53 1863267-3 1991 The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation. tb3+ 157-161 calmodulin 1 Homo sapiens 129-139 1863267-3 1991 The terbium fluorescence of phosphorylated calmodulin increased at a lower concentration of Tb3+ than that of non-phosphorylated calmodulin, indicating that Tb3+ binding affinity of calmodulin was increased by phosphorylation. tb3+ 157-161 calmodulin 1 Homo sapiens 129-139 2303477-2 1990 Moreover, the Tb3+ luminescence technique in parallel to a 19F NMR investigation, allowed us to measure the binding of a very potent specific inhibitor of porcine elastase (trifluoroacetyl-L-lysyl-alanyl p-trifluoromethylphenylanilide) to bovine subunit III. tb3+ 14-18 chymotrypsin like elastase 1 Bos taurus 163-171 2105078-1 1990 Intramolecular distance measurements were made in cardiac troponin C (cTnC) by fluorescence energy transfer using Eu3+ or Tb3+ as energy donors and Nd3+ or an organic chromophore as acceptors. tb3+ 122-126 troponin C1, slow skeletal and cardiac type Homo sapiens 50-68 2105078-1 1990 Intramolecular distance measurements were made in cardiac troponin C (cTnC) by fluorescence energy transfer using Eu3+ or Tb3+ as energy donors and Nd3+ or an organic chromophore as acceptors. tb3+ 122-126 troponin C1, slow skeletal and cardiac type Homo sapiens 70-74 33970959-2 2021 Ciprofloxacin (CP) makes efficient bondings to Tb3+ ion as a linker molecule through carboxylic and ketone groups to form a kind of lanthanide coordination polymer. tb3+ 47-51 ceruloplasmin Homo sapiens 0-13 33970959-2 2021 Ciprofloxacin (CP) makes efficient bondings to Tb3+ ion as a linker molecule through carboxylic and ketone groups to form a kind of lanthanide coordination polymer. tb3+ 47-51 ceruloplasmin Homo sapiens 15-17 33970959-3 2021 The addition of spermine that competes with Tb3+ ions for the interaction with CP due to its positive charge brings about weakened coordination linkage of CP and Tb3+. tb3+ 44-48 ceruloplasmin Homo sapiens 79-81 33970959-3 2021 The addition of spermine that competes with Tb3+ ions for the interaction with CP due to its positive charge brings about weakened coordination linkage of CP and Tb3+. tb3+ 44-48 ceruloplasmin Homo sapiens 155-157 33970959-3 2021 The addition of spermine that competes with Tb3+ ions for the interaction with CP due to its positive charge brings about weakened coordination linkage of CP and Tb3+. tb3+ 162-166 ceruloplasmin Homo sapiens 79-81 34358784-2 2022 In this work, guanosine monophosphate (GMP), terbium ion (Tb3+) and zeolitic imidazolate framework-8 (ZIF-8) are self-assembled to form a ZIF-8@GMP-Tb nanocomplex, which can be utilized as a ratiometric fluorescent probe to monitor alkaline phosphatase (ALP) activity. tb3+ 58-62 alkaline phosphatase, placental Homo sapiens 254-257 34358784-3 2022 Specifically, with adding ALP, the fluorescence intensity at 547 nm (one of the characteristic emission peaks of Tb3+) obviously decreased. tb3+ 113-117 alkaline phosphatase, placental Homo sapiens 26-29 34062750-0 2021 Mono- and Mixed Metal Complexes of Eu3+, Gd3+, and Tb3+ with a Diketone, Bearing Pyrazole Moiety and CHF2-Group: Structure, Color Tuning, and Kinetics of Energy Transfer between Lanthanide Ions. tb3+ 51-55 hes related family bHLH transcription factor with YRPW motif 1 Homo sapiens 101-105 34889024-4 2022 Interestingly, one fluorescent attenuation window was found with an increase of CF concentration (Q) from 0.1 to 10 mug mL-1 with the limit of detection (LOD) of 0.04 mug mL-1 at 544 nm belonging to the Tb3+ emission, as well as the other fluorescence enhanced window within the range of CF concentration from 10 to 100 mug mL-1 (LOD = 4 mug mL-1 ) at 617 nm of Eu3+ emission in the dispersed rare-earth doped MINs colloidal aqueous solution. tb3+ 203-207 L1 cell adhesion molecule Mus musculus 120-124 34855374-0 2021 Connectivity Replication of Neutral Eu3+- and Tb3+-Based Metal-Organic Frameworks (MOFs) from Anionic Cd2+-Based MOF Crystallites. tb3+ 46-50 CD2 molecule Homo sapiens 102-105 34792327-6 2021 SO-NTOs have a broad range of potential applications, which is illustrated by the T2-S1 state mixing in pyrazine, spin-forbidden versus spin-allowed 4f-5d transitions in the Tb3+ ion, and the phosphorescence of tris(2-phenylpyridine) iridium (Ir(ppy)3). tb3+ 174-178 spindlin 1 Homo sapiens 114-118 34792327-6 2021 SO-NTOs have a broad range of potential applications, which is illustrated by the T2-S1 state mixing in pyrazine, spin-forbidden versus spin-allowed 4f-5d transitions in the Tb3+ ion, and the phosphorescence of tris(2-phenylpyridine) iridium (Ir(ppy)3). tb3+ 174-178 spindlin 1 Homo sapiens 136-140 34170146-4 2021 Interestingly, this Tb-MOF exhibited dual luminescence owing to the partial energy transfer from the antenna H4L to Tb3+. tb3+ 116-120 H4 clustered histone 7 Homo sapiens 109-112 2604719-8 1989 Tb3+ (terbium ion) binding studies on the S100b.Zn2+6 complex proved that Tb3+ antagonizes only Ca2+ binding site II beta and confirmed the sequential occupation of Ca2+-binding sites on the S100b.Zn2+6 complex. tb3+ 0-4 S100 calcium binding protein B Bos taurus 42-47 35491036-3 2022 By employing terbium ion (Tb3+) as a metal node and guanine monophosphate (GMP) as a bridge ligand, an alkaline phosphatase (ALP)-responsive Tb/GMP CPs was fabricated, which allows amyloglucosidase (GA) to be integrated to form GA@Tb/GMP composite. tb3+ 26-30 alkaline phosphatase, placental Homo sapiens 103-123 35491036-3 2022 By employing terbium ion (Tb3+) as a metal node and guanine monophosphate (GMP) as a bridge ligand, an alkaline phosphatase (ALP)-responsive Tb/GMP CPs was fabricated, which allows amyloglucosidase (GA) to be integrated to form GA@Tb/GMP composite. tb3+ 26-30 alkaline phosphatase, placental Homo sapiens 125-128 35161072-3 2022 The analysis of the compression isotherms, infrared, and luminescence spectra of TbL3 bipy LBFs was performed by varying the concentration of Tb3+ in the subphases. tb3+ 142-146 transducin beta like 3 Homo sapiens 81-85 35057287-0 2022 Synthesis, Characterization and Biodistribution of GdF3:Tb3+@RB Nanocomposites. tb3+ 56-60 growth differentiation factor 3 Mus musculus 51-55 35057287-1 2022 Herein we report the development of a nanocomposite for X-ray-induced photodynamic therapy (X-PDT) and computed tomography (CT) based on PEG-capped GdF3:Tb3+ scintillating nanoparticles conjugated with Rose Bengal photosensitizer via electrostatic interactions. tb3+ 153-157 growth differentiation factor 3 Mus musculus 148-152 35057287-2 2022 Scintillating GdF3:Tb3+ nanoparticles were synthesized by a facile and cost-effective wet chemical precipitation method. tb3+ 19-23 growth differentiation factor 3 Mus musculus 14-18 35159907-2 2022 We explored and compared the loading/release ability of diclofenac (COX-2 antagonist), in both undoped- and luminescent Terbium3+ (Tb3+)-doped citrate-coated carbonated apatite nanoparticles at different temperatures (25, 37, 40 C) and pHs (7.4, 5.2). tb3+ 131-135 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-73 35161072-1 2022 In this study, we investigated the effect of terbium ions (Tb3+) on the subphases of the limiting area of the molecule for the complex compound (CC) TbL3 bipy (where HL is 3-methyl-1-phenyl-4-stearoylpyrazol-5-one and bipy is 2,2"-bipyridine). tb3+ 59-63 transducin beta like 3 Homo sapiens 149-153 35055276-0 2022 Luminescence of SiO2-BaF2:Tb3+, Eu3+ Nano-Glass-Ceramics Made from Sol-Gel Method at Low Temperature. tb3+ 26-30 BANF family member 2 Homo sapiens 21-25 2604719-8 1989 Tb3+ (terbium ion) binding studies on the S100b.Zn2+6 complex proved that Tb3+ antagonizes only Ca2+ binding site II beta and confirmed the sequential occupation of Ca2+-binding sites on the S100b.Zn2+6 complex. tb3+ 0-4 S100 calcium binding protein B Bos taurus 191-196 2604719-8 1989 Tb3+ (terbium ion) binding studies on the S100b.Zn2+6 complex proved that Tb3+ antagonizes only Ca2+ binding site II beta and confirmed the sequential occupation of Ca2+-binding sites on the S100b.Zn2+6 complex. tb3+ 74-78 S100 calcium binding protein B Bos taurus 42-47 2604719-8 1989 Tb3+ (terbium ion) binding studies on the S100b.Zn2+6 complex proved that Tb3+ antagonizes only Ca2+ binding site II beta and confirmed the sequential occupation of Ca2+-binding sites on the S100b.Zn2+6 complex. tb3+ 74-78 S100 calcium binding protein B Bos taurus 191-196 2447082-8 1988 Tb3+ and Ca2+ binding studies demonstrated a Ca2+-binding site in HPC4 required for high affinity antigen binding. tb3+ 0-4 HPC4 Homo sapiens 66-70 2590165-12 1989 Assuming that there were two Tb3+-binding sites on the toxin molecule, at pH 7.6 the association constants of the high-affinity and the low-affinity sites were determined to be 3.82 x 10(3) M-1 and 2.85 x 10(2) M-1 respectively. tb3+ 29-33 cholinergic receptor muscarinic 1 Homo sapiens 190-199 3595865-5 1987 Seminalplasmin also reduced the Tb3+-associated fluorescence of bovine spermatozoal plasma membrane. tb3+ 32-36 caltrin Bos taurus 0-14 3733748-1 1986 Distances between the four Ca2+-binding sites of calmodulin (CaM) have been measured by fluorescence energy transfer techniques using Eu3+ and Tb3+ as energy donors and a number of other lanthanide ions (Ln3+) as acceptors. tb3+ 143-147 calmodulin 1 Homo sapiens 49-59 3446175-0 1987 Spectroscopic studies on Tb3+ binding to S-100a protein. tb3+ 25-29 S100 calcium binding protein A1 Homo sapiens 41-47 3446175-9 1987 From u.v.-difference-spectroscopy results the single tryptophan and the tyrosine chromophores in S-100a protein are blue-shifted (i.e. exposed to the solvent) in the presence of Tb3+ and the observed conformational changes are similar to those induced by Ca2+, suggesting that Tb3+ can be employed as a Ca2+ analogue in spectral studies with S-100a protein. tb3+ 178-182 S100 calcium binding protein A1 Homo sapiens 97-103 3446175-9 1987 From u.v.-difference-spectroscopy results the single tryptophan and the tyrosine chromophores in S-100a protein are blue-shifted (i.e. exposed to the solvent) in the presence of Tb3+ and the observed conformational changes are similar to those induced by Ca2+, suggesting that Tb3+ can be employed as a Ca2+ analogue in spectral studies with S-100a protein. tb3+ 178-182 S100 calcium binding protein A1 Homo sapiens 342-348 3446175-9 1987 From u.v.-difference-spectroscopy results the single tryptophan and the tyrosine chromophores in S-100a protein are blue-shifted (i.e. exposed to the solvent) in the presence of Tb3+ and the observed conformational changes are similar to those induced by Ca2+, suggesting that Tb3+ can be employed as a Ca2+ analogue in spectral studies with S-100a protein. tb3+ 277-281 S100 calcium binding protein A1 Homo sapiens 97-103 3446175-9 1987 From u.v.-difference-spectroscopy results the single tryptophan and the tyrosine chromophores in S-100a protein are blue-shifted (i.e. exposed to the solvent) in the presence of Tb3+ and the observed conformational changes are similar to those induced by Ca2+, suggesting that Tb3+ can be employed as a Ca2+ analogue in spectral studies with S-100a protein. tb3+ 277-281 S100 calcium binding protein A1 Homo sapiens 342-348 3567142-3 1987 Addition of Ca2+ or Tb3+ to the ANS-apo-CaBP system is capable of enhancing its fluorescence up to about 2- or 5-fold, respectively, causing further blue shift of the emission maximum. tb3+ 20-24 S100 calcium binding protein G Homo sapiens 40-44 3567142-6 1987 Biphasic change of response has also been observed in UV absorption of the CaBP with increasing concentration of Tb3+. tb3+ 113-117 S100 calcium binding protein G Homo sapiens 75-79 3567142-8 1987 All these results indicate that the CaBP molecule contains a single ANS binding site and the conformation and/or microenvironment surrounding bound ANS of the protein is altered reversibly with binding of Ca2+ or Tb3+ to it and that there are differences between Ca2+- and Tb3+-induced conformation changes around the ANS-binding site and the tyrosine residue of it. tb3+ 213-217 S100 calcium binding protein G Homo sapiens 36-40 3567142-8 1987 All these results indicate that the CaBP molecule contains a single ANS binding site and the conformation and/or microenvironment surrounding bound ANS of the protein is altered reversibly with binding of Ca2+ or Tb3+ to it and that there are differences between Ca2+- and Tb3+-induced conformation changes around the ANS-binding site and the tyrosine residue of it. tb3+ 273-277 S100 calcium binding protein G Homo sapiens 36-40 2943224-5 1986 Plasmin treatment of the platelet surface reduced Tb3+ fluorescence by 68% at saturation without significantly affecting the approximate apparent Kd. tb3+ 50-54 plasminogen Homo sapiens 0-7 3733748-1 1986 Distances between the four Ca2+-binding sites of calmodulin (CaM) have been measured by fluorescence energy transfer techniques using Eu3+ and Tb3+ as energy donors and a number of other lanthanide ions (Ln3+) as acceptors. tb3+ 143-147 calmodulin 1 Homo sapiens 61-64 4079935-2 1985 The experimental results for protein preparations of calmodulin in which Ca2+ was isomorphically replaced by Tb3+ were obtained by a spectrometer working at the Institute of Nuclear Physics. tb3+ 109-113 calmodulin 1 Homo sapiens 53-63 3019337-1 1986 Calmodulin, spin labeled at Tyr-99, has been titrated with the lanthanides La3+, Nd3+, Eu3+, Tb3+, Er3+ and Lu3+ as well as Ca2+ and Cd2+. tb3+ 93-97 calmodulin 1 Homo sapiens 0-10 3730394-6 1986 Oncomodulin, however, was found to differ from parvalbumin in at least one important respect: In contrast to the muscle-associated protein, the affinities of the CD site in oncomodulation for Tb3+ and Ca2+ were found to be rather similar, with KCa/KTb approximately equal to 11 +/- 2. tb3+ 192-196 oncomodulin Rattus norvegicus 0-11 3092828-2 1986 In the range of concentrations tested, Cd2+ and lanthanides (Tb3+, Gd3+, Pr3+, Ce3+) could substitute for Ca2+ in activating the enzyme to about 60% and 70% respectively of the maximal level seen with Ca2+, at pH 8.2. tb3+ 61-65 T-cell surface antigen CD2 Oryctolagus cuniculus 39-42 3092828-2 1986 In the range of concentrations tested, Cd2+ and lanthanides (Tb3+, Gd3+, Pr3+, Ce3+) could substitute for Ca2+ in activating the enzyme to about 60% and 70% respectively of the maximal level seen with Ca2+, at pH 8.2. tb3+ 61-65 carbonic anhydrase 2 Oryctolagus cuniculus 106-109 3092828-2 1986 In the range of concentrations tested, Cd2+ and lanthanides (Tb3+, Gd3+, Pr3+, Ce3+) could substitute for Ca2+ in activating the enzyme to about 60% and 70% respectively of the maximal level seen with Ca2+, at pH 8.2. tb3+ 61-65 carbonic anhydrase 2 Oryctolagus cuniculus 201-204 3092828-5 1986 Cd2+ and Tb3+ were also able to replace Ca2+ required for the stimulation of phosphorylase kinase activity at pH 8.2 by exogenous calmodulin. tb3+ 9-13 carbonic anhydrase 2 Oryctolagus cuniculus 40-43 3092828-5 1986 Cd2+ and Tb3+ were also able to replace Ca2+ required for the stimulation of phosphorylase kinase activity at pH 8.2 by exogenous calmodulin. tb3+ 9-13 calmodulin Oryctolagus cuniculus 130-140 4066663-3 1985 In the present study, we find that the metal cations La3+, Tb3+, Pb2+, and Cd2+ are all capable of abolishing the cooperativity (Hill coefficient = 2.0) among the two felodipine-binding sites on calmodulin and can increase the apparent affinity of calmodulin for felodipine by approximately 20-fold. tb3+ 59-63 calmodulin 1 Homo sapiens 195-205 4066663-3 1985 In the present study, we find that the metal cations La3+, Tb3+, Pb2+, and Cd2+ are all capable of abolishing the cooperativity (Hill coefficient = 2.0) among the two felodipine-binding sites on calmodulin and can increase the apparent affinity of calmodulin for felodipine by approximately 20-fold. tb3+ 59-63 calmodulin 1 Homo sapiens 248-258 4066663-6 1985 In each case, the calcium-binding sites of calmodulin must be occupied (by calcium, La3+, Tb3+, Pb2+, or by Cd2+) before these metals can bind to sites which are distinct from the calcium-binding sites to produce the active conformer of calmodulin which exhibits enhanced affinity for felodipine. tb3+ 90-94 calmodulin 1 Homo sapiens 43-53 3839791-0 1985 Tb3+ binding to bovine prothrombin and bovine prothrombin fragment 1. tb3+ 0-4 coagulation factor II, thrombin Bos taurus 23-34 3839791-0 1985 Tb3+ binding to bovine prothrombin and bovine prothrombin fragment 1. tb3+ 0-4 coagulation factor II, thrombin Bos taurus 46-57 3839791-1 1985 The binding of Tb3+ to bovine prothrombin and the amino-terminal 156 residues of prothrombin (F-1) was studied. tb3+ 15-19 coagulation factor II, thrombin Bos taurus 30-41 3839791-12 1985 The emission properties of Tb3+ bound to F-1 were different in KCl versus NaCl containing buffer while the emission properties of Tb3+ bound to prothrombin were not. tb3+ 130-134 coagulation factor II, thrombin Bos taurus 144-155 3160702-3 1985 Terbium (Tb3+) competitively inhibited 45Ca2+ binding to fibrinogen during equilibrium dialysis, accelerated fibrin polymerization, and limited fibrinogen fragment D digestion by plasmin. tb3+ 9-13 fibrinogen beta chain Homo sapiens 57-67 3160702-3 1985 Terbium (Tb3+) competitively inhibited 45Ca2+ binding to fibrinogen during equilibrium dialysis, accelerated fibrin polymerization, and limited fibrinogen fragment D digestion by plasmin. tb3+ 9-13 fibrinogen beta chain Homo sapiens 144-154 3160702-4 1985 The intrinsic fluorescence of Ca2+-depleted fibrinogen was maximally enhanced by Ca2+ and Tb3+, but not by Mg2+, at about 3 mol of cation/mol of fibrinogen. tb3+ 90-94 fibrinogen beta chain Homo sapiens 44-54 3160702-5 1985 Protein-bound Tb3+ fluorescence at 545 nm was maximally enhanced by resonance energy transfer from tryptophan (excitation at 290 nm) at about 2 mol of Tb3+mol of fibrinogen and about 1 mol of Tb3+/mol of plasmic fragment D94 (Mr 94,000). tb3+ 14-18 fibrinogen beta chain Homo sapiens 162-172 6389227-2 1984 Terbium (Tb3+), an ion of the lanthanide series that has been used as a fluorescent probe for calcium (Ca2+) binding sites in proteins, binds to the proteins in both solubilized and purified human placental insulin receptor preparations. tb3+ 9-13 insulin receptor Homo sapiens 207-223 6389227-3 1984 Tb3+ fluorescence was determined directly and the effect of insulin binding on Tb3+-enhanced fluorescence was studied without the need to separate bound and free ligands. tb3+ 79-83 insulin Homo sapiens 60-67 6389227-4 1984 Tb3+ behaved similarly to, but was more potent (50-fold) than, Ca2+ in increasing the insulin bound to its receptor. tb3+ 0-4 insulin Homo sapiens 86-93 6389227-5 1984 When insulin bound to its receptor, the Tb3+ fluorescence of the receptor preparation decreased. tb3+ 40-44 insulin Homo sapiens 5-12 6389227-6 1984 When various insulin analogues were tested, the decrease in Tb3+ fluorescence was proportional to the biologic activity of the insulin analogues. tb3+ 60-64 insulin Homo sapiens 13-20 6469987-1 1984 The binding of Ca2+, Zn2+, Tb3+, and Mn2+ to metal-free bovine alpha-lactalbumin (apo-BLA) was studied by both analytical gel filtration using isotopic metal ions and by fluorescence titration. tb3+ 27-31 lactalbumin alpha Bos taurus 63-80 6389227-6 1984 When various insulin analogues were tested, the decrease in Tb3+ fluorescence was proportional to the biologic activity of the insulin analogues. tb3+ 60-64 insulin Homo sapiens 127-134 6389227-7 1984 In addition, Tb3+ could be displaced from insulin-sensitive sites by Ca2+, indicating that there were Ca2+ (and Tb3+) binding sites on or near the insulin receptor. tb3+ 13-17 insulin Homo sapiens 42-49 6389227-7 1984 In addition, Tb3+ could be displaced from insulin-sensitive sites by Ca2+, indicating that there were Ca2+ (and Tb3+) binding sites on or near the insulin receptor. tb3+ 13-17 insulin receptor Homo sapiens 147-163 6389227-7 1984 In addition, Tb3+ could be displaced from insulin-sensitive sites by Ca2+, indicating that there were Ca2+ (and Tb3+) binding sites on or near the insulin receptor. tb3+ 112-116 insulin receptor Homo sapiens 147-163 6389227-9 1984 The decrease in Tb3+ fluorescence after insulin binding may be indicative of a conformational change in the insulin receptor precipitated by the binding of insulin. tb3+ 16-20 insulin Homo sapiens 40-47 6389227-9 1984 The decrease in Tb3+ fluorescence after insulin binding may be indicative of a conformational change in the insulin receptor precipitated by the binding of insulin. tb3+ 16-20 insulin receptor Homo sapiens 108-124 6389227-9 1984 The decrease in Tb3+ fluorescence after insulin binding may be indicative of a conformational change in the insulin receptor precipitated by the binding of insulin. tb3+ 16-20 insulin Homo sapiens 108-115 6409902-4 1983 These results are consistent with the interpretation that binding of Tb3+ to the Ca2+-specific sites reduces the rate of dissociation of Ca2+ from, and thereby enhances the affinity for, the Ca2+-Mg2+ sites; this, in turn, suggests interactions between the two halves of the TnC molecule. tb3+ 69-73 tenascin C Homo sapiens 275-278 6236813-4 1984 As with calmodulin, the Ca2+-binding sites of all three purified calelectrins can be probed with Tb3+ which binds to them in a stoichiometric, saturable and Ca2+-displaceable manner. tb3+ 97-101 calmodulin Bos taurus 8-18 6469946-1 1984 Quantitative analyses were carried out on Tb3+ binding to porcine intestinal calcium-binding protein (CaBP). tb3+ 42-46 S100 calcium binding protein G Homo sapiens 102-106 6469946-2 1984 Tb3+ (emission at 547 nm) and intrinsic tyrosine (emission at 303 nm) fluorescences upon excitation at 260 nm increase almost in parallel with increasing Tb3+ concentration up to a molar ratio of 2 against the protein in the CaBP solution. tb3+ 0-4 S100 calcium binding protein G Homo sapiens 225-229 6469946-2 1984 Tb3+ (emission at 547 nm) and intrinsic tyrosine (emission at 303 nm) fluorescences upon excitation at 260 nm increase almost in parallel with increasing Tb3+ concentration up to a molar ratio of 2 against the protein in the CaBP solution. tb3+ 154-158 S100 calcium binding protein G Homo sapiens 225-229 6469946-3 1984 The pH dependence profile of Tb3+ fluorescence of the Tb3+-CaBP complex suggests that some free carboxylate groups are involved in the binding, as also suggested for Ca2+ binding. tb3+ 29-33 S100 calcium binding protein G Homo sapiens 59-63 6432301-4 1984 Excitation spectra of the Tb3+-bound forms of CaBP show that considerable energy transfer takes place from phenylalanine residues to the bound Tb3+, although some transfer from tyrosine is also detected. tb3+ 26-30 S100 calcium binding protein G Sus scrofa 46-50 6432301-4 1984 Excitation spectra of the Tb3+-bound forms of CaBP show that considerable energy transfer takes place from phenylalanine residues to the bound Tb3+, although some transfer from tyrosine is also detected. tb3+ 143-147 S100 calcium binding protein G Sus scrofa 46-50 6469946-4 1984 The results of fluorometric titration of Tb3+ and intrinsic tyrosine fluorescences of the CaBP complex with Tb3+ or Ca2+ led us to conclude that Tb3+ and Ca2+ have two common binding sites for each CaBP molecule. tb3+ 108-112 S100 calcium binding protein G Homo sapiens 90-94 6469946-4 1984 The results of fluorometric titration of Tb3+ and intrinsic tyrosine fluorescences of the CaBP complex with Tb3+ or Ca2+ led us to conclude that Tb3+ and Ca2+ have two common binding sites for each CaBP molecule. tb3+ 108-112 S100 calcium binding protein G Homo sapiens 198-202 6469946-4 1984 The results of fluorometric titration of Tb3+ and intrinsic tyrosine fluorescences of the CaBP complex with Tb3+ or Ca2+ led us to conclude that Tb3+ and Ca2+ have two common binding sites for each CaBP molecule. tb3+ 108-112 S100 calcium binding protein G Homo sapiens 90-94 6469946-4 1984 The results of fluorometric titration of Tb3+ and intrinsic tyrosine fluorescences of the CaBP complex with Tb3+ or Ca2+ led us to conclude that Tb3+ and Ca2+ have two common binding sites for each CaBP molecule. tb3+ 108-112 S100 calcium binding protein G Homo sapiens 198-202 6469946-6 1984 Tb3+ strongly inhibits 45Ca binding to one of the two Ca2+-binding sites in the CaBP. tb3+ 0-4 S100 calcium binding protein G Homo sapiens 80-84 6469946-7 1984 All of these and previous results indicate that each Tb3+ ion can bind to either of two high-affinity Ca2+-binding sites in porcine intestinal CaBP with an affinity different from that for Ca2+ ion. tb3+ 53-57 S100 calcium binding protein G Homo sapiens 143-147 6469946-8 1984 We discuss the localization of the Ca2+- and Tb3+-binding sites in the CaBP. tb3+ 45-49 S100 calcium binding protein G Homo sapiens 71-75 6688112-0 1983 Comparative abilities of lanthanide ions La3+ and Tb3+ to substitute for Ca2+ in regulating phospholipid-sensitive Ca2+-dependent protein kinase and myosin light chain kinase. tb3+ 50-54 myosin light chain kinase Rattus norvegicus 149-174 647063-1 1978 The interactions of angiotensin II and a synthetic analogue, [Asn1, Val5] angiotensin II, with Ca2+ and Tb3+ have been monitored using the intrinsic fluorescence of the tyrosine residue at position 4 in both molecules. tb3+ 104-108 angiotensinogen Homo sapiens 20-34 6885107-5 1983 We have used Tb3+ as an isomorphous analogue to study Ca2+ binding to CRP. tb3+ 13-17 C-reactive protein Homo sapiens 70-73 6885107-8 1983 A 50-fold molar excess of Ca2+ is sufficient to displace the Tb3+ suggesting that Tb3+ is bound with greater affinity to CRP than the natural analogue Ca2+. tb3+ 82-86 C-reactive protein Homo sapiens 121-124 6885107-9 1983 We propose that Tb3+ (by inference Ca2+) binding takes place near the CRP subunit disulfide bond, where two histidine residues are present. tb3+ 16-20 C-reactive protein Homo sapiens 70-73 6885107-10 1983 The pH dependency of Tb3+ binding is best explained by the deprotonation of a histidine residue(s) in CRP. tb3+ 21-25 C-reactive protein Homo sapiens 102-105 7085671-3 1982 We have carried out energy transfer measurements using Tb3+ as the donor and a number of lanthanide ions as acceptors in order to measure the distance between the two high affinity sites in TnC. tb3+ 55-59 tenascin C Homo sapiens 190-193 7085671-4 1982 Luminescence decay measurements showed that, in the absence of acceptors, TnC-bound Tb3+ decays with a single lifetime of 1.31 ms. tb3+ 84-88 tenascin C Homo sapiens 74-77 7085671-6 1982 The first was the same in lifetime as that of TnC-bound Tb3+ alone; the second has a shorter lifetime, presumably due to interlanthanide ion energy transfer. tb3+ 56-60 tenascin C Homo sapiens 46-49 7084230-5 1982 With calmodulin selectively nitrated at either of the two tyrosine residues we found that, although both tyrosine groups can transfer energy to the bound Tb3+, the fluorescence of only Tyr-138 is sensitive to metal binding. tb3+ 154-158 calmodulin 1 Homo sapiens 5-15 6276400-4 1982 The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin. tb3+ 15-19 calmodulin 1 Homo sapiens 23-33 6276400-4 1982 The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin. tb3+ 15-19 calmodulin 1 Homo sapiens 110-120 6276400-4 1982 The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin. tb3+ 66-70 calmodulin 1 Homo sapiens 23-33 6276400-4 1982 The binding of Tb3+ to calmodulin was followed by the increase of Tb3+ fluorescence at 545 nm upon binding to calmodulin. tb3+ 66-70 calmodulin 1 Homo sapiens 110-120 6276400-5 1982 This fluorescence was elicited either by exciting Tb3+ directly at 222 nm or by exciting the calmodulin tyrosine at 280 nm with resulting energy transfer from tyrosine to Tb3+. tb3+ 171-175 calmodulin 1 Homo sapiens 93-103 647063-1 1978 The interactions of angiotensin II and a synthetic analogue, [Asn1, Val5] angiotensin II, with Ca2+ and Tb3+ have been monitored using the intrinsic fluorescence of the tyrosine residue at position 4 in both molecules. tb3+ 104-108 angiotensinogen Homo sapiens 74-88 66108-2 1977 The fluorescence enhancement represents the binding of Tb3+ ions not only to (apo)transferrin, but to albumin and gamma-globulins as well. tb3+ 55-59 transferrin Homo sapiens 82-93 945070-6 1976 Dissociation constants for the complexes of enzyme with Ca2+, Eu3+, and Tb3+ were evaluated in PRR titrations by competition of these cations with Gd3+ binding. tb3+ 72-76 GRDX Homo sapiens 147-150 33960995-7 2021 More significantly, upon combining a few percent of Nd3+ and Gd3+ with Tb3+, the resulting trimetallic Tb0.4Gd0.5Nd0.1PCF shows dual emissions of both visible and near-infrared light. tb3+ 71-75 GRDX Homo sapiens 61-64 34023870-6 2021 As such, intense red and green UC emissions of Eu3+ and Tb3+ can further be generated via the cascade sensitization of Tm3+ and Gd3+ in Cs2NaYF6:Yb/Tm/Gd/Eu and Cs2NaYF6:Yb/Tm/Gd/Tb NPs, respectively. tb3+ 56-60 tropomyosin 3 Homo sapiens 119-122 34023870-6 2021 As such, intense red and green UC emissions of Eu3+ and Tb3+ can further be generated via the cascade sensitization of Tm3+ and Gd3+ in Cs2NaYF6:Yb/Tm/Gd/Eu and Cs2NaYF6:Yb/Tm/Gd/Tb NPs, respectively. tb3+ 56-60 GRDX Homo sapiens 128-131 32768732-2 2021 In this study, we reported that doping Terbium (III) ions (Tb3+) in self-activated luminescent nHAp via a facile hydrothermal reaction, using trisodium citrate (Cit3-), generates unique emission-tunable probes known as Cit/Tb-nHAp. tb3+ 59-63 citron rho-interacting serine/threonine kinase Homo sapiens 161-164 33615778-7 2021 Effects of the dilution of the Eu3+ and Tb3+ luminescent ions by Gd3+ optically inactive ions are unexpected and to the best of our knowledge unprecedented. tb3+ 40-44 GRDX Homo sapiens 65-68 33562698-0 2021 Structural and Photoluminescence Investigations of Tb3+/Eu3+ Co-Doped Silicate Sol-Gel Glass-Ceramics Containing CaF2 Nanocrystals. tb3+ 51-55 CCR4-NOT transcription complex subunit 8 Homo sapiens 113-117 33562698-6 2021 Performed decay analysis from the 5D0 (Eu3+) and the 5D4 (Tb3+) state revealed a correlation with the change in Tb3+-Eu3+ and Eu3+-Eu3+ interionic distances resulting from both the variable Tb3+:Eu3+ molar ratio and their partial segregation in CaF2 nanophase. tb3+ 58-62 CCR4-NOT transcription complex subunit 8 Homo sapiens 245-249 33562698-6 2021 Performed decay analysis from the 5D0 (Eu3+) and the 5D4 (Tb3+) state revealed a correlation with the change in Tb3+-Eu3+ and Eu3+-Eu3+ interionic distances resulting from both the variable Tb3+:Eu3+ molar ratio and their partial segregation in CaF2 nanophase. tb3+ 112-116 CCR4-NOT transcription complex subunit 8 Homo sapiens 245-249 32852009-4 2020 Upon the 6H15/2 4I13/2 excitation at 389 nm of the Dy3+ ion, the ET1 mechanism (Dy3+ Tb3+) was confirmed as a non-radiative dipole-dipole interaction. tb3+ 89-93 endothelin 1 Homo sapiens 67-70 32500616-2 2020 The Tb2 O2 SO4 compound was obtained at 1300 K and was used to compare thermal stability and photoluminescence behaviour with that of Gd2 O2 SO4 :Tb3+ (0.1, 1.0, and 10.0 mol%). tb3+ 146-150 receptor accessory protein 5 Homo sapiens 4-7 33239623-3 2020 The temperature responsive luminescence behavior of PSS-[Tb2(TCAn)2] within 293-333 K range in water is modulated by reversible changes derived from the back energy transfer from metal to ligand (M* T1) correlating with the energy gap between the triplet levels of ligands and resonant 5D4 level of Tb3+ ion. tb3+ 301-305 receptor accessory protein 5 Homo sapiens 57-60 33239623-6 2020 The insignificant release of toxic Tb3+ ions from PSS-[Tb2(TCAn)2] within heating/cooling cycle and the low cytotoxicity of the colloids point to their applicability in intracellular temperature monitoring. tb3+ 35-39 receptor accessory protein 5 Homo sapiens 55-58 32805836-4 2020 With the presence of thiocholine (TCh), an enzymatic product hydrolyzed from acetylthiocholine (ATCh) by AChE, the competitive coordination of Tb3+ between GMP and TCh results in the collapse of ICP network and thereby the release of GQDs into the solution, thus, the fluorescence of Tb/GMP turns off and the fluorescence of GQDs turns on. tb3+ 143-147 acetylcholinesterase (Cartwright blood group) Homo sapiens 105-109 32852009-5 2020 Under the 7F6 5L10 excitation at 370 nm of the Tb3+ ion, the ET2 mechanism (Tb3+ Eu3+) was identified as a non-radiative quadrupole-quadrupole interaction. tb3+ 49-53 endothelin 2 Homo sapiens 63-66 32175503-0 2020 3,5-Dihydroxy Benzoic Acid-Capped CaF2:Tb3+ Nanocrystals as Luminescent Probes for the WO4 2- Ion in Aqueous Solution. tb3+ 39-43 CCR4-NOT transcription complex subunit 8 Homo sapiens 34-38 32175503-2 2020 This is achieved using 3,5-dihydroxybenzoic acid-capped CaF2:Tb3+ (5%) nanocrystals (NCs) as a luminescent probe. tb3+ 61-65 CCR4-NOT transcription complex subunit 8 Homo sapiens 56-60 32175503-3 2020 This is accomplished based on the energy transfer luminescence from the WO4 2- ion to the Tb3+ ion in small-size CaF2:Tb3+ NCs. tb3+ 90-94 CCR4-NOT transcription complex subunit 8 Homo sapiens 113-117 32175503-3 2020 This is accomplished based on the energy transfer luminescence from the WO4 2- ion to the Tb3+ ion in small-size CaF2:Tb3+ NCs. tb3+ 118-122 CCR4-NOT transcription complex subunit 8 Homo sapiens 113-117 29778708-0 2018 Fluorescence resonance energy transfer of CaF2: Eu2+, Tb3+ applied to dye-sensitized solar cells. tb3+ 54-58 CCR4-NOT transcription complex subunit 8 Homo sapiens 42-46 31216643-4 2019 Inosine, an enzymatic product of ADA with stronger sensitization efficiency for Tb3+ than adenosine, produced a strong luminescence by forming an inosine-Tb3+ complex, and it enabled the direct monitoring of ADA activity in real-time. tb3+ 80-84 adenosine deaminase Homo sapiens 33-36 31216643-4 2019 Inosine, an enzymatic product of ADA with stronger sensitization efficiency for Tb3+ than adenosine, produced a strong luminescence by forming an inosine-Tb3+ complex, and it enabled the direct monitoring of ADA activity in real-time. tb3+ 154-158 adenosine deaminase Homo sapiens 33-36 31216643-4 2019 Inosine, an enzymatic product of ADA with stronger sensitization efficiency for Tb3+ than adenosine, produced a strong luminescence by forming an inosine-Tb3+ complex, and it enabled the direct monitoring of ADA activity in real-time. tb3+ 154-158 adenosine deaminase Homo sapiens 208-211 31216643-5 2019 By introducing only Tb3+ to adenosine and ADA in the buffer, the enhancement of luminescence enabled the detection of a low concentration of ADA (detection limit 1.6 U/L). tb3+ 20-24 adenosine deaminase Homo sapiens 141-144 31499989-3 2019 The adamantane can be immobilized on the surface of Tb3+-doped LDHs to obtain LDH-Ad, which could be further utilized for modified by the beta-cyclodextrin (beta-CD) containing hyperbranched polyglycerols (beta-CD-HPG) through the host-guest interaction. tb3+ 52-56 ACD shelterin complex subunit and telomerase recruitment factor Homo sapiens 157-164 31943967-1 2019 Biocompatible poly(4-styrenesulfonic acid-co-maleic acid)-stabilized GdF3 : Eu3+ (Tb3+ ) nanoparticles were obtained by a one-step coprecipitation method in ethylene glycol or water. tb3+ 83-87 growth differentiation factor 3 Homo sapiens 69-73 31152239-2 2019 This is achieved using 4-mercaptobenzoic acid (4-MBA)-capped CaF2:Tb3+ nanocrystals that were synthesized by a microwave procedure. tb3+ 66-70 CCR4-NOT transcription complex subunit 8 Homo sapiens 61-65 31152239-3 2019 4-MBA acts as both a capping agent and a sensitizer for the Tb3+ ions in CaF2 host matrix. tb3+ 60-64 CCR4-NOT transcription complex subunit 8 Homo sapiens 73-77 31152239-10 2019 Graphical abstract Schematic illustration of the use of 4-mercaptobenzoic acid (MBA)-capped CaF2:Tb3+ nanocrystals as a fluorescent nanoprobe for the detection of nitroaromatic analytes. tb3+ 97-101 CCR4-NOT transcription complex subunit 8 Homo sapiens 92-96 31152239-12 2019 The specific pi interaction between 4-MBA capped CaF2 nanocrystals and nitroaromatics leads to reduction in the fluorescence intensity by inhibiting the energy transfer from 4-MBA to Tb3+ ion in CaF2 nanocrystals. tb3+ 183-187 CCR4-NOT transcription complex subunit 8 Homo sapiens 49-53 31152239-12 2019 The specific pi interaction between 4-MBA capped CaF2 nanocrystals and nitroaromatics leads to reduction in the fluorescence intensity by inhibiting the energy transfer from 4-MBA to Tb3+ ion in CaF2 nanocrystals. tb3+ 183-187 CCR4-NOT transcription complex subunit 8 Homo sapiens 195-199 32254721-1 2018 In this study, bimetallic lanthanide coordination polymer nanoparticles (Tb-GMP-Eu CPNs) were developed for sensing alkaline phosphatase (ALP) by utilizing guanine monophosphate (GMP) as the bridge ligand to self-assemble with Tb3+ and Eu3+ in Tris-HCl buffer solution. tb3+ 227-231 alkaline phosphatase, placental Homo sapiens 116-136 32254721-1 2018 In this study, bimetallic lanthanide coordination polymer nanoparticles (Tb-GMP-Eu CPNs) were developed for sensing alkaline phosphatase (ALP) by utilizing guanine monophosphate (GMP) as the bridge ligand to self-assemble with Tb3+ and Eu3+ in Tris-HCl buffer solution. tb3+ 227-231 alkaline phosphatase, placental Homo sapiens 138-141 32254721-4 2018 When ALP was introduced into the Tb-GMP-Eu CPNs system, it would destruct the combination between Tb and GMP by a dephosphorylation process, resulting in interruption of energy transfer from Tb3+ to Eu3+ and therefore the fluorescence quenching of Eu3+. tb3+ 191-195 alkaline phosphatase, placental Homo sapiens 5-8 29778708-2 2018 The emission spectra of CaF2: Eu2+, Tb3+ included the blue light of Eu2+ (4f 5d) at 430 nm and green emission of Tb3+ (5D4 7F5) at 542 nm under the monitoring wavelengths at 398 nm, which matched well the absorption range of the N719 dye in DSSCs. tb3+ 36-40 CCR4-NOT transcription complex subunit 8 Homo sapiens 24-28 29778708-2 2018 The emission spectra of CaF2: Eu2+, Tb3+ included the blue light of Eu2+ (4f 5d) at 430 nm and green emission of Tb3+ (5D4 7F5) at 542 nm under the monitoring wavelengths at 398 nm, which matched well the absorption range of the N719 dye in DSSCs. tb3+ 115-119 CCR4-NOT transcription complex subunit 8 Homo sapiens 24-28 29778708-6 2018 Moreover, CaF2: Eu2+, Tb3+ enlarged the surface area of TiO2 photonaodes, which helped the adsorption performance of the TiO2 film. tb3+ 22-26 CCR4-NOT transcription complex subunit 8 Homo sapiens 10-14 29671424-0 2018 A fluorescent probe based on a Tb3+/Cu2+ co-functionalized MOF for urinary sarcosine detection. tb3+ 31-35 lysine acetyltransferase 8 Homo sapiens 59-62 30011931-7 2018 The substitution of Ca2+ by Tb3+ enables the electron and ion hopping in CaF2 nanocrystals, resulting in increased permittivity. tb3+ 28-32 CCR4-NOT transcription complex subunit 8 Homo sapiens 73-77 29660683-1 2018 Tb3+-doped YAlO3 (YAP) single crystal was grown by Czochralski (Cz) method. tb3+ 0-4 Yes1 associated transcriptional regulator Homo sapiens 18-21 29671424-1 2018 A novel luminescent probe based on a Tb3+/Cu2+ heterometallic metal-organic framework (MOF) was first designed for beamed monitoring of urinary sarcosine, a differential metabolite that can indicate the progression of prostate cancer (PCa). tb3+ 37-41 lysine acetyltransferase 8 Homo sapiens 62-91 28530267-1 2017 We describe a lanthanide biosensor that responds to CDK4 kinase activity in melanoma cell extracts through a significant and dose dependent increase in luminescence, thanks to sensitization of a DOTA[Tb3+] complex incorporated into a CDK4 substrate peptide by a unique tryptophan residue in an adjacent phosphoaminoacid binding moiety. tb3+ 200-204 cyclin dependent kinase 4 Homo sapiens 52-56 29242884-4 2018 Recently, it was demonstrated that Ho3+, Dy3+, Tb3+, and Gd3+ complexes enhance the polarization at 1.2 K and 3.35 T when using the trityl radical as the primary paramagnetic center. tb3+ 47-51 histidyl-tRNA synthetase 2, mitochondrial Homo sapiens 35-38 29543253-1 2018 In this Letter, we report for the first time, to the best of our knowledge, on an emission at 8 mum from Tb3+-doped Ga5Ge20Sb10Se65 chalcogenide fibers with doping levels at 1000 ppm and 500 ppm. tb3+ 105-109 latexin Homo sapiens 96-99 32264370-2 2017 The self-adaptive assembly of terbium ions (Tb3+), adenosine monophosphate (AMP), glucose oxidase (GOx), and carbon dots (CDs) leads to the formation of a GOx&CDs@AMP/Tb composite with catalytic and fluorescence properties. tb3+ 44-48 hydroxyacid oxidase 1 Homo sapiens 82-97 32264370-2 2017 The self-adaptive assembly of terbium ions (Tb3+), adenosine monophosphate (AMP), glucose oxidase (GOx), and carbon dots (CDs) leads to the formation of a GOx&CDs@AMP/Tb composite with catalytic and fluorescence properties. tb3+ 44-48 hydroxyacid oxidase 1 Homo sapiens 155-158 32264370-5 2017 On this basis, by considering the advantages of carboxyphenylboronic acid (CPBA) in the sensitization of Tb3+ fluorescence and specific recognition of hydrogen peroxide, a dual-emissive GOx&CDs@AMP/Tb-CPBA composite was further fabricated for the ratiometric sensing of glucose. tb3+ 105-109 hydroxyacid oxidase 1 Homo sapiens 186-189 28524205-0 2017 Structure and luminescence analyses of simultaneously synthesised (Lu1-xGdx)2O2S:Tb3+ and (Lu1-xGdx)2O3:Tb3. tb3+ 81-85 PDZ domain containing 4 Homo sapiens 67-70 28524205-7 2017 From this analysis it was concluded that the colour change of (Lu1-xGdx)2O2S:0.1%Tb3+ is caused by increasing energy transfer of the 5D3-level of Tb3+ to the charge transfer band of (Lu1-xGdx)2O2S:Tb3+ upon increasing x. tb3+ 81-85 PDZ domain containing 4 Homo sapiens 63-66 28524205-7 2017 From this analysis it was concluded that the colour change of (Lu1-xGdx)2O2S:0.1%Tb3+ is caused by increasing energy transfer of the 5D3-level of Tb3+ to the charge transfer band of (Lu1-xGdx)2O2S:Tb3+ upon increasing x. tb3+ 81-85 PDZ domain containing 4 Homo sapiens 183-186 28524205-7 2017 From this analysis it was concluded that the colour change of (Lu1-xGdx)2O2S:0.1%Tb3+ is caused by increasing energy transfer of the 5D3-level of Tb3+ to the charge transfer band of (Lu1-xGdx)2O2S:Tb3+ upon increasing x. tb3+ 146-150 PDZ domain containing 4 Homo sapiens 63-66 28524205-7 2017 From this analysis it was concluded that the colour change of (Lu1-xGdx)2O2S:0.1%Tb3+ is caused by increasing energy transfer of the 5D3-level of Tb3+ to the charge transfer band of (Lu1-xGdx)2O2S:Tb3+ upon increasing x. tb3+ 146-150 PDZ domain containing 4 Homo sapiens 183-186 28524205-7 2017 From this analysis it was concluded that the colour change of (Lu1-xGdx)2O2S:0.1%Tb3+ is caused by increasing energy transfer of the 5D3-level of Tb3+ to the charge transfer band of (Lu1-xGdx)2O2S:Tb3+ upon increasing x. tb3+ 146-150 PDZ domain containing 4 Homo sapiens 63-66 28524205-7 2017 From this analysis it was concluded that the colour change of (Lu1-xGdx)2O2S:0.1%Tb3+ is caused by increasing energy transfer of the 5D3-level of Tb3+ to the charge transfer band of (Lu1-xGdx)2O2S:Tb3+ upon increasing x. tb3+ 146-150 PDZ domain containing 4 Homo sapiens 183-186 28530267-1 2017 We describe a lanthanide biosensor that responds to CDK4 kinase activity in melanoma cell extracts through a significant and dose dependent increase in luminescence, thanks to sensitization of a DOTA[Tb3+] complex incorporated into a CDK4 substrate peptide by a unique tryptophan residue in an adjacent phosphoaminoacid binding moiety. tb3+ 200-204 cyclin dependent kinase 4 Homo sapiens 234-238 27987304-5 2017 One random pVIII phage library was screened for peptide sequences that bind specifically to the fluorescent phosphor LaPO4 :Ce3+ ,Tb3+ (LAP). tb3+ 130-134 LAP Homo sapiens 136-139