PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 32543371-3 2020 Here we report the cryo-electron microscopy (cryo-EM) structure of Homo sapiens CHD4 engaged with a nucleosome core particle in the presence of the non-hydrolysable ATP analogue AMP-PNP at an overall resolution of 3.1 A. Adenylyl Imidodiphosphate 178-185 chromodomain helicase DNA binding protein 4 Homo sapiens 80-84 28483598-6 2017 We found that stretch activation requires the presence of the SUR subunit and that inhibition of MgATPase activity with either the non-hydrolysable ATP analog AMP-PNP or the ATPase inhibitor BeFx significantly reduced the stimulatory effect of stretch. Adenylyl Imidodiphosphate 159-166 ATP binding cassette subfamily C member 8 Homo sapiens 62-65 31311868-3 2019 An X-ray structure of active 2P-ERK2 complexed with AMP-PNP reveals a shift in the Gly-rich loop along with domain closure to position the nucleotide in a more catalytically productive conformation relative to inactive 0P-ERK2:ATP. Adenylyl Imidodiphosphate 52-59 mitogen-activated protein kinase 1 Homo sapiens 32-36 31311868-3 2019 An X-ray structure of active 2P-ERK2 complexed with AMP-PNP reveals a shift in the Gly-rich loop along with domain closure to position the nucleotide in a more catalytically productive conformation relative to inactive 0P-ERK2:ATP. Adenylyl Imidodiphosphate 52-59 mitogen-activated protein kinase 1 Homo sapiens 222-226 31311868-6 2019 Solution measurements by hydrogen-exchange mass spectrometry (HX-MS) reveal distinct binding interactions for Vertex-11e, GDC-0994, and AMP-PNP with active vs. inactive ERK2, where the extent of HX protection correlates with R state formation. Adenylyl Imidodiphosphate 136-143 mitogen-activated protein kinase 1 Homo sapiens 169-173 31131400-4 2019 A translocation model is proposed for the Upf1-like helicase members according to three different structural conditions in solution characterized through H/D exchange assay, including substrate state (SARS-Nsp13-dsDNA bound with AMPPNP), transition state (bound with ADP-AlF4-) and product state (bound with ADP). Adenylyl Imidodiphosphate 229-235 UPF1 RNA helicase and ATPase Homo sapiens 42-46 31131400-4 2019 A translocation model is proposed for the Upf1-like helicase members according to three different structural conditions in solution characterized through H/D exchange assay, including substrate state (SARS-Nsp13-dsDNA bound with AMPPNP), transition state (bound with ADP-AlF4-) and product state (bound with ADP). Adenylyl Imidodiphosphate 229-235 seryl-tRNA synthetase 1 Homo sapiens 201-205 30679311-4 2019 To address this issue, here we first solved three crystal structures of the IRAK4 kinase domain (at <=2.6 A resolution), in its unphosphorylated, inactive state bound to either the ATP analog AMP-PNP or to one of the two small-molecule inhibitors JH-I-25 and JH-I-17. Adenylyl Imidodiphosphate 195-202 interleukin 1 receptor associated kinase 4 Homo sapiens 76-81 30296498-6 2019 Furthermore, PTS2 proteins are translocated to peroxisomes in the presence of a non-hydrolyzable ATP analogue, adenylyl imidodiphosphate, and N-ethylmaleimide, suggesting that ATP-dependent chaperones including Hsc70 are dispensable for PTS2 protein import. Adenylyl Imidodiphosphate 111-136 heat shock protein family A (Hsp70) member 8 Homo sapiens 211-216 29980677-5 2018 AMPPNP-bound Kif2A can form stable complexes with tubulin in solution and trigger MT depolymerization. Adenylyl Imidodiphosphate 0-6 kinesin family member 2A Homo sapiens 13-18 28648599-4 2017 Furthermore, the effect of BDM on the S1-bound adenosine 5"-(beta,gamma-imido) triphosphate (AMPPNP) 31P NMR spectrum suggests that BDM changes the microenvironment around the phosphorus atoms of myosin-bound nucleotide. Adenylyl Imidodiphosphate 93-99 myosin heavy chain 14 Homo sapiens 196-202 30891827-4 2019 Here, we present crystal structures of algal ArsA1 (the Get3 homolog) in a distinct nucleotide-free open state and bound to adenylyl-imidodiphosphate. Adenylyl Imidodiphosphate 124-149 guanine nucleotide exchange factor GET3 Saccharomyces cerevisiae S288C 56-60 30461091-0 2019 Crystal structure of human vaccinia-related kinase 1 in complex with AMP-PNP, a non-hydrolyzable ATP analog. Adenylyl Imidodiphosphate 69-76 VRK serine/threonine kinase 1 Homo sapiens 27-52 30461091-5 2019 Here we report the molecular characterization of VRK1 in complex with AMP-PNP, a non-hydrolyzable ATP-analog, using NMR titration followed by the co-crystal structure determined upto 2.07 A resolution. Adenylyl Imidodiphosphate 70-77 VRK serine/threonine kinase 1 Homo sapiens 49-53 30461091-6 2019 We also carried out the structural comparison of the AMP-PNP bound-form with its apo and inhibitor-bound counterparts, which has enabled us to present our rationale toward designing VRK1-specific inhibitors. Adenylyl Imidodiphosphate 53-60 VRK serine/threonine kinase 1 Homo sapiens 182-186 27558949-5 2016 We also examined the interaction of these FGFR1 variants to AMP-PNP, a nonhydrolyzable analogue of ATP, and showed that N546K showed increased affinity for the ATP analogue as compared with the wild type. Adenylyl Imidodiphosphate 60-67 fibroblast growth factor receptor 1 Homo sapiens 42-47 27328749-7 2016 The chaperonin-bound MreB is also significantly compacted after addition of AMP-PNP for both the GroEL/ES and TRiC systems. Adenylyl Imidodiphosphate 76-83 GroEL Escherichia coli 97-102 27528681-3 2016 We solved the crystal structure of the murine MORC3 ATPase-CW domain bound to the nucleotide analog AMPPNP (phosphoaminophosphonic acid-adenylate ester) and in complex with a trimethylated histone H3 lysine 4 (H3K4) peptide (H3K4me3). Adenylyl Imidodiphosphate 108-151 microrchidia 3 Mus musculus 46-51 26293246-3 2015 Applying this method to the human serine/threonine kinase B-Raf, frequently mutated in cancer, we found that binding of ATP or its nonhydrolyzable analogue AMP-PNP, but not ADP, stabilized the structure of both B-Raf(WT) and B-Raf(V600E). Adenylyl Imidodiphosphate 156-163 B-Raf proto-oncogene, serine/threonine kinase Homo sapiens 58-63 26597175-0 2015 Structures of the CDK12/CycK complex with AMP-PNP reveal a flexible C-terminal kinase extension important for ATP binding. Adenylyl Imidodiphosphate 42-49 cyclin dependent kinase 12 Homo sapiens 18-23 26597175-0 2015 Structures of the CDK12/CycK complex with AMP-PNP reveal a flexible C-terminal kinase extension important for ATP binding. Adenylyl Imidodiphosphate 42-49 cyclin K Homo sapiens 24-28 26597175-3 2015 To better define these interactions we determined the crystal structure of the human CDK12/CycK complex with and without the kinase extension in the presence of AMP-PNP. Adenylyl Imidodiphosphate 161-168 cyclin dependent kinase 12 Homo sapiens 85-90 26597175-3 2015 To better define these interactions we determined the crystal structure of the human CDK12/CycK complex with and without the kinase extension in the presence of AMP-PNP. Adenylyl Imidodiphosphate 161-168 cyclin K Homo sapiens 91-95 26293246-3 2015 Applying this method to the human serine/threonine kinase B-Raf, frequently mutated in cancer, we found that binding of ATP or its nonhydrolyzable analogue AMP-PNP, but not ADP, stabilized the structure of both B-Raf(WT) and B-Raf(V600E). Adenylyl Imidodiphosphate 156-163 B-Raf proto-oncogene, serine/threonine kinase Homo sapiens 211-216 26293246-3 2015 Applying this method to the human serine/threonine kinase B-Raf, frequently mutated in cancer, we found that binding of ATP or its nonhydrolyzable analogue AMP-PNP, but not ADP, stabilized the structure of both B-Raf(WT) and B-Raf(V600E). Adenylyl Imidodiphosphate 156-163 B-Raf proto-oncogene, serine/threonine kinase Homo sapiens 211-216 25785725-6 2015 In addition, we determined the structure of a TRAP1-adenylyl-imidodiphosphate (AMP-PNP) complex. Adenylyl Imidodiphosphate 79-86 TNF receptor associated protein 1 Homo sapiens 46-51 26377800-5 2015 The crystal structure of the unphosphorylated form of DJNK complexed with adenylyl imidodiphosphate (AMP-PNP) has been solved at 1.79 A resolution. Adenylyl Imidodiphosphate 74-99 basket Drosophila melanogaster 54-58 26377800-5 2015 The crystal structure of the unphosphorylated form of DJNK complexed with adenylyl imidodiphosphate (AMP-PNP) has been solved at 1.79 A resolution. Adenylyl Imidodiphosphate 101-108 basket Drosophila melanogaster 54-58 24563543-2 2014 As was expected, based on the finding of previous studies, the SR398/GroES complex was extremely stable in the presence of an excess amount of free adenosine 5"-[gamma-thio]triphosphate (ATPgammaS) or adenosine 5"-(beta,gamma-imido)triphosphate (AMPPNP). Adenylyl Imidodiphosphate 246-252 heat shock protein family E (Hsp10) member 1 Homo sapiens 69-74 25030449-5 2014 Here, we present the apo structure of the heterodimeric ABC exporter TM287/288 and compare it to the previously solved structure with adenosine 5"-(beta,gamma-imido)triphosphate (AMP-PNP) bound at the degenerate site. Adenylyl Imidodiphosphate 179-186 ATP binding cassette subfamily B member 6 (Langereis blood group) Homo sapiens 56-59 23914841-4 2013 Here we report the first structures of MELK in complex with AMP-PNP and with nanomolar inhibitors. Adenylyl Imidodiphosphate 60-67 maternal embryonic leucine zipper kinase Homo sapiens 39-43 24531485-5 2014 This paper reports the crystal structure of MPK38 (T167E), which mimics a phosphorylated state of the activation loop, in complex with AMP-PNP. Adenylyl Imidodiphosphate 135-142 maternal embryonic leucine zipper kinase Mus musculus 44-49 24462203-3 2014 Here we present a functional characterization of 2.5 A and 3.25 A X-ray crystal and small-angle X-ray scattering structures of RNase L bound to a natural 2-5A activator with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP. Adenylyl Imidodiphosphate 225-232 ribonuclease L Homo sapiens 127-134 24095729-6 2013 Free RIP3 exists in an active conformation, whereas MLKL-bound RIP3 is stabilized by AMP-PNP to adopt an inactive conformation. Adenylyl Imidodiphosphate 85-92 mixed lineage kinase domain-like Mus musculus 52-56 24095729-6 2013 Free RIP3 exists in an active conformation, whereas MLKL-bound RIP3 is stabilized by AMP-PNP to adopt an inactive conformation. Adenylyl Imidodiphosphate 85-92 receptor-interacting serine-threonine kinase 3 Mus musculus 63-67 23777303-3 2013 The performance of the constructed estimators is demonstrated with computer simulations of Forster-type resonance energy transfer (FRET) measurements and also with FRET experimental data of the agonist-binding domain of the GluA2 subunit of AMPA receptors with agonists chloro- and iodo-willardiines and with adenylate kinase both in the apo form and with substrates AMP-PNP and AMP. Adenylyl Imidodiphosphate 367-374 glutamate ionotropic receptor AMPA type subunit 2 Homo sapiens 224-229 23500491-3 2013 Here, we report the first crystal structure of KIF4 complexed with the non-hydrolyzable ATP analog, AMPPNP (adenylyl imidodiphosphate), at 1.7A resolution. Adenylyl Imidodiphosphate 100-106 kinesin family member 4A Homo sapiens 47-51 23620589-4 2013 Here we show that CFTR activation by adenosine 5"-O-(thiotriphosphate) (ATPgammaS), adenosine 5"-(beta,gamma-imino)triphosphate (AMP-PNP), and guanosine 5"-3-O-(thio)triphosphate (GTPgammaS) is enhanced substantially by gain of function (GOF) mutations in the cytosolic loops that increase unliganded activity. Adenylyl Imidodiphosphate 84-127 CF transmembrane conductance regulator Homo sapiens 18-22 23620589-4 2013 Here we show that CFTR activation by adenosine 5"-O-(thiotriphosphate) (ATPgammaS), adenosine 5"-(beta,gamma-imino)triphosphate (AMP-PNP), and guanosine 5"-3-O-(thio)triphosphate (GTPgammaS) is enhanced substantially by gain of function (GOF) mutations in the cytosolic loops that increase unliganded activity. Adenylyl Imidodiphosphate 129-136 CF transmembrane conductance regulator Homo sapiens 18-22 23500491-3 2013 Here, we report the first crystal structure of KIF4 complexed with the non-hydrolyzable ATP analog, AMPPNP (adenylyl imidodiphosphate), at 1.7A resolution. Adenylyl Imidodiphosphate 108-133 kinesin family member 4A Homo sapiens 47-51 23554946-7 2013 Two experiments indicate that phosphorylation is required for dBest1 activation: nonspecific protein kinase inhibitors or intracellular perfusion with the non-hydrolyzable ATP analog AMP-PNP dramatically reduce the amplitude of dBest1 currents. Adenylyl Imidodiphosphate 183-190 Bestrophin 1 Drosophila melanogaster 62-68 22864626-9 2013 Binding conformation of P-gp co-crystallized complexes with ADP, AMP-PNP (Adenylyl-imidodiphosphate), and ATP were compared with piperine. Adenylyl Imidodiphosphate 65-72 PGP Canis lupus familiaris 24-28 22864626-9 2013 Binding conformation of P-gp co-crystallized complexes with ADP, AMP-PNP (Adenylyl-imidodiphosphate), and ATP were compared with piperine. Adenylyl Imidodiphosphate 74-99 PGP Canis lupus familiaris 24-28 23154170-3 2013 Here, we present the first crystal structures of full-length Syk (fl-Syk) as wild type and as Y348F,Y352F mutant forms in complex with AMP-PNP revealing an autoinhibited conformation. Adenylyl Imidodiphosphate 135-142 spleen associated tyrosine kinase Homo sapiens 61-64 23154170-3 2013 Here, we present the first crystal structures of full-length Syk (fl-Syk) as wild type and as Y348F,Y352F mutant forms in complex with AMP-PNP revealing an autoinhibited conformation. Adenylyl Imidodiphosphate 135-142 spleen associated tyrosine kinase Homo sapiens 69-72 23154170-4 2013 The comparison with the crystal structure of the truncated Syk kinase domain in complex with AMP-PNP taken together with ligand binding studies by surface plasmon resonance (SPR) suggests conformational differences in the ATP sites of autoinhibited and activated Syk forms. Adenylyl Imidodiphosphate 93-100 spleen associated tyrosine kinase Homo sapiens 59-62 23154170-4 2013 The comparison with the crystal structure of the truncated Syk kinase domain in complex with AMP-PNP taken together with ligand binding studies by surface plasmon resonance (SPR) suggests conformational differences in the ATP sites of autoinhibited and activated Syk forms. Adenylyl Imidodiphosphate 93-100 spleen associated tyrosine kinase Homo sapiens 263-266 23554946-7 2013 Two experiments indicate that phosphorylation is required for dBest1 activation: nonspecific protein kinase inhibitors or intracellular perfusion with the non-hydrolyzable ATP analog AMP-PNP dramatically reduce the amplitude of dBest1 currents. Adenylyl Imidodiphosphate 183-190 Bestrophin 1 Drosophila melanogaster 228-234 23028292-6 2012 Here, we investigated whether interactions with the ATP analog AMP-PNP and ADP can shift the conformational ensemble of Csk in solution using a combination of small angle x-ray scattering and molecular dynamics simulations. Adenylyl Imidodiphosphate 63-70 C-terminal Src kinase Homo sapiens 120-123 20597513-7 2010 Crystallographic characterization of inactive versus AMP-PNP-liganded structures of FAK1 showed that a large conformational motion of the activation loop upon ATP binding may be an essential step during catalysis and would explain the viscosity effect observed on k(cat)/K(m) for MgATP but not on k(cat)/K(m) for FAK-tide. Adenylyl Imidodiphosphate 53-60 protein tyrosine kinase 2 Homo sapiens 84-88 22101826-4 2011 Here, two X-ray crystallographic structures of human Suv3 in complex with AMPPNP, a nonhydrolysable analog of ATP, and with a short five-nucleotide strand of RNA are presented at resolutions of 2.08 and 2.9 A, respectively. Adenylyl Imidodiphosphate 74-80 Suv3 like RNA helicase Homo sapiens 53-57 21904029-5 2011 ADP-bound PDK4 has a slightly wider active-site cleft and a more disordered ATP lid compared with AMPPNP-bound PDK4, although both forms of PDK4 assume open conformations with a wider active-site cleft than that in the closed conformation of the previously reported ADP-bound PDK2 structure. Adenylyl Imidodiphosphate 98-104 pyruvate dehydrogenase kinase 4 Homo sapiens 10-14 21904029-5 2011 ADP-bound PDK4 has a slightly wider active-site cleft and a more disordered ATP lid compared with AMPPNP-bound PDK4, although both forms of PDK4 assume open conformations with a wider active-site cleft than that in the closed conformation of the previously reported ADP-bound PDK2 structure. Adenylyl Imidodiphosphate 98-104 pyruvate dehydrogenase kinase 4 Homo sapiens 111-115 21904029-5 2011 ADP-bound PDK4 has a slightly wider active-site cleft and a more disordered ATP lid compared with AMPPNP-bound PDK4, although both forms of PDK4 assume open conformations with a wider active-site cleft than that in the closed conformation of the previously reported ADP-bound PDK2 structure. Adenylyl Imidodiphosphate 98-104 pyruvate dehydrogenase kinase 4 Homo sapiens 111-115 21904029-7 2011 M77976 binding also leads to a large domain rearrangement that further expands the active-site cleft of PDK4 compared with the ADP- and AMPPNP-bound forms. Adenylyl Imidodiphosphate 136-142 pyruvate dehydrogenase kinase 4 Homo sapiens 104-108 21288910-6 2011 The binding of AMPPNP or ADP results in a 3-fold increase in the affinity of TraI for ssDNA. Adenylyl Imidodiphosphate 15-21 TraI, lipoprotein Escherichia coli 77-81 21056978-8 2011 Binding of the non-hydrolysable ATP analog adenosine 5"-(beta,gamma-imino)triphosphate to the ternary complex leads to 3-fold faster release of actin from CCT following addition of ATP, suggesting a two-step folding process with a conformational change occurring upon closure of the cavity and a subsequent final folding step involving packing of the C terminus to the native-like state. Adenylyl Imidodiphosphate 43-86 actin Saccharomyces cerevisiae S288C 144-149 20726546-1 2010 A complex of RON(M1254T) with AMP-PNP and Mg(2+) reveals a substratelike positioning of Tyr1238 as well as likely catalysis-competent placement of the AMP-PNP and Mg(2+) components and indicates a tendency for cis phosphorylation. Adenylyl Imidodiphosphate 30-37 macrophage stimulating 1 receptor Homo sapiens 13-16 20726546-1 2010 A complex of RON(M1254T) with AMP-PNP and Mg(2+) reveals a substratelike positioning of Tyr1238 as well as likely catalysis-competent placement of the AMP-PNP and Mg(2+) components and indicates a tendency for cis phosphorylation. Adenylyl Imidodiphosphate 151-158 macrophage stimulating 1 receptor Homo sapiens 13-16 20597513-7 2010 Crystallographic characterization of inactive versus AMP-PNP-liganded structures of FAK1 showed that a large conformational motion of the activation loop upon ATP binding may be an essential step during catalysis and would explain the viscosity effect observed on k(cat)/K(m) for MgATP but not on k(cat)/K(m) for FAK-tide. Adenylyl Imidodiphosphate 53-60 protein tyrosine kinase 2 Homo sapiens 84-87 19759018-6 2009 The presence of 5"-adenylyl-beta,gamma-imidodiphosphate (AMPPNP), a nonhydrolyzable ATP analog, promotes stable complex formation between RecQ4 and single-stranded DNA. Adenylyl Imidodiphosphate 57-63 RecQ4 helicase Drosophila melanogaster 138-143 20362584-7 2010 While ATP or AMP-PNP (adenylyl-imidodiphosphate) binding to wild-type myosin subfragment-1 enhanced tryptophan fluorescence by approximately 15% or approximately 8%, respectively, enhancement does not occur in the mutant. Adenylyl Imidodiphosphate 13-20 zipper Drosophila melanogaster 70-76 20362584-7 2010 While ATP or AMP-PNP (adenylyl-imidodiphosphate) binding to wild-type myosin subfragment-1 enhanced tryptophan fluorescence by approximately 15% or approximately 8%, respectively, enhancement does not occur in the mutant. Adenylyl Imidodiphosphate 22-47 zipper Drosophila melanogaster 70-76 20118258-5 2010 ORF735 existed in solution as a salt-stable dimer and was capable of assembling into a salt-sensitive oligomer that was significantly larger than a hexamer in the presence of a divalent cation (Mg(2+)) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP). Adenylyl Imidodiphosphate 276-282 hypothetical protein Saccharolobus solfataricus P2 0-6 20479275-3 2010 Here, we report the 3.4 A resolution crystal structure of a minimal UPF3b-EJC assembly, consisting of the interacting domains of five proteins (UPF3b, MAGO, Y14, eIF4AIII, and Barentsz) together with RNA and adenylyl-imidodiphosphate. Adenylyl Imidodiphosphate 208-233 UPF3B regulator of nonsense mediated mRNA decay Homo sapiens 68-73 20146535-6 2010 We found that LRRK2 follows a rapid equilibrium random mechanism for the phosphorylation of PLK-peptide with either ATP or PLK-peptide being the first substrate binding to the enzyme, as evidenced by initial velocity and inhibition mechanism studies with nucleotide analogues AMP and AMP-PNP, product ADP, and an analogue of the peptide substrate. Adenylyl Imidodiphosphate 284-291 leucine-rich repeat kinase 2 Mus musculus 14-19 20146535-6 2010 We found that LRRK2 follows a rapid equilibrium random mechanism for the phosphorylation of PLK-peptide with either ATP or PLK-peptide being the first substrate binding to the enzyme, as evidenced by initial velocity and inhibition mechanism studies with nucleotide analogues AMP and AMP-PNP, product ADP, and an analogue of the peptide substrate. Adenylyl Imidodiphosphate 284-291 polo like kinase 1 Mus musculus 92-95 20179333-2 2010 In this study, the crystal structures of the human Hsp70 nucleotide-binding domain (NBD) fragment were determined in the nucleotide-free state and in complex with adenosine 5"-(beta,gamma-imido)triphosphate (AMPPNP). Adenylyl Imidodiphosphate 208-214 heat shock protein family A (Hsp70) member 4 Homo sapiens 51-56 20062530-7 2010 To fully characterise hDmc1-DNA complexes we have analysed their organisation in the presence of Ca2+, Mg2+, ATP, AMP-PNP, ssDNA and dsDNA. Adenylyl Imidodiphosphate 114-121 DNA meiotic recombinase 1 Homo sapiens 22-27 19956600-3 2009 The crystal structure of the NTD RSK2 was determined at 1.8 A resolution in complex with AMP-PNP. Adenylyl Imidodiphosphate 89-96 ribosomal protein S6 kinase A3 Homo sapiens 33-37 19748356-2 2009 Here we determined high-resolution X-ray crystal structures of Mss116p complexed with an RNA oligonucleotide and ATP analogs AMP-PNP, ADP-BeF(3)(-), or ADP-AlF(4)(-). Adenylyl Imidodiphosphate 125-132 ATP-dependent RNA helicase Saccharomyces cerevisiae S288C 63-70 19285157-5 2009 We further investigated the mode of peptide interaction with the proteolytically inactive Lon mutant S679A in the absence and presence of ADP or AMPPNP by 2-dimensional nuclear magnetic resonance spectroscopy, and discovered that the binding interaction between protein and peptide varies with the nucleotide bound to the enzyme. Adenylyl Imidodiphosphate 145-151 putative ATP-dependent Lon protease Escherichia coli 90-93 19652352-0 2009 Crystallization and preliminary X-ray diffraction of the DEAD-box protein Mss116p complexed with an RNA oligonucleotide and AMP-PNP. Adenylyl Imidodiphosphate 124-131 ATP-dependent RNA helicase Saccharomyces cerevisiae S288C 74-81 19622740-6 2009 Compressed Rad51 filaments can re-elongate when presented with either ATP or the non-hydrolyzable analog AMP-PNP, and these cycles of elongation and compression are reversible. Adenylyl Imidodiphosphate 105-112 RAD51 recombinase Homo sapiens 11-16 19622740-8 2009 Similarly, wild-type Rad51 bound to DNA in the presence of AMP-PNP was trapped in the elongated state. Adenylyl Imidodiphosphate 59-66 RAD51 recombinase Homo sapiens 21-26 19554567-6 2009 In contrast to cytosolic Hsp90, crystal structures of the endoplasmic reticulum homolog, Grp94, show the same conformation in the presence of both ADP and AMPPNP. Adenylyl Imidodiphosphate 155-161 heat shock protein 90, beta (Grp94), member 1 Mus musculus 89-94 18194602-4 2007 RESULTS: AMP-PNP, one non-hydrolysis ATP analogue and P2Y receptor agonist, induced significant phosphorylation of Akt in a time- and dose-dependent manner in IE8 cells. Adenylyl Imidodiphosphate 9-16 AKT serine/threonine kinase 1 Homo sapiens 115-118 18458329-3 2008 Here we present the structure of the extracellular domain of Rattus norvegicus NTPDase2 in an active state at resolutions between 1.7 A and 2.1 A in four different forms: (i) apo form, (ii) ternary complex with the nonhydrolyzable ATP analog AMPPNP and cofactor Ca(2+), (iii) quaternary complex with Ca(2+) and bound products AMP and phosphate, and (iv) binary product complex with AMP only. Adenylyl Imidodiphosphate 242-248 ectonucleoside triphosphate diphosphohydrolase 2 Rattus norvegicus 79-87 17963730-3 2007 On MT binding and in the presence of nucleotides ADP and AMPPNP, the spin labels on L11, particularly at A252C and L249C, significantly decreased the fraction of the slow component. Adenylyl Imidodiphosphate 57-63 immunoglobulin kappa variable 1-6 Homo sapiens 84-87 19332621-12 2009 Finally, we show that MgAMP-PNP exerts its effects on CFTR gating via a similar mechanism as MgPPi. Adenylyl Imidodiphosphate 22-31 CF transmembrane conductance regulator Homo sapiens 54-58 19135893-2 2009 We have determined the X-ray crystal structure of the NOD catalytic domain in the ADP- and AMPPNP-bound states. Adenylyl Imidodiphosphate 91-97 no distributive disjunction Drosophila melanogaster 54-57 19135893-5 2009 Thermodynamic studies show that NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including AMPPNP, are weakened. Adenylyl Imidodiphosphate 135-141 no distributive disjunction Drosophila melanogaster 32-35 18984583-4 2009 Here we report the crystal structure of the non-liganded form of Lyn kinase domain, as well as in complex with three different inhibitors: the ATP analogue AMP-PNP; the pan Src kinase inhibitor PP2; and the BCR-Abl/Src-family inhibitor Dasatinib. Adenylyl Imidodiphosphate 156-163 LYN proto-oncogene, Src family tyrosine kinase Homo sapiens 65-68 18725455-6 2008 The structure of BC bound to AMPPNP and the two catalytically essential magnesium ions resolves inconsistencies between the kinetics of active-site BC mutants and previously reported BC structures. Adenylyl Imidodiphosphate 29-35 methylcrotonyl-CoA carboxylase subunit 2 Homo sapiens 17-19 18725455-6 2008 The structure of BC bound to AMPPNP and the two catalytically essential magnesium ions resolves inconsistencies between the kinetics of active-site BC mutants and previously reported BC structures. Adenylyl Imidodiphosphate 29-35 methylcrotonyl-CoA carboxylase subunit 2 Homo sapiens 148-150 18725455-6 2008 The structure of BC bound to AMPPNP and the two catalytically essential magnesium ions resolves inconsistencies between the kinetics of active-site BC mutants and previously reported BC structures. Adenylyl Imidodiphosphate 29-35 methylcrotonyl-CoA carboxylase subunit 2 Homo sapiens 148-150 18387944-2 2008 Here, we present the crystal structure of PDHK2 bound to the inner lipoyl-bearing domain of dihydrolipoamide transacetylase (L2) determined with or without bound adenylyl imidodiphosphate. Adenylyl Imidodiphosphate 162-187 pyruvate dehydrogenase kinase 2 Homo sapiens 42-47 17925457-8 2008 Perfusion of ADP or control pipette solution had no effect, whereas perfusion of ATP or AMP-PNP, a nonhydrolyzable analog of ATP, significantly inhibited TRPC5 currents. Adenylyl Imidodiphosphate 88-95 transient receptor potential cation channel subfamily C member 5 Homo sapiens 154-159 17965184-2 2007 We report here the 1.9 A crystal structure of the catalytic domain of inactive human SGK1 in complex with AMP-PNP. Adenylyl Imidodiphosphate 106-113 serum/glucocorticoid regulated kinase 1 Homo sapiens 85-89 17936703-4 2007 Here, we report the 2.4 A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP. Adenylyl Imidodiphosphate 79-85 heat shock protein 90 beta family member 1 Homo sapiens 57-62 18194602-5 2007 LY294002, a specific inhibitor of PI-3K, effectively blocked Akt phosphorylation induced by AMP-PNP. Adenylyl Imidodiphosphate 92-99 AKT serine/threonine kinase 1 Homo sapiens 61-64 17461553-4 2007 We determined the crystal structures of the T210V mutant of the kinase domain of human Plk1 complexed with the nonhydrolyzable ATP analogue adenylylimidodiphosphate (AMPPNP) or the pyrrolo-pyrazole inhibitor PHA-680626 at 2.4 and 2.1 A resolution, respectively. Adenylyl Imidodiphosphate 140-164 polo like kinase 1 Homo sapiens 87-91 17724204-5 2007 This functional inhibition of Cx43 cell-to-cell dye transfer was sustained in the presence of the nonhydrolyzable ATP analogue AMP-PNP (adenyl-5"-yl imidophosphate), the ectonucleotidase inhibitor ARL 67156, or the protein phosphatase inhibitor okadaic acid. Adenylyl Imidodiphosphate 127-134 gap junction protein alpha 1 Homo sapiens 30-34 17461553-4 2007 We determined the crystal structures of the T210V mutant of the kinase domain of human Plk1 complexed with the nonhydrolyzable ATP analogue adenylylimidodiphosphate (AMPPNP) or the pyrrolo-pyrazole inhibitor PHA-680626 at 2.4 and 2.1 A resolution, respectively. Adenylyl Imidodiphosphate 166-172 polo like kinase 1 Homo sapiens 87-91 17157262-2 2007 We studied binding of ATP and of the ATP analogs adenosine 5"-(beta,gamma-methylene)triphosphate (AMPCP) and beta,gamma-imidoadenosine 5"-triphosphate (AMPPNP) to the Ca(2+)-ATPase of the sarcoplasmic reticulum membrane (SERCA1a) with time-resolved infrared spectroscopy. Adenylyl Imidodiphosphate 152-158 dynein axonemal heavy chain 8 Homo sapiens 174-180 17260965-4 2007 Non-phosphorylated MEK1 (npMEK1) has a high affinity for both AMP-PNP and ADP (Kd approximately 2microM). Adenylyl Imidodiphosphate 62-69 mitogen-activated protein kinase kinase 1 Homo sapiens 19-23 17244533-2 2007 Here we present the electron cryomicroscopy reconstruction of an ATP-activated ClpB trap mutant, along with reconstructions of ClpB in the AMPPNP, ADP, and in the nucleotide-free state. Adenylyl Imidodiphosphate 139-145 caseinolytic mitochondrial matrix peptidase chaperone subunit B Homo sapiens 127-131 17159905-3 2007 The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Adenylyl Imidodiphosphate 99-105 UPF1 RNA helicase and ATPase Homo sapiens 53-58 15808862-4 2005 While the apo Pim1 structure is nearly identical with that reported recently, the structure of AMPPNP bound to Pim1 is significantly different. Adenylyl Imidodiphosphate 95-101 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 111-115 16354672-3 2006 Here, we present the NMR structure of the AMP-PNP-bound nucleotide binding domain KdpBN of the Escherichia coli Kdp-ATPase at high resolution. Adenylyl Imidodiphosphate 42-49 ATPase Escherichia coli 116-122 16403413-5 2006 We demonstrate that human p23 interacts with Hsp90 in both the absence and presence of nucleotide with a higher affinity in the presence of the ATP analogue AMP-PNP. Adenylyl Imidodiphosphate 157-164 prostaglandin E synthase 3 Homo sapiens 26-29 16403413-5 2006 We demonstrate that human p23 interacts with Hsp90 in both the absence and presence of nucleotide with a higher affinity in the presence of the ATP analogue AMP-PNP. Adenylyl Imidodiphosphate 157-164 heat shock protein 90 alpha family class A member 1 Homo sapiens 45-50 16361109-4 2006 We have calculated helically averaged 3D maps of microtubules decorated with ZEN-4 motor domain in the presence of AMP-PNP, ADP, ADP-AlF(4)(-), and nucleotide-free conditions. Adenylyl Imidodiphosphate 115-122 Kinesin-like protein Caenorhabditis elegans 77-82 16227208-7 2005 We have solved the crystal structure of Pim-1 bound to a high affinity peptide substrate in complexes with either the ATP analog AMP-PNP or the bisindolylmaleimide kinase inhibitor 2-[1-(3-dimethylaminopropyl)-1H-indol-3-yl]-3-(1H-indol-3-yl)maleimide HCl. Adenylyl Imidodiphosphate 129-136 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 40-45 16183882-7 2005 The on-rate of venom binding for intraburst block could be modulated by changing CFTR activity with vanadate or adenylyl-imidodiphosphate, or by introducing the Walker A mutation K1250A. Adenylyl Imidodiphosphate 112-137 cystic fibrosis transmembrane conductance regulator L homeolog Xenopus laevis 81-85 16262696-2 2005 Because the presence of ATP or adenylylimidodiphosphate reduces atrial natriuretic peptide (ANP) binding and is required for maximal guanylyl cyclase activity, a direct interaction of ATP with the receptor KHD domain is plausible. Adenylyl Imidodiphosphate 31-55 natriuretic peptide A Homo sapiens 64-90 16262696-2 2005 Because the presence of ATP or adenylylimidodiphosphate reduces atrial natriuretic peptide (ANP) binding and is required for maximal guanylyl cyclase activity, a direct interaction of ATP with the receptor KHD domain is plausible. Adenylyl Imidodiphosphate 31-55 natriuretic peptide A Homo sapiens 92-95 17101799-4 2007 Wild-type Hsp90 bound Sti1 in a nucleotide-independent manner, while Sba1 and Cpr6 specifically and independently interacted with Hsp90 in the presence of the nonhydrolyzable analog of ATP, AMP-PNP. Adenylyl Imidodiphosphate 190-197 Hsp90 cochaperone SBA1 Saccharomyces cerevisiae S288C 69-73 17101799-4 2007 Wild-type Hsp90 bound Sti1 in a nucleotide-independent manner, while Sba1 and Cpr6 specifically and independently interacted with Hsp90 in the presence of the nonhydrolyzable analog of ATP, AMP-PNP. Adenylyl Imidodiphosphate 190-197 peptidylprolyl isomerase CPR6 Saccharomyces cerevisiae S288C 78-82 17101799-4 2007 Wild-type Hsp90 bound Sti1 in a nucleotide-independent manner, while Sba1 and Cpr6 specifically and independently interacted with Hsp90 in the presence of the nonhydrolyzable analog of ATP, AMP-PNP. Adenylyl Imidodiphosphate 190-197 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 130-135 16115868-5 2005 Here we report the x-ray structure of Gal1p in complex with alpha-d-galactose and Mg-adenosine 5"-(beta,gamma-imido)triphosphate (AMPPNP) determined to 2.4 Angstrom resolution. Adenylyl Imidodiphosphate 130-136 galactokinase Saccharomyces cerevisiae S288C 38-43 16185715-5 2005 In contrast, higher protection from exchange by AMP-PNP was observed in active ERK2 compared to inactive ERK2, in a region corresponding to the conserved DFG motif, which is located in the C-terminal lobe and coordinates Mg2+ at the catalytic site. Adenylyl Imidodiphosphate 48-55 mitogen-activated protein kinase 1 Homo sapiens 79-83 16185715-5 2005 In contrast, higher protection from exchange by AMP-PNP was observed in active ERK2 compared to inactive ERK2, in a region corresponding to the conserved DFG motif, which is located in the C-terminal lobe and coordinates Mg2+ at the catalytic site. Adenylyl Imidodiphosphate 48-55 mitogen-activated protein kinase 1 Homo sapiens 105-109 16185715-6 2005 Thus, AMP-PNP binding simultaneously protects residues within the N and C terminus in the active form of ERK2, but not the inactive form. Adenylyl Imidodiphosphate 6-13 mitogen-activated protein kinase 1 Homo sapiens 105-109 15964839-4 2005 Crystal structures of the GCN2 protein kinase domain have been determined for wild-type and R794G mutant forms in the apo state and bound to ATP/AMPPNP. Adenylyl Imidodiphosphate 145-151 eukaryotic translation initiation factor 2 alpha kinase 4 Homo sapiens 26-30 15590630-4 2005 Here we report the three-dimensional architecture of human galactokinase with bound alpha-D-galactose and Mg-AMPPNP. Adenylyl Imidodiphosphate 106-115 galactokinase 1 Homo sapiens 59-72 15657297-6 2005 CFTR channel inhibition was not obviously dependent on phosphorylation state but was markedly slowed when channels were first "locked open" by a poorly hydrolyzable ATP analogue (AMP-PNP). Adenylyl Imidodiphosphate 179-186 CF transmembrane conductance regulator Homo sapiens 0-4 15525646-4 2005 We have determined the crystal structures of apo Pim-1 kinase and its AMP-PNP (5"-adenylyl-beta,gamma-imidodiphosphate) complex to 2.1-angstroms resolutions. Adenylyl Imidodiphosphate 70-77 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 49-54 15525646-8 2005 3) The binding mode of AMP-PNP to Pim-1 kinase is unique and does not involve a critical hinge region hydrogen bond interaction. Adenylyl Imidodiphosphate 23-30 Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens 34-39 15557326-9 2005 In membranes expressing the ABCG2-K86M mutant, ATP, ADP, and AMP-PNP decreased, whereas Ko143 increased 5D3 binding. Adenylyl Imidodiphosphate 61-68 ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens 28-33 15364914-5 2004 8-Azido[alpha-32P]ATP binds to MRP4 (concentration for half-maximal binding approximately 3 microm) and is displaced by ATP or by its non-hydrolyzable analog AMPPNP (concentrations for half-maximal inhibition of 13.3 and 308 microm). Adenylyl Imidodiphosphate 158-164 ATP binding cassette subfamily C member 4 Homo sapiens 31-35 15525689-8 2004 CaM added with adenosine 5"-(beta,gamma-imido)triphosphate (AMP-PNP) also induced channel activity, although with much lower potency and shorter duration. Adenylyl Imidodiphosphate 60-67 calmodulin-3 Cavia porcellus 0-3 15698563-3 2005 Small-angle X-ray scattering (SAXS) measurements of p97 in the presence of AMP-PNP (ATP state), ADP-AlF(x) (hydrolysis transition state), ADP, or no nucleotide reveal major changes in the positions of the N domains with respect to the hexameric ring during the ATP hydrolysis cycle. Adenylyl Imidodiphosphate 75-82 valosin containing protein Homo sapiens 52-55 15579537-6 2004 The activation process of I(TRPC6) or its acceleration by Ca2+(o) probably involves phosphorylation by calmodulin (CaM)-dependent kinase II (CaMKII), as pretreatment with calmidazolium (3 microM), coexpression of Ca2+-insensitive mutant CaM, and intracellular perfusion of the non-hydrolysable ATP analogue AMP-PNP and a CaMKII-specific inhibitory peptide all effectively prevented channel activation. Adenylyl Imidodiphosphate 307-314 transient receptor potential cation channel subfamily C member 6 Homo sapiens 28-33 15249227-17 2004 Use of the non-hydrolyzable ATP analogue AMP-PNP yielded similar results to those observed with ATP, suggesting that ATP binding rather than ATP hydrolysis is required for the protein conformation modifying reaction of oligomeric Aip2p/Dld2p. Adenylyl Imidodiphosphate 41-48 D-lactate dehydrogenase Saccharomyces cerevisiae S288C 230-235 15351742-18 2004 In the presence of 1mM ATP or AMP-PNP, oligomeric Aip2p/Dld2p bound to all substrates so far examined, and modified the conformation of actin, DNase I, the mature form of invertase, prepro-alpha-factor, pro-alpha-factor, and mitochondrial superoxide dismutase, as determined by the trypsin susceptibility assay. Adenylyl Imidodiphosphate 30-37 D-lactate dehydrogenase Saccharomyces cerevisiae S288C 50-55 15351742-18 2004 In the presence of 1mM ATP or AMP-PNP, oligomeric Aip2p/Dld2p bound to all substrates so far examined, and modified the conformation of actin, DNase I, the mature form of invertase, prepro-alpha-factor, pro-alpha-factor, and mitochondrial superoxide dismutase, as determined by the trypsin susceptibility assay. Adenylyl Imidodiphosphate 30-37 D-lactate dehydrogenase Saccharomyces cerevisiae S288C 56-61 15465351-3 2004 Binding order and stoichiometry of cGMP, the non-hydrolysable ATP analog beta,gamma-imidoadenosine 5"-triphosphate (AMPPNP) and Mn2+ for PKG were characterized as model for the active PKG-cGMP-ATP/Mg2+ complex. Adenylyl Imidodiphosphate 116-122 protein kinase cGMP-dependent 1 Homo sapiens 137-140 15465351-4 2004 Already in the absence of cGMP, a noncovalent complex between PKG and two molecules of AMPPNP could be observed by ESI-TOF-MS. Adenylyl Imidodiphosphate 87-93 protein kinase cGMP-dependent 1 Homo sapiens 62-65 15465351-5 2004 Binding of AMPPNP to PKG was strongly enhanced by the addition of MnCl2 to the spray solution. Adenylyl Imidodiphosphate 11-17 protein kinase cGMP-dependent 1 Homo sapiens 21-24 15465351-6 2004 This is in agreement with binding of AMPPNP/Mn2+ in the ATP binding pocket of PKG since all protein kinases require a metal ion to accompany ATP in the ATP-binding pocket for proper positioning of the beta and gamma phosphates. Adenylyl Imidodiphosphate 37-43 protein kinase cGMP-dependent 1 Homo sapiens 78-81 15249227-17 2004 Use of the non-hydrolyzable ATP analogue AMP-PNP yielded similar results to those observed with ATP, suggesting that ATP binding rather than ATP hydrolysis is required for the protein conformation modifying reaction of oligomeric Aip2p/Dld2p. Adenylyl Imidodiphosphate 41-48 D-lactate dehydrogenase Saccharomyces cerevisiae S288C 236-241 15286375-3 2004 We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). Adenylyl Imidodiphosphate 93-118 kinesin family member 1A Homo sapiens 50-55 15286375-3 2004 We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes). Adenylyl Imidodiphosphate 120-127 kinesin family member 1A Homo sapiens 50-55 14758478-6 2004 ATP, ADP, AMP and AMP-PNP all quickly and reversibly inhibited TRPM4 with IC(50) values between 2 and 19 microM (at +100 mV). Adenylyl Imidodiphosphate 18-25 transient receptor potential cation channel subfamily M member 4 Homo sapiens 63-68 14993667-2 2004 Here, binary complex structures of full-length TPK I/GSK3 beta with the ATP analogues ADP and AMPPNP solved by the X-ray diffraction method at 2.1 and 1.8 A resolution, respectively, are reported. Adenylyl Imidodiphosphate 94-100 glycogen synthase kinase 3 beta Homo sapiens 53-62 14985083-7 2004 The anterograde and retrograde movements of GFP-PrPC were blocked by a kinesin family inhibitor (AMP-PNP) and a dynein family inhibitor (vanadate), respectively. Adenylyl Imidodiphosphate 97-104 prion protein Mus musculus 44-52 12964162-0 2003 NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol. Adenylyl Imidodiphosphate 93-100 heat shock protein 90 alpha family class A member 1 Homo sapiens 66-71 14596595-7 2003 The affinities of several nucleotides (ATP, ADP, AMP, adenosine, and AMPPNP) to Sky1p and the prototype kinase, cAMP-dependent protein kinase, were compared in the absence and presence of the metal activator, Mg(2+), using a fluorescence-based displacement assay. Adenylyl Imidodiphosphate 69-75 serine/threonine protein kinase SKY1 Saccharomyces cerevisiae S288C 80-85 12816949-9 2003 ATP and ADP decreased the affinity of PDK2 for E2 by 3-5-fold and adenosine 5"-(beta,gamma-imino)triphosphate or phosphorylation of E1 similarly reduced PDK2 binding to E2.E1. Adenylyl Imidodiphosphate 66-109 pyruvate dehydrogenase kinase 2 Homo sapiens 153-157 14556639-2 2003 Full-length hPNK was subjected to sedimentation and spectroscopic analyses in association with its ligands, a 20-mer oligonucleotide, ATP, and AMP-PNP (a nonhydrolyzable analogue of ATP). Adenylyl Imidodiphosphate 143-150 polynucleotide kinase 3'-phosphatase Homo sapiens 12-16 14556639-10 2003 Furthermore, the nonphosphorylated oligonucleotide was able to bind to hPNK in the presence of AMP-PNP with a K(d) value of 2.5 microM, confirming the formation of a ternary complex. Adenylyl Imidodiphosphate 95-102 polynucleotide kinase 3'-phosphatase Homo sapiens 71-75 12875848-3 2003 Comparison of these structures with that of the MgAMPPNP-NAG complex allows to delineate three successive steps during phosphoryl transfer: at the beginning, when the attacking and leaving O atoms and the P atom are imperfectly aligned and the distance between the attacking O atom and the P atom is 2.8A; midway, at the bipyramidal intermediate, with nearly perfect alignment and a distance of 2.3A; and, when the transfer is completed. Adenylyl Imidodiphosphate 48-56 N-acetyl-alpha-glucosaminidase Homo sapiens 57-60 12799385-4 2003 Under certain conditions, ATP is two times more effective than adenylyl imidodiphosphate (AMP-PNP), a hydrolysis-resistant ATP analog; however, this study mainly used AMP-PNP to focus on the role of adenine nucleotide binding to retGC. Adenylyl Imidodiphosphate 63-88 guanylate cyclase 2D, retinal Homo sapiens 229-234 12799385-4 2003 Under certain conditions, ATP is two times more effective than adenylyl imidodiphosphate (AMP-PNP), a hydrolysis-resistant ATP analog; however, this study mainly used AMP-PNP to focus on the role of adenine nucleotide binding to retGC. Adenylyl Imidodiphosphate 90-97 guanylate cyclase 2D, retinal Homo sapiens 229-234 12799385-5 2003 When photoreceptor outer segment homogenates are preincubated with AMP-PNP (EC50 = 0.65 +/- 0.20 mM), GCAP2 enhanced the retGC activity 10-13 times over the control rate. Adenylyl Imidodiphosphate 67-74 guanylate cyclase activator 1B Homo sapiens 102-107 12799385-5 2003 When photoreceptor outer segment homogenates are preincubated with AMP-PNP (EC50 = 0.65 +/- 0.20 mM), GCAP2 enhanced the retGC activity 10-13 times over the control rate. Adenylyl Imidodiphosphate 67-74 guanylate cyclase 2D, retinal Homo sapiens 121-126 11882671-5 2002 Continuous activity of hClC-4 was sustained to different degrees by internal nucleotides: ATP approximately ATPgammaS >> AMP-PNP approximate GTP > ADP. Adenylyl Imidodiphosphate 127-134 chloride voltage-gated channel 4 Homo sapiens 23-29 12634057-2 2003 We present the cryo-electron microscopy three-dimensional reconstruction of endogenous p97 in an AMP-PNP bound state at 24 A resolution. Adenylyl Imidodiphosphate 97-104 melanotransferrin Homo sapiens 87-90 12657723-5 2003 Molecular dynamics and docking simulations, targeting the ATP binding site of aurora2 with adenylyl imidodiphosphate (AMP-PNP), staurosporine, and six small molecular S/T kinase inhibitors, identified active-site residues that interact with these inhibitors differentially. Adenylyl Imidodiphosphate 91-116 aurora kinase A Homo sapiens 78-85 12657723-5 2003 Molecular dynamics and docking simulations, targeting the ATP binding site of aurora2 with adenylyl imidodiphosphate (AMP-PNP), staurosporine, and six small molecular S/T kinase inhibitors, identified active-site residues that interact with these inhibitors differentially. Adenylyl Imidodiphosphate 118-125 aurora kinase A Homo sapiens 78-85 12657723-6 2003 The docked structures of the aurora2-AMP-PNP and aurora2-staurosporine complexes indicated that the adenine ring of AMP-PNP and the indolocarbazole moiety of staurosporine have similar positions and orientations and provided the basis for the docking of the other S/T kinase inhibitors. Adenylyl Imidodiphosphate 37-44 aurora kinase A Homo sapiens 29-36 12525166-6 2003 We show that with bound ADP.vanadate, which mimics the transition state between ATP and hydrolysis products, or with the ATP analogues AMP-PNP or ADP.BeF(x)() the myosin filaments are substantially ordered at higher temperatures but are reversibly disordered by cooling. Adenylyl Imidodiphosphate 135-142 myosin heavy chain 14 Homo sapiens 163-169 12467574-2 2002 We have determined structures of yeast glutathione synthase in two forms: unbound (2.3 A resolution) and bound to its substrate gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions (1.8 A resolution). Adenylyl Imidodiphosphate 167-174 glutathione synthase Saccharomyces cerevisiae S288C 39-59 12351849-0 2002 A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase. Adenylyl Imidodiphosphate 57-63 N-acetylglucosamine kinase Homo sapiens 147-174 12351849-0 2002 A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase. Adenylyl Imidodiphosphate 115-121 N-acetylglucosamine kinase Homo sapiens 147-174 11861646-8 2002 We have now characterized the interactions of the 8-azido-photoactive analogues of ATP, ADP, and 5"-adenyl-beta,gamma-imidodiphosphate (AMP-PNP) with the two domains of functional membrane-bound CFTR. Adenylyl Imidodiphosphate 136-143 CF transmembrane conductance regulator Homo sapiens 195-199 11888286-5 2002 AMPPNP inhibition assays and ATP/ADP binding assays provide binding constants for ATP and ADP to DbpA with and without RNA substrates. Adenylyl Imidodiphosphate 0-6 ATPase Escherichia coli 82-93 12736270-0 2003 Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP. Adenylyl Imidodiphosphate 32-38 heat shock protein family D (Hsp60) member 1 Homo sapiens 53-58 12736270-0 2003 Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP. Adenylyl Imidodiphosphate 32-38 hexokinase 1 Homo sapiens 60-70 12736270-4 2003 In ADP and AMPPNP, GroES bound quickly to GroEL but bound very slowly to the GroEL loaded with unfolded rhodanese or malate dehydrogenase. Adenylyl Imidodiphosphate 11-17 heat shock protein family E (Hsp10) member 1 Homo sapiens 19-24 12736270-6 2003 AMPPNP supported cis folding of malate dehydrogenase to some extent but not cis folding of rhodanese. Adenylyl Imidodiphosphate 0-6 malic enzyme 1 Homo sapiens 32-52 12736270-7 2003 In the absence of hexokinase, apparent cis folding of rhodanese and malate dehydrogenase was observed in ADP and AMPPNP. Adenylyl Imidodiphosphate 113-119 malic enzyme 1 Homo sapiens 68-88 12727866-5 2003 Interestingly, although ATP supports GSH flux through CFTR, this activity is enhanced in the presence of the non-hydrolyzable ATP analog AMP-PNP. Adenylyl Imidodiphosphate 137-144 CF transmembrane conductance regulator Homo sapiens 54-58 12614151-3 2003 To gain further understanding of the determinants for efficient conversion by the enzyme thymidylate kinase (TMPK) of clinically important thymidine monophosphate analogues to the corresponding diphosphates, we solved the crystal structures of the enzyme, with either ADP or the ATP analogue AppNHp at the phosphoryl donor site, in complex with TMP, AZTMP (previous work), NH2TMP, d4TMP, ddTMP, and FLTMP (this work) at the phosphoryl acceptor site. Adenylyl Imidodiphosphate 292-298 deoxythymidylate kinase Homo sapiens 109-113 12508051-6 2003 Poorly hydrolyzable nucleotide analogs, MgAMPPNP, MgAMPPCP, and MgATPgammaS, could open CFTR channels, but only to a maximal rate of opening approximately 20-fold lower than attained by MgATP acting on the same channels. Adenylyl Imidodiphosphate 40-48 cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) Xenopus laevis 88-92 12135363-9 2002 Together with the small change in the K(i) of Pd1 at increasing S3 concentrations, the Pd1 inhibition data support the existence of an isomechanism in Lon catalyzing the hydrolysis of S3 in the presence of ATP or AMPPNP. Adenylyl Imidodiphosphate 213-219 putative ATP-dependent Lon protease Escherichia coli 151-154 10512721-7 1999 When GroES was present, ATP as well as ADP and AMP-PNP were effective in reducing the affinity between GroEL and the refolding intermediate of alpha-lactalbumin. Adenylyl Imidodiphosphate 47-54 heat shock protein family E (Hsp10) member 1 Homo sapiens 5-10 11790804-8 2002 Peptide (AIP) and lipophilic (KN-62) protein kinase inhibitors prevented the Ca(2+)/CaM-induced changes in channel gating without altering basal Ca(v)3.2 channel activity (27 nM free Ca(2+)) as did replacing pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable analogue. Adenylyl Imidodiphosphate 225-250 calmodulin 3 Homo sapiens 84-87 11790804-8 2002 Peptide (AIP) and lipophilic (KN-62) protein kinase inhibitors prevented the Ca(2+)/CaM-induced changes in channel gating without altering basal Ca(v)3.2 channel activity (27 nM free Ca(2+)) as did replacing pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable analogue. Adenylyl Imidodiphosphate 252-259 calmodulin 3 Homo sapiens 84-87 11752435-6 2001 The Arp2/3 complex bound to ADP or the nonhydrolyzable ATP analogue AMP-PNP cannot nucleate actin filaments, but addition of the phosphate analogue BeF(3) partially restores activity to the ADP-Arp2/3 complex. Adenylyl Imidodiphosphate 68-75 actin related protein 2 Homo sapiens 4-8 11551925-8 2001 In addition, Dmc1 catalyzes strand assimilation of ssDNA oligonucleotides into homologous supercoiled duplex DNA in a reaction promoted by ATP or the non-hydrolyzable ATP analogue AMP-PNP. Adenylyl Imidodiphosphate 180-187 recombinase DMC1 Saccharomyces cerevisiae S288C 13-17 11580247-11 2001 ATP, AMP-PNP, and ADP bound forms of FliI within the FliH/FliI complex regained sensitivity to clostripain cleavage. Adenylyl Imidodiphosphate 5-12 FLII actin remodeling protein Homo sapiens 37-41 11580247-11 2001 ATP, AMP-PNP, and ADP bound forms of FliI within the FliH/FliI complex regained sensitivity to clostripain cleavage. Adenylyl Imidodiphosphate 5-12 FLII actin remodeling protein Homo sapiens 58-62 11580247-12 2001 Also, the sensitivity of the two FliI(CL38) cleavage sites was much greater in the ATP and AMP-PNP bound forms than in either the ADP bound form or nucleotide-free FliI. Adenylyl Imidodiphosphate 91-98 FLII actin remodeling protein Homo sapiens 33-37 11483510-3 2001 Here we find that upon ATP binding, mimicked by the non-hydrolysable analog AMP-PNP (5"-adenylyl-imido-diphosphate), to both CCT-alpha-actin and CCT- beta-tubulin complexes, the chaperonin component undergoes concerted movements of the apical domains, resulting in the cavity being closed off by the helical protrusions of the eight apical domains. Adenylyl Imidodiphosphate 76-83 t-complex 1 Homo sapiens 125-134 11483510-3 2001 Here we find that upon ATP binding, mimicked by the non-hydrolysable analog AMP-PNP (5"-adenylyl-imido-diphosphate), to both CCT-alpha-actin and CCT- beta-tubulin complexes, the chaperonin component undergoes concerted movements of the apical domains, resulting in the cavity being closed off by the helical protrusions of the eight apical domains. Adenylyl Imidodiphosphate 76-83 chaperonin containing TCP1 subunit 2 Homo sapiens 145-154 11483510-5 2001 Docking of the AMP-PNP-CCT-bound conformations of alpha-actin and beta-tubulin to their respective native atomic structures suggests that both proteins have progressed towards their native states. Adenylyl Imidodiphosphate 15-22 CCT Homo sapiens 23-26 10986338-6 2000 The facilitation of acetylcholine release by beta, gamma-imido ATP (30 microM) was also prevented by the nicotinic acetylcholine receptor antagonist, D-tubocurarine (1 microM) and the facilitatory effect (40%) of the nicotinic acetylcholine receptor agonist, 1,1-dimethyl-4-phenylpiperazinium (1 microM) was abolished by PPADS (10 microM). Adenylyl Imidodiphosphate 45-66 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 105-137 10986338-6 2000 The facilitation of acetylcholine release by beta, gamma-imido ATP (30 microM) was also prevented by the nicotinic acetylcholine receptor antagonist, D-tubocurarine (1 microM) and the facilitatory effect (40%) of the nicotinic acetylcholine receptor agonist, 1,1-dimethyl-4-phenylpiperazinium (1 microM) was abolished by PPADS (10 microM). Adenylyl Imidodiphosphate 45-66 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 217-249 10962022-7 2000 Split channels with no R domain (from coexpression of CFTR segments 1-633 and 837-1480) were highly active without phosphorylation, but otherwise displayed the characteristics of channels cut after the R domain, including higher apparent ATP affinity, and less tight binding of AMPPNP at the locking site, than for WT. Adenylyl Imidodiphosphate 278-284 cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) Xenopus laevis 54-58 10919864-12 2000 In excised-patch recordings, all functional severed CFTR channels displayed the hallmark characteristics of CFTR, including the requirement of phosphorylation and exposure to MgATP for gating, ability to be locked open by pyrophosphate or AMP-PNP, small single channel conductances, and high apparent affinity of channel opening by MgATP. Adenylyl Imidodiphosphate 239-246 CF transmembrane conductance regulator Homo sapiens 52-56 10919864-12 2000 In excised-patch recordings, all functional severed CFTR channels displayed the hallmark characteristics of CFTR, including the requirement of phosphorylation and exposure to MgATP for gating, ability to be locked open by pyrophosphate or AMP-PNP, small single channel conductances, and high apparent affinity of channel opening by MgATP. Adenylyl Imidodiphosphate 239-246 CF transmembrane conductance regulator Homo sapiens 108-112 10574795-8 1999 The molecular symmetry brings the two bound AMP-PNP molecules, at the centre of two extended surface regions, to a common side of the dimeric hexokinase I molecule. Adenylyl Imidodiphosphate 44-51 hexokinase 1 Homo sapiens 142-154 10574795-9 1999 CONCLUSIONS: The binding of AMP-PNP to a protein site separated from the catalytic centre of human hexokinase I can be related to the role played by some nucleotides in dissociating the enzyme from the mitochondrial membrane, and helps in defining the molecular regions of hexokinase I that are expected to be in contact with the mitochondrion. Adenylyl Imidodiphosphate 28-35 hexokinase 1 Homo sapiens 99-111 10574795-9 1999 CONCLUSIONS: The binding of AMP-PNP to a protein site separated from the catalytic centre of human hexokinase I can be related to the role played by some nucleotides in dissociating the enzyme from the mitochondrial membrane, and helps in defining the molecular regions of hexokinase I that are expected to be in contact with the mitochondrion. Adenylyl Imidodiphosphate 28-35 hexokinase 1 Homo sapiens 273-285 11564753-3 2001 Eg5 dynamics are frozen by adenylimidodiphosphate. Adenylyl Imidodiphosphate 27-49 kinesin family member 11 S homeolog Xenopus laevis 0-3 11665840-4 2001 The ATP-analogue adenylylimidodiphosphate (AMP-PNP) slightly potentiated the ANP effect on GC activity in broken cell preparations and significantly reduced GC sensitivity to isatin. Adenylyl Imidodiphosphate 17-41 natriuretic peptide A Rattus norvegicus 77-80 11665840-4 2001 The ATP-analogue adenylylimidodiphosphate (AMP-PNP) slightly potentiated the ANP effect on GC activity in broken cell preparations and significantly reduced GC sensitivity to isatin. Adenylyl Imidodiphosphate 43-50 natriuretic peptide A Rattus norvegicus 77-80 11101309-7 2000 P-glycoprotein fluorescence was highly quenched on binding of fluorescent nucleotides, and moderately quenched by ATP, ADP, and AMP-PNP, suggesting that the site for nucleotide binding is located relatively close to tryptophan residues. Adenylyl Imidodiphosphate 128-135 ATP binding cassette subfamily B member 1 Homo sapiens 0-14 10944121-3 2000 C-terminal truncation mutants lacking inherent dimerization displayed reduced ATPase activity, but dimerized in the presence of 5"-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted association of N-termini in intact Hsp90 dimers was demonstrated. Adenylyl Imidodiphosphate 170-177 heat shock protein 90 alpha family class A member 1 Homo sapiens 223-228 10512721-7 1999 When GroES was present, ATP as well as ADP and AMP-PNP were effective in reducing the affinity between GroEL and the refolding intermediate of alpha-lactalbumin. Adenylyl Imidodiphosphate 47-54 heat shock protein family D (Hsp60) member 1 Homo sapiens 103-108 10512721-7 1999 When GroES was present, ATP as well as ADP and AMP-PNP were effective in reducing the affinity between GroEL and the refolding intermediate of alpha-lactalbumin. Adenylyl Imidodiphosphate 47-54 lactalbumin alpha Homo sapiens 143-160 10512721-8 1999 The affinity at a saturating concentration of ADP or AMP-PNP was about ten times lower than with GroEL alone. Adenylyl Imidodiphosphate 53-60 heat shock protein family D (Hsp60) member 1 Homo sapiens 97-102 10387103-8 1999 However, the binding of dCyd to dCK in the presence of ATP or UTP was accompanied by a 1.5- or 3-fold higher quenching amplitude as compared with dCyd alone or in the presence of AMP-PNP. Adenylyl Imidodiphosphate 179-186 Calcium/calmodulin-dependent protein kinase II Drosophila melanogaster 32-35 10463939-4 1999 Whereas phosphorylation of the IRK by ATP is inhibited by the nonhydrolyzable competitor adenylyl-imidodiphosphate, phosphorylation by PCr is enhanced. Adenylyl Imidodiphosphate 89-114 potassium inwardly rectifying channel subfamily J member 12 Homo sapiens 31-34 10446215-5 1999 Here we report that the membrane-associated form of GAD (MGAD) is greatly activated by ATP, whereas adenosine 5"-[beta,gamma-imido]triphosphate (AMP-PNP), a non-hydrolyzable ATP analog, has no effect on MGAD activity. Adenylyl Imidodiphosphate 145-152 glutamate decarboxylase 1 Homo sapiens 52-55 10398692-0 1999 Dual effects of ADP and adenylylimidodiphosphate on CFTR channel kinetics show binding to two different nucleotide binding sites. Adenylyl Imidodiphosphate 24-48 CF transmembrane conductance regulator Homo sapiens 52-56 10398692-7 1999 The results present the first direct evidence that AMP-PNP binds to two sites on the CFTR. Adenylyl Imidodiphosphate 51-58 CF transmembrane conductance regulator Homo sapiens 85-89 10387103-2 1999 In this study, stopped-flow experiments were used to monitor intrinsic fluorescence changes induced upon binding of various phosphate donors (ATP, UTP, and the nonhydrolyzable analogue AMP-PNP) and the acceptor dCyd to recombinant dCK. Adenylyl Imidodiphosphate 185-192 Calcium/calmodulin-dependent protein kinase II Drosophila melanogaster 231-234 10387103-7 1999 Whereas the kinetics of the binding of ATP, UTP, and AMP-PNP to dCK showed some differences, UTP exhibiting the tightest binding, no significant differences were observed for the binding of dCyd to dCK in the presence or absence of phosphate donors. Adenylyl Imidodiphosphate 53-60 Calcium/calmodulin-dependent protein kinase II Drosophila melanogaster 64-67 10395457-6 1999 When ADP, ATP, or AMP-PNP were added to a solution of GroEL and Mg2+, C138 incorporated approximately 0.8 labels, while C458 incorporated approximately 0.1 labels. Adenylyl Imidodiphosphate 18-25 heat shock protein family D (Hsp60) member 1 Homo sapiens 54-59 10359598-7 1999 The nonhydrolyzable ATP analogue adenosine 5"-(beta,gamma-imino)-triphosphate was half as effective as ATP in stimulating the wild-type receptor but was equally as potent in stimulating NPR-A-6E, suggesting that ATP is required to keep the wild-type but not 6E variant phosphorylated. Adenylyl Imidodiphosphate 33-77 natriuretic peptide receptor 1 Homo sapiens 186-191 10404594-5 1999 RESULTS: We report here the high-resolution crystal structures of an activated Lck kinase domain in complex with three structurally distinct ATP-competitive inhibitors: AMP-PNP (a non-selective, non-hydrolyzable ATP analog); staurosporine (a potent but non-selective protein kinase inhibitor); and PP2 (a potent Src family selective protein tyrosine kinase inhibitor). Adenylyl Imidodiphosphate 169-176 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 79-82 10404594-5 1999 RESULTS: We report here the high-resolution crystal structures of an activated Lck kinase domain in complex with three structurally distinct ATP-competitive inhibitors: AMP-PNP (a non-selective, non-hydrolyzable ATP analog); staurosporine (a potent but non-selective protein kinase inhibitor); and PP2 (a potent Src family selective protein tyrosine kinase inhibitor). Adenylyl Imidodiphosphate 169-176 neuropeptide Y receptor Y6 (pseudogene) Homo sapiens 298-301 10404594-5 1999 RESULTS: We report here the high-resolution crystal structures of an activated Lck kinase domain in complex with three structurally distinct ATP-competitive inhibitors: AMP-PNP (a non-selective, non-hydrolyzable ATP analog); staurosporine (a potent but non-selective protein kinase inhibitor); and PP2 (a potent Src family selective protein tyrosine kinase inhibitor). Adenylyl Imidodiphosphate 169-176 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 312-315 10395457-6 1999 When ADP, ATP, or AMP-PNP were added to a solution of GroEL and Mg2+, C138 incorporated approximately 0.8 labels, while C458 incorporated approximately 0.1 labels. Adenylyl Imidodiphosphate 18-25 mucin 7, secreted Homo sapiens 64-67 9756927-3 1998 Binding of ATP or AMP-PNP (adenosine 5"-(beta, gamma-imino)triphosphate), but not ADP, or of a peptidic substrate induces depolymerization of FLAG-BiP.ent and stabilization of monomeric species. Adenylyl Imidodiphosphate 18-25 heat shock protein 5 Mus musculus 147-150 9914513-1 1999 The conformational properties of the molecular chaperone GroEL in the presence of ATP, its non-hydrolyzable analog 5"-adenylimidodiphosphate (AMP-PNP), and ADP have been analyzed by differential scanning calorimetry (DSC), Fourier-transform infra-red (FT-IR) and fluorescence spectroscopy. Adenylyl Imidodiphosphate 142-149 heat shock protein family D (Hsp60) member 1 Homo sapiens 57-62 9914513-4 1999 The similar sensitivity to K+ of the temperature range where activation of the GroEL ATPase activity, the low temperature endotherm, and the increase of the ANS fluorescence are abserved strongly indicates the existence of a conformational state of GroEL during ATP hydrolysis, different from that generated on ADP or AMP-PNP binding. Adenylyl Imidodiphosphate 318-325 heat shock protein family D (Hsp60) member 1 Homo sapiens 249-254 9756927-3 1998 Binding of ATP or AMP-PNP (adenosine 5"-(beta, gamma-imino)triphosphate), but not ADP, or of a peptidic substrate induces depolymerization of FLAG-BiP.ent and stabilization of monomeric species. Adenylyl Imidodiphosphate 27-71 heat shock protein 5 Mus musculus 147-150 9739089-5 1998 RESULTS: We report here the structure of unphosphorylated JNK3 in complex with adenylyl imidodiphosphate, an ATP analog. Adenylyl Imidodiphosphate 79-104 mitogen-activated protein kinase 10 Mus musculus 58-62 9760234-5 1998 We report here similar scattering experiments on the CaM.MLCK complex with the addition of substrates; a nonhydrolyzable analogue of adenosine-triphosphate, AMPPNP, and a peptide substrate for MLCK, a phosphorylation sequence from myosin regulatory light chain (pRLC). Adenylyl Imidodiphosphate 157-163 calmodulin 3 Homo sapiens 53-56 9760234-5 1998 We report here similar scattering experiments on the CaM.MLCK complex with the addition of substrates; a nonhydrolyzable analogue of adenosine-triphosphate, AMPPNP, and a peptide substrate for MLCK, a phosphorylation sequence from myosin regulatory light chain (pRLC). Adenylyl Imidodiphosphate 157-163 myosin light chain kinase Homo sapiens 57-61 9760234-9 1998 Finally, the kinase itself becomes more compact in the CaM.MLCK.pRLC.AMPPNP complex compared to the complex without substrates. Adenylyl Imidodiphosphate 69-75 calmodulin 3 Homo sapiens 55-58 9760234-9 1998 Finally, the kinase itself becomes more compact in the CaM.MLCK.pRLC.AMPPNP complex compared to the complex without substrates. Adenylyl Imidodiphosphate 69-75 myosin light chain kinase Homo sapiens 59-63 9724742-8 1998 Although IRP-1 activation is unaffected by addition of excess ATP or GTP to this in vitro system, it is negatively affected by the nonhydrolyzable nucleotide analogs adenylyl-imidodiphosphate and guanylyl-imidophosphate and completely blocked by ATP-gammaS and GTP-gammaS. Adenylyl Imidodiphosphate 166-191 aconitase 1 Homo sapiens 9-14 9632692-3 1998 When membranes from NIH 3T3 cells stably overexpressing GC-A were incubated with ATP, AMPPNP, or ATPgammaS, only ATPgammaS dramatically potentiated ANP-dependent cyclase activity. Adenylyl Imidodiphosphate 86-92 natriuretic peptide receptor 1 Mus musculus 56-60 9789567-5 1998 This tight binding of AMP-PNP presumably occurs at CFTR"s C-terminal nucleotide binding domain. Adenylyl Imidodiphosphate 22-29 CF transmembrane conductance regulator Homo sapiens 51-55 9632802-7 1998 The nonhydrolyzable analogs of ATP, adenosine-5"-O-(3-thiotriphosphate) (ATPgammaS) and adenyl-imidodiphosphate, each stabilized the primer recognition complex containing RFC and PCNA in the absence of p21. Adenylyl Imidodiphosphate 88-111 proliferating cell nuclear antigen Homo sapiens 179-183 9632802-7 1998 The nonhydrolyzable analogs of ATP, adenosine-5"-O-(3-thiotriphosphate) (ATPgammaS) and adenyl-imidodiphosphate, each stabilized the primer recognition complex containing RFC and PCNA in the absence of p21. Adenylyl Imidodiphosphate 88-111 cyclin dependent kinase inhibitor 1A Homo sapiens 202-205 9632755-5 1998 Using an in vitro assembly assay, purified Sba1(His6) bound to Hsp90 only in the presence of adenosine 5"-O-(3-thiotriphosphate) or adenyl-imidodiphosphate. Adenylyl Imidodiphosphate 132-155 Hsp90 cochaperone SBA1 Saccharomyces cerevisiae S288C 43-47 9632755-5 1998 Using an in vitro assembly assay, purified Sba1(His6) bound to Hsp90 only in the presence of adenosine 5"-O-(3-thiotriphosphate) or adenyl-imidodiphosphate. Adenylyl Imidodiphosphate 132-155 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase HIS6 Saccharomyces cerevisiae S288C 48-52 9632755-5 1998 Using an in vitro assembly assay, purified Sba1(His6) bound to Hsp90 only in the presence of adenosine 5"-O-(3-thiotriphosphate) or adenyl-imidodiphosphate. Adenylyl Imidodiphosphate 132-155 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 63-68 9538267-8 1998 Immunoprecipitation also revealed that the 18.1 kDa protein formed a complex with the 21.9 kDa protein and the 45 kDa protein with mHsp70; the latter complex was dissociated in an ATP- or ADP-dependent manner and the reaction was impeded by AMP-PNP or inorganic phosphate. Adenylyl Imidodiphosphate 241-248 heat shock protein 1B Mus musculus 131-137 9569250-1 1998 The gating cycle of CFTR (Cystic Fibrosis Transmembrane conductance Regulator) chloride channels requires ATP hydrolysis and can be interrupted by exposure to the nonhydrolyzable nucleotide AMP-PNP. Adenylyl Imidodiphosphate 190-197 CF transmembrane conductance regulator Homo sapiens 20-24 9569250-1 1998 The gating cycle of CFTR (Cystic Fibrosis Transmembrane conductance Regulator) chloride channels requires ATP hydrolysis and can be interrupted by exposure to the nonhydrolyzable nucleotide AMP-PNP. Adenylyl Imidodiphosphate 190-197 CF transmembrane conductance regulator Homo sapiens 26-77 9569250-3 1998 The rate of channel locking increased from 1.05 x 10(-3) sec-1 to 58.7 x 10(-3) sec-1 when AMP-PNP concentration was raised from 0.5 to 5 mM in the presence of 1 mM MgATP and 180 nM protein kinase A catalytic subunit (PKA). Adenylyl Imidodiphosphate 91-98 secretory blood group 1, pseudogene Homo sapiens 57-62 9569250-3 1998 The rate of channel locking increased from 1.05 x 10(-3) sec-1 to 58.7 x 10(-3) sec-1 when AMP-PNP concentration was raised from 0.5 to 5 mM in the presence of 1 mM MgATP and 180 nM protein kinase A catalytic subunit (PKA). Adenylyl Imidodiphosphate 91-98 secretory blood group 1, pseudogene Homo sapiens 80-85 9569250-3 1998 The rate of channel locking increased from 1.05 x 10(-3) sec-1 to 58.7 x 10(-3) sec-1 when AMP-PNP concentration was raised from 0.5 to 5 mM in the presence of 1 mM MgATP and 180 nM protein kinase A catalytic subunit (PKA). Adenylyl Imidodiphosphate 91-98 protein kinase cAMP-activated catalytic subunit alpha Homo sapiens 182-216 9569250-7 1998 AMP-PNP increased Po at temperatures above 30 degrees C but did not cause locking, evidence that the stabilizing interactions between domains, which have been proposed to maintain CFTR in the open burst state, are relatively weak. Adenylyl Imidodiphosphate 0-7 CF transmembrane conductance regulator Homo sapiens 180-184 9508802-11 1998 Wild-type and mutant CFTR channels became locked in open bursts when exposed to mixtures of ATP and the non-hydrolysable analogue AMP-PNP. Adenylyl Imidodiphosphate 130-137 CF transmembrane conductance regulator Homo sapiens 21-25 9508803-11 1998 5"-Adenylylimidodiphosphate (AMP-PNP) and pyrophosphate, two compounds that disrupt cycles of ATP hydrolysis, stabilized the open state of human CFTR. Adenylyl Imidodiphosphate 43-50 CF transmembrane conductance regulator Homo sapiens 159-163 9508803-12 1998 However, neither agent locked murine CFTR Cl- channels open, although AMP-PNP increased the Po of murine CFTR. Adenylyl Imidodiphosphate 70-77 cystic fibrosis transmembrane conductance regulator Mus musculus 105-109 9287333-6 1997 Quinazoline-induced EGFR dimerization was abrogated in vitro by ATP and the ATP analog adenyl-5"-yl imidodiphosphate. Adenylyl Imidodiphosphate 87-116 epidermal growth factor receptor Homo sapiens 20-24 9889854-1 1998 Experimentally it is observed that the head regions of weakly-binding myosin crossbridges (crossbridges with ATP or ADP.Pi at the nucleotide binding site) are mobile while attached to actin, while strongly-binding crossbridge heads, such as those with PPi or AMP-PNP at the nucleotide binding site, are immobile (Pate and Cooke, Biophys. Adenylyl Imidodiphosphate 259-266 myosin heavy chain 14 Homo sapiens 70-76 9651105-5 1998 The non-hydrolysable ATP analogue, adenylylimidodiphosphate, potentiated the effects of submaximal doses of ANP, BNP and urodilatin on this particulate GC-A, and attenuated or abolished sensitivity to isatin. Adenylyl Imidodiphosphate 35-59 natriuretic peptide B Rattus norvegicus 113-116 9651105-5 1998 The non-hydrolysable ATP analogue, adenylylimidodiphosphate, potentiated the effects of submaximal doses of ANP, BNP and urodilatin on this particulate GC-A, and attenuated or abolished sensitivity to isatin. Adenylyl Imidodiphosphate 35-59 grancalcin Rattus norvegicus 152-156 9341138-4 1997 In this report, the binding of GroES to highly purified GroEL in the presence of ATP, ADP, and the nonhydrolyzable ATP analogue, 5"-adenylyl beta,gamma-imidodiphosphate (AMP-PNP), was investigated by using the fluorescence anisotropy of succinimidyl-1-pyrenebutyrate-labeled GroES. Adenylyl Imidodiphosphate 170-177 chaperonin GroES Escherichia coli 31-36 9341138-4 1997 In this report, the binding of GroES to highly purified GroEL in the presence of ATP, ADP, and the nonhydrolyzable ATP analogue, 5"-adenylyl beta,gamma-imidodiphosphate (AMP-PNP), was investigated by using the fluorescence anisotropy of succinimidyl-1-pyrenebutyrate-labeled GroES. Adenylyl Imidodiphosphate 170-177 GroEL Escherichia coli 56-61 9341138-6 1997 In contrast, in the presence of ADP or AMP-PNP only one molecule of oligomeric GroES can be tightly bound by GroEL. Adenylyl Imidodiphosphate 39-46 chaperonin GroES Escherichia coli 79-84 9341138-6 1997 In contrast, in the presence of ADP or AMP-PNP only one molecule of oligomeric GroES can be tightly bound by GroEL. Adenylyl Imidodiphosphate 39-46 GroEL Escherichia coli 109-114 9341138-7 1997 With AMP-PNP, binding of a small amount (<20%) of a second GroES can be detected. Adenylyl Imidodiphosphate 5-12 chaperonin GroES Escherichia coli 62-67 9305951-0 1997 X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Adenylyl Imidodiphosphate 48-56 myosin, heavy chain 10, non-muscle Gallus gallus 99-105 9305951-1 1997 The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myosin II (S1dC) complexed with MgAMPPNP, MgATPgammaS, and MgADP are reported at 2.1, 1.9, and 2.1 A resolution, respectively. Adenylyl Imidodiphosphate 124-132 myosin, heavy chain 10, non-muscle Gallus gallus 50-56 9305951-6 1997 The overall structures of all three complexes are very similar to that of the beryllium fluoride complex which suggests that the differences in the physiological effects of ATPgammaS and AMPPNP are due to the changes in the equilibrium between the actin-bound and actin-free states of myosin caused by the lower affinity of AMPPNP for myosin. Adenylyl Imidodiphosphate 187-193 myosin, heavy chain 10, non-muscle Gallus gallus 285-291 9305951-6 1997 The overall structures of all three complexes are very similar to that of the beryllium fluoride complex which suggests that the differences in the physiological effects of ATPgammaS and AMPPNP are due to the changes in the equilibrium between the actin-bound and actin-free states of myosin caused by the lower affinity of AMPPNP for myosin. Adenylyl Imidodiphosphate 187-193 myosin, heavy chain 10, non-muscle Gallus gallus 335-341 9305951-6 1997 The overall structures of all three complexes are very similar to that of the beryllium fluoride complex which suggests that the differences in the physiological effects of ATPgammaS and AMPPNP are due to the changes in the equilibrium between the actin-bound and actin-free states of myosin caused by the lower affinity of AMPPNP for myosin. Adenylyl Imidodiphosphate 324-330 myosin, heavy chain 10, non-muscle Gallus gallus 285-291 9497339-3 1998 We have investigated several parameters characteristic of the interaction of Rad51p with ssDNA and dsDNA, particularly the effects of the nucleotide cofactors ATP and ADP and the analogs adenosine 5"-O-(thiotriphosphate) (ATPgammaS) and adenylyl-imidodiphosphate (AMP-PNP). Adenylyl Imidodiphosphate 237-262 recombinase RAD51 Saccharomyces cerevisiae S288C 77-83 9497339-3 1998 We have investigated several parameters characteristic of the interaction of Rad51p with ssDNA and dsDNA, particularly the effects of the nucleotide cofactors ATP and ADP and the analogs adenosine 5"-O-(thiotriphosphate) (ATPgammaS) and adenylyl-imidodiphosphate (AMP-PNP). Adenylyl Imidodiphosphate 264-271 recombinase RAD51 Saccharomyces cerevisiae S288C 77-83 9497339-4 1998 Rad51p binding to both 1-N6-ethenoadenosine and 3-N4-ethenocytidine ssDNA (epsilonDNA) and dsDNA requires the presence of Mg2+ and ATP; no binding occurs in the presence of ADP, AMP-PNP, or ATPgammaS. Adenylyl Imidodiphosphate 178-185 recombinase RAD51 Saccharomyces cerevisiae S288C 0-6 9497339-5 1998 Binding of Rad51p to dsDNA also requires ATP; ADP is ineffective, whereas ATPgammaS and AMP-PNP are considerably less able to promote binding and only at elevated concentrations of Rad51p. Adenylyl Imidodiphosphate 88-95 recombinase RAD51 Saccharomyces cerevisiae S288C 11-17 9497339-5 1998 Binding of Rad51p to dsDNA also requires ATP; ADP is ineffective, whereas ATPgammaS and AMP-PNP are considerably less able to promote binding and only at elevated concentrations of Rad51p. Adenylyl Imidodiphosphate 88-95 recombinase RAD51 Saccharomyces cerevisiae S288C 181-187 9407071-4 1997 Electron microscopy, image processing, and biochemical analysis of GroEL, a single-ring mutant (SR1) and a inter-ring communication affected mutant (A126V), in the presence of ATP and adenylyl imidodiphosphate, have allowed the identification of a conformational change in the apical domains that is strictly dependent on the communication between the two GroEL rings. Adenylyl Imidodiphosphate 184-209 heat shock protein family D (Hsp60) member 1 Homo sapiens 67-72 9395538-4 1997 We show here that the transcript release activity of factor 2 requires ATP or dATP and that adenosine 5"-O-(thiotriphosphate) (ATPgammaS), adenosine 5"-(beta,gamma-imino)triphosphate (AMP-PNP), or other NTPs do not support the activity. Adenylyl Imidodiphosphate 139-182 lodestar Drosophila melanogaster 53-61 9395538-4 1997 We show here that the transcript release activity of factor 2 requires ATP or dATP and that adenosine 5"-O-(thiotriphosphate) (ATPgammaS), adenosine 5"-(beta,gamma-imino)triphosphate (AMP-PNP), or other NTPs do not support the activity. Adenylyl Imidodiphosphate 184-191 lodestar Drosophila melanogaster 53-61 9341138-4 1997 In this report, the binding of GroES to highly purified GroEL in the presence of ATP, ADP, and the nonhydrolyzable ATP analogue, 5"-adenylyl beta,gamma-imidodiphosphate (AMP-PNP), was investigated by using the fluorescence anisotropy of succinimidyl-1-pyrenebutyrate-labeled GroES. Adenylyl Imidodiphosphate 170-177 chaperonin GroES Escherichia coli 275-280 9305994-9 1997 A 62-kDa intracellular fragment of RetGC-1 becomes more sensitive to cleavage by trypsin after preincubation at 30 degrees C unless ATP, AMP-PNP, or GCAP is present. Adenylyl Imidodiphosphate 137-144 guanylate cyclase 2D, retinal Homo sapiens 35-42 9285593-3 1997 We show here, however, that for the folding of malate dehydrogenase and Rubisco there is also an absolute requirement for ATP in the cis ring, as ADP and AMP-PNP are unable to promote folding. Adenylyl Imidodiphosphate 154-161 malic enzyme 1 Homo sapiens 47-67 8861908-3 1996 Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 A resolution for GroEL and GroEL-GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Adenylyl Imidodiphosphate 203-210 heat shock protein family D (Hsp60) member 1 Homo sapiens 116-121 9199497-1 1997 AMPPNP was found to be hydrolyzed by the motor domain of ncd (the product of a Drosophila gene, non-claret disjunctional), a kinesin-related protein. Adenylyl Imidodiphosphate 0-6 Kinesin light chain Drosophila melanogaster 125-132 9136876-6 1997 In the presence of ADP or ATP analogues such as ATP-gamma-S or AMP-PNP, the affinity to bind GroES increases by at least 2 orders of magnitude depending on the nucleotide concentration. Adenylyl Imidodiphosphate 63-70 chaperonin GroES Escherichia coli 93-98 9087913-2 1997 Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution. Adenylyl Imidodiphosphate 276-283 heat shock protein family D (Hsp60) member 1 Homo sapiens 197-202 9087913-2 1997 Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution. Adenylyl Imidodiphosphate 276-283 heat shock protein family D (Hsp60) member 1 Homo sapiens 197-202 9087913-3 1997 Both AMP-PNP and ATP induce similar conformational shifts in the apical domains of GroEL. Adenylyl Imidodiphosphate 5-12 heat shock protein family D (Hsp60) member 1 Homo sapiens 83-88 8910403-4 1996 In addition, the wild type Rad51 protein can catalyze pairing and strand exchange in the presence of the nonhydrolyzable ATP analogues adenylyl-imidodiphosphate and adenosine 5"-O-thiotriphosphate. Adenylyl Imidodiphosphate 135-160 recombinase RAD51 Saccharomyces cerevisiae S288C 27-32 8861908-3 1996 Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 A resolution for GroEL and GroEL-GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Adenylyl Imidodiphosphate 203-210 heat shock protein family D (Hsp60) member 1 Homo sapiens 106-111 9054367-7 1997 The inability of the nonhydrolyzable ATP analog, AMP-PNP, to cause a similar effect is explained by the interaction of bisANS with a transient conformational state of GroEL formed consequent to ATP hydrolysis. Adenylyl Imidodiphosphate 49-56 heat shock protein family D (Hsp60) member 1 Homo sapiens 167-172 9087913-5 1997 At the RR state for AMP-PNP and ATP, both GroEL rings undergo conformational changes, albeit of different magnitude, giving rise to a structurally asymmetric particle (one ring in the "open" state, while the other is in an "intermediate" state). Adenylyl Imidodiphosphate 20-27 heat shock protein family D (Hsp60) member 1 Homo sapiens 42-47 8943246-4 1996 Intrinsic fluorescence studies of the two mutants reveal that nucleotide binding (ADP or AMP-PNP (adenosine 5"-(beta,gamma-imino)triphosphate)) induces conformational changes in the tetradecamer that are independent of the presence of the co-chaperonin, GroES. Adenylyl Imidodiphosphate 89-96 heat shock protein family E (Hsp10) member 1 Homo sapiens 254-259 8943246-4 1996 Intrinsic fluorescence studies of the two mutants reveal that nucleotide binding (ADP or AMP-PNP (adenosine 5"-(beta,gamma-imino)triphosphate)) induces conformational changes in the tetradecamer that are independent of the presence of the co-chaperonin, GroES. Adenylyl Imidodiphosphate 98-141 heat shock protein family E (Hsp10) member 1 Homo sapiens 254-259 8861908-3 1996 Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 A resolution for GroEL and GroEL-GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Adenylyl Imidodiphosphate 203-210 heat shock protein family E (Hsp10) member 1 Homo sapiens 122-127 8634260-1 1996 ATP, its nonhydrolyzable analogue, AMP-PNP, and albumin were found to promote the dissociation of rhodopsin kinase from rod outer segments (ROS) containing photoactivated-rhodopsin (Rho*). Adenylyl Imidodiphosphate 35-42 G protein-coupled receptor kinase 7 Homo sapiens 98-114 8760028-1 1996 Previously, we showed in the native sweat duct that, in the presence of 0.1-0.5 mM ATP, nonhydrolyzable ATP analogue adenosine 5"-adenylylimidodiphosphate (AMP-PNP) can activate cystic fibrosis transmembrane conductance regulator Cl- conductance (CFTR GCl) (15). Adenylyl Imidodiphosphate 156-163 CF transmembrane conductance regulator Homo sapiens 247-251 8760028-4 1996 However, AMP-PNP can sustain previously activated CFTR GCl in the absence of ATP, even though Mg2+ is required for phosphorylation activation of CFTR GCl. Adenylyl Imidodiphosphate 9-16 CF transmembrane conductance regulator Homo sapiens 50-54 8759925-3 1996 Once phosphorylated, CFTR channels require hydrolyzable nucleotides to be active, but they can be locked in an open burst state when exposed to mixtures of ATP and its hydrolysis-resistant analogue AMP-PNP. Adenylyl Imidodiphosphate 198-205 CF transmembrane conductance regulator Homo sapiens 21-25 8810904-6 1996 The Trp fluorescence of a single Trp SecA mutant containing Trp775 decreased and increased upon the addition of NBS-I saturating concentrations of ADP or AMP-PNP, respectively. Adenylyl Imidodiphosphate 154-161 NME/NM23 nucleoside diphosphate kinase 1 Homo sapiens 112-115 8634260-1 1996 ATP, its nonhydrolyzable analogue, AMP-PNP, and albumin were found to promote the dissociation of rhodopsin kinase from rod outer segments (ROS) containing photoactivated-rhodopsin (Rho*). Adenylyl Imidodiphosphate 35-42 rhodopsin Homo sapiens 156-180 8845766-3 1996 To clarify the role of ATP in mhsp70-driven translocation, we tested the effect of the purified ATP analogues AMP-PNP and ATP gamma S on the Tim44-mhsp70 interaction. Adenylyl Imidodiphosphate 110-117 translocase of inner mitochondrial membrane 44 Homo sapiens 141-146 9079389-7 1996 Higher concentrations of GroES in the presence of ATP or AMP-PNP, but not ADP, produce a proportion of a fast-folding state, rising to 50% at a GroES7:GroEL14 stoichiometry of > or = 2:1. Adenylyl Imidodiphosphate 57-64 heat shock protein family E (Hsp10) member 1 Homo sapiens 25-30 8700870-4 1996 The rate of GroEL dissociation from the nonnative chain was increased significantly in the presence of 5"-adenylylimidodiphosphate (AMP-PNP), ADP, and ATP, yielding maximal values between 0.04 and 0.22 s(-1). Adenylyl Imidodiphosphate 132-139 GroEL Escherichia coli 12-17 7547923-7 1995 Second, binding of the ATP analogues AMP-PNP, dATP, and ATP gamma S to nucleotide-free hsc70 had very little further effect on the properties of the nucleotide-free hsc70. Adenylyl Imidodiphosphate 37-44 heat shock protein family A (Hsp70) member 8 Homo sapiens 87-92 8938718-5 1996 The ATP analog AMP-PNP has only minimal effects on channel activity after treatment with NS004, suggesting that hydrolysis of the ATP is required for its action on mSlo. Adenylyl Imidodiphosphate 15-22 potassium large conductance calcium-activated channel, subfamily M, alpha member 1 Mus musculus 164-168 7881906-7 1994 The presence of sulphate ions in the crystals and comparisons with the related Ha-ras-p21 oncogene product are used to infer the ATP-binding site, corroborated by the difference electron density for the ATP analogue AMP-PNP. Adenylyl Imidodiphosphate 216-223 H3 histone pseudogene 16 Homo sapiens 86-89 7982925-2 1994 The 10 S conformation of smooth muscle myosin could be induced by addition of 1-N6-ethenoadenosine or mant ADP plus beryllium fluoride, as well as by mant adenosine 5"-(beta,gamma-iminotriphosphate) (AMPPNP). Adenylyl Imidodiphosphate 200-206 myosin heavy chain 14 Homo sapiens 39-45 7626095-7 1995 The activity of eIF-2B was also inhibited following addition of either ATP or AMPPNP to a post-mitochondrial supernatant prepared from rat liver. Adenylyl Imidodiphosphate 78-84 eukaryotic translation initiation factor 2B subunit delta Rattus norvegicus 16-22 7918993-1 1994 We have used saturation transfer electron paramagnetic resonance (ST-EPR) to measure the microsecond rotational motion of actin-bound myosin heads in spin-labeled myofibrils in the presence of the ATP analogs AMPPNP (5"-adenylylimido-diphosphate) and ATP gamma S (adenosine-5"-O-(3-thiotriphosphate)). Adenylyl Imidodiphosphate 209-215 myosin heavy chain 14 Homo sapiens 134-140 8067390-3 1994 Purinergic receptor agonists inhibited AVP-stimulated Pf with the following rank order efficacy: ATP = ADP = UTP = AMP-PNP = alpha, beta-methylene-ATP > 2-methylthio-ATP >> AMP > adenosine, consistent with the pharmacology of a "nucleotide" receptor subtype. Adenylyl Imidodiphosphate 115-122 vasopressin-neurophysin 2-copeptin Oryctolagus cuniculus 39-42 7918993-2 1994 AMPPNP and ATP gamma S are believed to trap myosin in two major conformational intermediates of the actomyosin ATPase cycle, respectively known as the weakly bound and strongly bound states. Adenylyl Imidodiphosphate 0-6 myosin heavy chain 14 Homo sapiens 44-50 7918993-6 1994 At physiological ionic strength (mu = 165 mM), actin-bound myosin heads were found to be rotationally mobile on the microsecond time scale (tau r = 24 +/- 8 microseconds) in the presence of ATP gamma S, but not AMPPNP. Adenylyl Imidodiphosphate 211-217 myosin heavy chain 14 Homo sapiens 59-65 8007973-6 1994 The antirepressor first coeluted with TFIIH, was depleted from this fraction by antibodies directed against the TFIIH subunit p62, was dependent on either ATP or dATP, and then was inhibited by the ATP analogs AMP-PNP and ATP gamma S. Relief of HMG2-mediated repression as well as basal promoter function of TFIIH may involve a helicase that coelutes with TFIIH and displays similar nucleotide specificities. Adenylyl Imidodiphosphate 210-217 general transcription factor IIH subunit 1 Homo sapiens 38-43 8007973-6 1994 The antirepressor first coeluted with TFIIH, was depleted from this fraction by antibodies directed against the TFIIH subunit p62, was dependent on either ATP or dATP, and then was inhibited by the ATP analogs AMP-PNP and ATP gamma S. Relief of HMG2-mediated repression as well as basal promoter function of TFIIH may involve a helicase that coelutes with TFIIH and displays similar nucleotide specificities. Adenylyl Imidodiphosphate 210-217 general transcription factor IIH subunit 1 Homo sapiens 112-117 8007973-6 1994 The antirepressor first coeluted with TFIIH, was depleted from this fraction by antibodies directed against the TFIIH subunit p62, was dependent on either ATP or dATP, and then was inhibited by the ATP analogs AMP-PNP and ATP gamma S. Relief of HMG2-mediated repression as well as basal promoter function of TFIIH may involve a helicase that coelutes with TFIIH and displays similar nucleotide specificities. Adenylyl Imidodiphosphate 210-217 nucleoporin 62 Homo sapiens 126-129 8007973-6 1994 The antirepressor first coeluted with TFIIH, was depleted from this fraction by antibodies directed against the TFIIH subunit p62, was dependent on either ATP or dATP, and then was inhibited by the ATP analogs AMP-PNP and ATP gamma S. Relief of HMG2-mediated repression as well as basal promoter function of TFIIH may involve a helicase that coelutes with TFIIH and displays similar nucleotide specificities. Adenylyl Imidodiphosphate 210-217 high mobility group box 2 Homo sapiens 245-249 8007973-6 1994 The antirepressor first coeluted with TFIIH, was depleted from this fraction by antibodies directed against the TFIIH subunit p62, was dependent on either ATP or dATP, and then was inhibited by the ATP analogs AMP-PNP and ATP gamma S. Relief of HMG2-mediated repression as well as basal promoter function of TFIIH may involve a helicase that coelutes with TFIIH and displays similar nucleotide specificities. Adenylyl Imidodiphosphate 210-217 general transcription factor IIH subunit 1 Homo sapiens 112-117 8007973-6 1994 The antirepressor first coeluted with TFIIH, was depleted from this fraction by antibodies directed against the TFIIH subunit p62, was dependent on either ATP or dATP, and then was inhibited by the ATP analogs AMP-PNP and ATP gamma S. Relief of HMG2-mediated repression as well as basal promoter function of TFIIH may involve a helicase that coelutes with TFIIH and displays similar nucleotide specificities. Adenylyl Imidodiphosphate 210-217 general transcription factor IIH subunit 1 Homo sapiens 112-117 8319379-9 1993 Other hydrolysis-resistant P2 purinoceptor agonists, including ATP gamma S and AMP-PNP, were as effective as ATP in stimulating Pl turnover and Ca2+ mobilization as well as in inhibiting PG cell growth in vitro, suggesting the potential usefulness of such ATP analogs in clinical trials. Adenylyl Imidodiphosphate 79-86 pyrimidinergic receptor P2Y6 Homo sapiens 27-42 7515176-3 1994 We found that, although the hydrolysis-resistant ATP analogue 5"-adenosine(beta,gamma- imino)triphosphate (AMP-PNP) cannot open phosphorylated CFTR channels, it can cause channels opened by ATP to remain open for many minutes. Adenylyl Imidodiphosphate 107-114 CF transmembrane conductance regulator Homo sapiens 143-147 7515176-5 1994 However, this action of AMP-PNP is restricted to highly phosphorylated CFTR channels, which, in the presence of ATP, display a relatively high open probability, but is not seen in partially phosphorylated CFTR channels, which have a low open probability in the presence of ATP. Adenylyl Imidodiphosphate 24-31 CF transmembrane conductance regulator Homo sapiens 71-75 8399168-5 1993 Complex formation is demonstrated between ADF and actin containing either ATP, ADP, or AMPPNP as the bound nucleotide. Adenylyl Imidodiphosphate 87-93 destrin, actin depolymerizing factor Gallus gallus 42-45 8399168-5 1993 Complex formation is demonstrated between ADF and actin containing either ATP, ADP, or AMPPNP as the bound nucleotide. Adenylyl Imidodiphosphate 87-93 actin, beta Gallus gallus 50-55 7687826-4 1993 To examine the effect of AMP-PNP, we applied it to the cytosolic surface of phosphorylated CFTR Cl- channels contained in excised, cell-free patches of membrane. Adenylyl Imidodiphosphate 25-32 CF transmembrane conductance regulator Homo sapiens 91-95 7687826-5 1993 We found that preparations of 10 mM AMP-PNP opened phosphorylated CFTR Cl- channels. Adenylyl Imidodiphosphate 36-43 CF transmembrane conductance regulator Homo sapiens 66-70 7687826-6 1993 However, this effect was due to contaminating ATP: high-pressure liquid chromatography analysis of AMP-PNP demonstrated that 10 mM AMP-PNP could contain up to 50 microM ATP, which could account for the observed stimulation of CFTR Cl- channel activity. Adenylyl Imidodiphosphate 99-106 CF transmembrane conductance regulator Homo sapiens 226-230 7687826-6 1993 However, this effect was due to contaminating ATP: high-pressure liquid chromatography analysis of AMP-PNP demonstrated that 10 mM AMP-PNP could contain up to 50 microM ATP, which could account for the observed stimulation of CFTR Cl- channel activity. Adenylyl Imidodiphosphate 131-138 CF transmembrane conductance regulator Homo sapiens 226-230 8095403-4 1993 Inclusion of the co-protein, cpn10, tightens the binding of ATP, AMP-PNP, and ADP(P(i)) to give K1/2 values of 6 microM, 100 microM, and < 0.07 microM, respectively, and cooperativity is increased. Adenylyl Imidodiphosphate 65-72 heat shock protein family E (Hsp10) member 1 Homo sapiens 29-34 1586664-9 1992 In the presence of Mg2+ a third anion binding site can be occupied by phosphate but neither by AMP-PNP nor PPAPS. Adenylyl Imidodiphosphate 95-102 mucin 7, secreted Homo sapiens 19-22 8417143-3 1993 The ecto-5"-nucleotidase (EC 3.1.3.5) had a Km of 21 microM, was inhibited by AMPPNP and alpha,beta-methylene ADP, and by a specific antiserum. Adenylyl Imidodiphosphate 78-84 5'-nucleotidase ecto Homo sapiens 4-24 8417143-6 1993 The intraterminal 5"-nucleotidase enzyme, which amounted to 40% of the total 5"-nucleotidase activity, was inhibited by AMPPNP, alpha,beta-methylene ADP, and the antiserum, and also had the same kinetic properties as the ectoenzyme. Adenylyl Imidodiphosphate 120-126 5'-nucleotidase ecto Homo sapiens 18-33 8417143-6 1993 The intraterminal 5"-nucleotidase enzyme, which amounted to 40% of the total 5"-nucleotidase activity, was inhibited by AMPPNP, alpha,beta-methylene ADP, and the antiserum, and also had the same kinetic properties as the ectoenzyme. Adenylyl Imidodiphosphate 120-126 5'-nucleotidase ecto Homo sapiens 77-92 1355477-7 1992 However, our experiments indicated that tryptophanase dissociated readily from GroEL in the presence of not only ATP, but also in the presence of non-hydrolyzable ATP analogues such as ATP gamma S (adenosine 5"-O-(3-thiotriphosphate)) and AMP-PNP (adenyl-5"-yl imidodiphosphate) as well. Adenylyl Imidodiphosphate 239-246 GroEL Escherichia coli 79-84 1355477-7 1992 However, our experiments indicated that tryptophanase dissociated readily from GroEL in the presence of not only ATP, but also in the presence of non-hydrolyzable ATP analogues such as ATP gamma S (adenosine 5"-O-(3-thiotriphosphate)) and AMP-PNP (adenyl-5"-yl imidodiphosphate) as well. Adenylyl Imidodiphosphate 248-277 GroEL Escherichia coli 79-84 1332001-3 1992 Furthermore, ET potentiates, in a concentration-dependent fashion, the adenosine 5"-triphosphate (ATP) or the adenylylimidodiphosphate (AMP-PNP) but not the noradrenaline (NA)-induced motor activity. Adenylyl Imidodiphosphate 110-134 endothelin 1 Rattus norvegicus 13-15 1332001-3 1992 Furthermore, ET potentiates, in a concentration-dependent fashion, the adenosine 5"-triphosphate (ATP) or the adenylylimidodiphosphate (AMP-PNP) but not the noradrenaline (NA)-induced motor activity. Adenylyl Imidodiphosphate 136-143 endothelin 1 Rattus norvegicus 13-15 1386850-8 1992 A similar difference in the dissociation constants of myosin for F-actin was observed in the presence of adenylyl imidodiphosphate. Adenylyl Imidodiphosphate 105-130 myosin heavy chain 14 Homo sapiens 54-60 1607384-2 1992 In physiologically relevant buffers, AMPPNP binding to myosin caused transition to the soluble 10S myosin conformation due to trapping of nucleotide at the active sites. Adenylyl Imidodiphosphate 37-43 myosin heavy chain 14 Homo sapiens 55-61 1607384-2 1992 In physiologically relevant buffers, AMPPNP binding to myosin caused transition to the soluble 10S myosin conformation due to trapping of nucleotide at the active sites. Adenylyl Imidodiphosphate 37-43 myosin heavy chain 14 Homo sapiens 99-105 1607384-6 1992 Severin-induced fragmentation of actin in actomyosin fibers resulted in immediate disassembly of myosin thick filaments, demonstrating that actin filaments were indispensable for mediating myosin assembly in the presence of AMPPNP. Adenylyl Imidodiphosphate 224-230 myosin heavy chain 14 Homo sapiens 46-52 8428637-4 1993 In the presence of ATP or AMP-PNP, insulin significantly enhanced the binding of [35S]GTP-gamma-S to the partially purified insulin receptor. Adenylyl Imidodiphosphate 26-33 insulin receptor Rattus norvegicus 124-140 1680001-6 1991 The complex between GroEL and denatured LDH is destabilized by the binding of magnesium/ATP (Mg/ATP) or by the nonhydrolyzable analogue adenylyl imidodiphosphate (AMP-PNP). Adenylyl Imidodiphosphate 136-161 GroEL Escherichia coli 20-25 1657157-1 1991 We have used saturation-transfer electron paramagnetic resonance (ST-EPR) to detect the microsecond rotational motions of spin-labeled myosin subfragment one (MSL-S1) bound to actin in the presence of the ATP analogues AMPPNP (5"-adenylylimido diphosphate) and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)], which are believed to trap myosin in strongly and weakly bound intermediate states of the actomyosin ATPase cycle, respectively. Adenylyl Imidodiphosphate 219-225 myosin heavy chain 14 Homo sapiens 135-141 1680001-6 1991 The complex between GroEL and denatured LDH is destabilized by the binding of magnesium/ATP (Mg/ATP) or by the nonhydrolyzable analogue adenylyl imidodiphosphate (AMP-PNP). Adenylyl Imidodiphosphate 163-170 GroEL Escherichia coli 20-25 1676598-7 1991 The order of inhibition, with magnesium as metal cofactor, was ATP greater than GMP-PNP greater than AMP-PNP approximately GTP-gamma-S; with manganese, AMP-PNP was more inhibitory than GTP-gamma-S. Adenylyl Imidodiphosphate 152-159 5'-nucleotidase, cytosolic II Homo sapiens 80-83 2166167-9 1990 At high ionic strength, AMPPNP disoriented the spin labels as ATP did under relaxing conditions, suggesting that the myosin head is detached from and/or weakly (flexibly) attached to a thin filament. Adenylyl Imidodiphosphate 24-30 myosin heavy chain 14 Homo sapiens 117-123 1849890-8 1991 This nonhydrolyzable analog of ATP inhibited 17A3 binding, and the effect of AMP-PNP (like ATP) was potentiated by insulin. Adenylyl Imidodiphosphate 77-84 insulin Homo sapiens 115-122 2150967-3 1990 When the pretreated SR vesicles were allowed to react with 1 mM [14C]PBM in the presence of 1 mM AMPPNP, the amount of [14C]PBM incorporated into the ATPase increased with time in parallel with the formation of dimeric ATPase and reached the maximum labeling density of 1 mol of [14C]PBM per mol of dimeric ATPase at 40 min after the start of the reaction. Adenylyl Imidodiphosphate 97-103 dynein axonemal heavy chain 8 Homo sapiens 150-156 2150967-3 1990 When the pretreated SR vesicles were allowed to react with 1 mM [14C]PBM in the presence of 1 mM AMPPNP, the amount of [14C]PBM incorporated into the ATPase increased with time in parallel with the formation of dimeric ATPase and reached the maximum labeling density of 1 mol of [14C]PBM per mol of dimeric ATPase at 40 min after the start of the reaction. Adenylyl Imidodiphosphate 97-103 dynein axonemal heavy chain 8 Homo sapiens 219-225 2150967-3 1990 When the pretreated SR vesicles were allowed to react with 1 mM [14C]PBM in the presence of 1 mM AMPPNP, the amount of [14C]PBM incorporated into the ATPase increased with time in parallel with the formation of dimeric ATPase and reached the maximum labeling density of 1 mol of [14C]PBM per mol of dimeric ATPase at 40 min after the start of the reaction. Adenylyl Imidodiphosphate 97-103 dynein axonemal heavy chain 8 Homo sapiens 219-225 2150967-5 1990 The labeling density of [14C]NEM decreased from 2 to 1 mol per mol of the ATPase when the SR vesicles were allowed to react with [14C]NEM in the presence of AMPPNP. Adenylyl Imidodiphosphate 157-163 dynein axonemal heavy chain 8 Homo sapiens 74-80 34332033-3 2021 The secretagogue, adenylyl-imidodiphosphate, increased mucin secretion in SPOC1 (3.5-fold) and UNCN3T (1.5-fold) cells but not in Calu-3 cells. Adenylyl Imidodiphosphate 18-43 solute carrier family 13 member 2 Rattus norvegicus 55-60 2111815-5 1990 Hydrolysis of ATP is not required for inhibition, for adenyl-5"-yl imidodiphosphate (AMP-PNP), a nonhydrolyzable analogue of ATP, is as active an inhibitor; adenosine 5"-O-(thiotriphosphate) (ATP gamma S) inhibits far more weakly. Adenylyl Imidodiphosphate 54-83 purine nucleoside phosphorylase Homo sapiens 89-92 2551376-2 1989 These studies suggested that ethylene glycol shifts the structure of myosin.AMP-PNP toward the weak-binding conformation, i.e., toward the structure of myosin.ATP. Adenylyl Imidodiphosphate 76-83 myosin heavy chain 14 Homo sapiens 69-75 35529948-5 2022 Here, the crystal structures of the catalytically inactive kinase domain of SOBIR1 (SOBIR1-KD) from Arabidopsis thaliana were determined in complexes with AMP-PNP and Mg2+. Adenylyl Imidodiphosphate 155-162 Leucine-rich repeat protein kinase family protein Arabidopsis thaliana 76-82 2534124-4 1989 When SR vesicles were allowed to react with 1 mM PBM in the presence of 1 mM adenyl-5"-imidodiphosphate (AMP-PNP), the rate of oligomerization was markedly reduced and the amount of dimeric Ca2(+)-ATPase increased with time. Adenylyl Imidodiphosphate 105-112 dynein axonemal heavy chain 8 Homo sapiens 197-203 2534124-6 1989 When 1 mol of fluorescein isothiocyanate (FITC) was bound per mol of ATPase, the effects of AMP-PNP on the cross-linking with PBM were completely abolished. Adenylyl Imidodiphosphate 92-99 dynein axonemal heavy chain 8 Homo sapiens 69-75 2534124-9 1989 When SR vesicles were pretreated with PBM in the presence of AMP-PNP and digested with trypsin for a short time, the dimeric ATPase was degraded to a peptide with an apparent molecular mass of about 170 kDa. Adenylyl Imidodiphosphate 61-68 dynein axonemal heavy chain 8 Homo sapiens 125-131 35041979-0 2022 Cryo-EM Structure of AMP-PNP-bound Human Mitochondrial ATP-binding cassette transporter ABCB7. Adenylyl Imidodiphosphate 21-28 ATP binding cassette subfamily B member 7 Homo sapiens 88-93 35041979-2 2022 Here, we determined the structure of the nonhydrolyzable ATP analog adenosine-5"-(beta-gamma-imido) triphosphate (AMP-PNP) bound human ABCB7 at 3.3 A by single-particle electron cryo-microscopy (cryo-EM). Adenylyl Imidodiphosphate 114-121 ATP binding cassette subfamily B member 7 Homo sapiens 135-140 35041979-3 2022 The AMP-PNP-bound human ABCB7 shows an inverted V-shaped homodimeric architecture with an inward-facing open conformation. Adenylyl Imidodiphosphate 4-11 ATP binding cassette subfamily B member 7 Homo sapiens 24-29 35041979-4 2022 One AMP-PNP molecule and Mg2+ were identified in each nucleotide-binding domain (NBD) of the hABCB7 monomer. Adenylyl Imidodiphosphate 4-11 ATP binding cassette subfamily B member 7 Homo sapiens 93-99 2551376-2 1989 These studies suggested that ethylene glycol shifts the structure of myosin.AMP-PNP toward the weak-binding conformation, i.e., toward the structure of myosin.ATP. Adenylyl Imidodiphosphate 76-83 myosin heavy chain 14 Homo sapiens 152-158 2551376-7 1989 Therefore, our results confirm that ethylene glycol shifts the structure of the myosin.AMP-PNP toward the weak-binding conformation. Adenylyl Imidodiphosphate 87-94 myosin heavy chain 14 Homo sapiens 80-86 3011856-4 1986 In the presence of MgPPi or MgAMPPNP at 25 degrees C both 200 and 160 kDa fragments were present for several minutes after myosin heavy chain had been completely digested, suggesting that two populations of crossbridges (attached and detached) co-existed at the same time within the myofibril. Adenylyl Imidodiphosphate 28-36 myosin heavy chain 14 Homo sapiens 123-129 2841826-1 1988 We have used electron paramagnetic resonance (EPR) to study the effects of ATP and nucleotide analogs (mainly AMPPNP) on the orientation (measured by conventional EPR) and microsecond rotational dynamics (measured by saturation transfer EPR, STEPR) of spin-labeled myosin heads, both in glycerinated muscle fibers and in solutions of purified S1 and actin. Adenylyl Imidodiphosphate 110-116 myosin heavy chain 14 Homo sapiens 265-271 2824762-17 1987 The outflows of noradrenaline and 3,4-dihydroxyphenylglycol (DOPEG) induced by perivascular nerve stimulation increased with ATP (above 10(-6) M) or AMP-PNP (above 10(-5) M), while there was no change with mATP (10(-8)-10(-5) M) or 10.1 mM-K+o solution. Adenylyl Imidodiphosphate 149-156 solute carrier family 45, member 2 Mus musculus 206-210 3539181-5 1986 In addition, studies performed in the presence of single-stranded DNA demonstrated that the affinity of ATP, dATP, ATP-gamma-S, and AMP-PNP for recA protein is significantly increased. Adenylyl Imidodiphosphate 132-139 RAD51 recombinase Homo sapiens 144-148 3276399-4 1988 For CDP reductase, the activation by adenylylimido diphosphate and inhibition by dGTP and dTTP in these extracts from the ED1 and ED2 cells were the same as for the wild-type L1210 cells. Adenylyl Imidodiphosphate 37-62 cut-like homeobox 1 Mus musculus 4-7 3276399-4 1988 For CDP reductase, the activation by adenylylimido diphosphate and inhibition by dGTP and dTTP in these extracts from the ED1 and ED2 cells were the same as for the wild-type L1210 cells. Adenylyl Imidodiphosphate 37-62 ectodysplasin-A Mus musculus 122-125 3276399-4 1988 For CDP reductase, the activation by adenylylimido diphosphate and inhibition by dGTP and dTTP in these extracts from the ED1 and ED2 cells were the same as for the wild-type L1210 cells. Adenylyl Imidodiphosphate 37-62 unconventional SNARE in the ER 1 homolog (S. cerevisiae) Mus musculus 130-133 3539181-3 1986 Quantitative analysis of the cross-linking inhibition studies using a variety of nucleotide cofactors as competitors has shown that the binding affinity of adenine-containing nucleotides for recA protein decreases in the following order: ATP-gamma-S greater than dATP greater than ATP greater than adenylyl beta,gamma-imidodiphosphate (AMP-PNP) much greater than adenylyl beta,gamma-methylenediphosphate (AMP-PCP) approximately adenine. Adenylyl Imidodiphosphate 336-343 RAD51 recombinase Homo sapiens 191-195 4033761-5 1985 AMP-PNP may produce this effect by binding to an ATP-binding site on the transport machinery, thereby stabilizing the motility complex that is normally formed by a transported vesicle, an ATPase and a microtubule. Adenylyl Imidodiphosphate 0-7 dynein axonemal heavy chain 8 Homo sapiens 188-194 2868012-0 1986 Hydrolysis of adenyl-5-yl imidodiphosphate by beef heart mitochondrial ATPase. Adenylyl Imidodiphosphate 14-42 ATP synthase F1 subunit epsilon Homo sapiens 57-77 2868012-1 1986 Beef heart mitochondrial ATPase (F1) catalyzes the hydrolysis of the ATP analog adenyl-5-yl imidodiphosphate (AMP-PNP). Adenylyl Imidodiphosphate 80-108 ATP synthase F1 subunit epsilon Homo sapiens 11-31 2868012-1 1986 Beef heart mitochondrial ATPase (F1) catalyzes the hydrolysis of the ATP analog adenyl-5-yl imidodiphosphate (AMP-PNP). Adenylyl Imidodiphosphate 110-117 ATP synthase F1 subunit epsilon Homo sapiens 11-31 6746611-2 1984 The tryptic digestion of S-1 decreased the affinity of S-1 for F-actin both in the absence of nucleotide and the presence of AMPPNP or ATP, suggesting that the peptide cutting impairs the structures participating in the binding of S-1 or S-1-nucleotide complex with F-actin. Adenylyl Imidodiphosphate 125-131 proteasome 26S subunit, non-ATPase 1 Homo sapiens 25-28 2989278-12 1985 Known changes in ATPase conformation accompanying Ca2+ and adenyl-5"-yl imidodiphosphate X Mg binding did not affect the spin probe distribution. Adenylyl Imidodiphosphate 59-88 dynein axonemal heavy chain 8 Homo sapiens 17-23 6238959-2 1984 The Ca-ATPase was obtained in pure form by eluting the column with 400 microM adenyl 5"-yl imidodiphosphate, yielding an enzyme of almost twice the starting specific activity in a fraction containing half the initial protein. Adenylyl Imidodiphosphate 78-107 dynein axonemal heavy chain 8 Homo sapiens 7-13 2991534-1 1985 Molecular movements generated in the heavy-chain regions (27-50-20(X 10(3)) Mr) of myosin S1 on interaction with nucleotides ATP, AMPPNP, ADP and PPi were investigated by limited proteolysis of several enzyme-metal nucleotide complexes in the absence and presence of reversibly bound and crosslinked F-actin. Adenylyl Imidodiphosphate 130-136 myosin heavy chain 14 Homo sapiens 83-89 3158347-1 1985 Interrelationships between the binding by rabbit muscle phosphofructokinase of citrate, ATP, GTP, and adenyl-5"-yl imidodiphosphate (AMP-PNP) were investigated. Adenylyl Imidodiphosphate 102-131 ATP-dependent 6-phosphofructokinase, muscle type Oryctolagus cuniculus 56-75 3158347-1 1985 Interrelationships between the binding by rabbit muscle phosphofructokinase of citrate, ATP, GTP, and adenyl-5"-yl imidodiphosphate (AMP-PNP) were investigated. Adenylyl Imidodiphosphate 133-140 ATP-dependent 6-phosphofructokinase, muscle type Oryctolagus cuniculus 56-75 6477873-5 1984 The relative amounts of the 50K, 110K, and 150K peptides and the rates of myosin heavy-chain digestion in the presence of pyrophosphate and AMPPNP indicate partial dissociation of myosin from actin. Adenylyl Imidodiphosphate 140-146 PBV1SPCR2 Oryctolagus cuniculus 74-92 6746611-2 1984 The tryptic digestion of S-1 decreased the affinity of S-1 for F-actin both in the absence of nucleotide and the presence of AMPPNP or ATP, suggesting that the peptide cutting impairs the structures participating in the binding of S-1 or S-1-nucleotide complex with F-actin. Adenylyl Imidodiphosphate 125-131 proteasome 26S subunit, non-ATPase 1 Homo sapiens 55-58 6746611-2 1984 The tryptic digestion of S-1 decreased the affinity of S-1 for F-actin both in the absence of nucleotide and the presence of AMPPNP or ATP, suggesting that the peptide cutting impairs the structures participating in the binding of S-1 or S-1-nucleotide complex with F-actin. Adenylyl Imidodiphosphate 125-131 proteasome 26S subunit, non-ATPase 1 Homo sapiens 55-58 6746611-2 1984 The tryptic digestion of S-1 decreased the affinity of S-1 for F-actin both in the absence of nucleotide and the presence of AMPPNP or ATP, suggesting that the peptide cutting impairs the structures participating in the binding of S-1 or S-1-nucleotide complex with F-actin. Adenylyl Imidodiphosphate 125-131 proteasome 26S subunit, non-ATPase 1 Homo sapiens 55-58 6456267-0 1981 Sarcoplasmic reticulum ATPase catalyzes hydrolysis of adenyl-5"-yl imidodiphosphate. Adenylyl Imidodiphosphate 54-83 dynein axonemal heavy chain 8 Homo sapiens 23-29 6715529-9 1984 3H-Labelled AMPPNP binds to muscle fibres in 50% ethylene glycol in a similar amount to the number of myosin heads present. Adenylyl Imidodiphosphate 12-18 myosin heavy chain 14 Homo sapiens 102-108 6213262-5 1982 The temperature dependence of the chemical shift clearly indicates two limiting states for the S-1-CF3 with a highly temperature-dependent equilibrium between 5 and 40 degrees C. The low-temperature state appears to be identical with the state resulting from the binding of Mg.ADP or Mg.AMPPNP at 25 degree C. The energetics of the conformational change have been studied under various conditions. Adenylyl Imidodiphosphate 287-293 proteasome 26S subunit, non-ATPase 1 Homo sapiens 95-102 6285374-5 1982 Both the kinetics and the extent of the EGF-dependent thiophosphorylation at 0 degrees C are similar to those obtained with [gamma-32P]ATP, provided that ATP hydrolysis by the membrane preparation is inhibited by addition of adenosine 5"-[beta, gamma-imino]-triphosphate. Adenylyl Imidodiphosphate 225-270 epidermal growth factor Homo sapiens 40-43 6215942-0 1982 Studies of the nucleotide-binding sites on the mitochondrial F1-ATPase through the use of a photoactivable derivative of adenylyl imidodiphosphate. Adenylyl Imidodiphosphate 121-146 dynein axonemal heavy chain 8 Homo sapiens 64-70 6215942-1 1982 (1)N-4-Azido-2-nitrophenyl-gamma-[3H]aminobutyryl-AdoPP[NH] P(NAP4-AdoPP[NH]P) a photoactivable derivative of 5-adenylyl imidodiphosphate (AdoPP[NH]P), was synthesized. Adenylyl Imidodiphosphate 110-137 suppressor of cytokine signaling 7 Homo sapiens 62-66 7074085-1 1982 The kinetics of binding of the nonhydrolyzable nucleotides adenosine 5"-diphosphate (ADP) and adenosine 5"-(beta, gamma-imidotriphosphate) (AMP-PNP) to myosin subfragment 1 (SF-1) and actosubfragment 1 (acto-SF-1) were reinvestigated. Adenylyl Imidodiphosphate 140-147 splicing factor 1 Homo sapiens 152-178 7298614-0 1981 Temperature-modulated binding of ADP and adenyl-5"-yl imidodiphosphate to myosin subfragment 1 studied by calorimetric titration. Adenylyl Imidodiphosphate 41-70 myosin heavy chain 14 Homo sapiens 74-80 6456267-1 1981 Sarcoplasmic reticulum ATPase has been found to cleave the ATP analog adenyl-5"-yl imidodiphosphate in a calcium-dependent reaction. Adenylyl Imidodiphosphate 70-99 dynein axonemal heavy chain 8 Homo sapiens 23-29 7266930-1 1981 A marked depression of evoked CA1 potentials was observed with the nucleotide analogues a,b-methylene ADP (AOPCP) and adenylimido-diphosphate (AIP) and with 2"-adenosine monophosphate (2"-AMP). Adenylyl Imidodiphosphate 118-141 carbonic anhydrase 1 Rattus norvegicus 30-33 6457038-3 1981 Boundary sedimentation studies of phosphofructokinase in the presence of 1.0 mM fructose 6-phosphate, 0.1 mM adenylyl imidodiphosphate at pH 7.0 and 23 +/- 1 degrees C were performed. Adenylyl Imidodiphosphate 109-134 ATP-dependent 6-phosphofructokinase, muscle type Oryctolagus cuniculus 34-53 7266930-1 1981 A marked depression of evoked CA1 potentials was observed with the nucleotide analogues a,b-methylene ADP (AOPCP) and adenylimido-diphosphate (AIP) and with 2"-adenosine monophosphate (2"-AMP). Adenylyl Imidodiphosphate 143-146 carbonic anhydrase 1 Rattus norvegicus 30-33 6448862-10 1980 Adenylyl imidodiphosphate can partially prevent activation of dynein ATPase by calmodulin plus Ca++, but at much higher concentrations than required for prevention by ATP. Adenylyl Imidodiphosphate 0-25 calmodulin Bos taurus 79-89 6452897-7 1981 Adenylyl imidodiphosphate and quercetin, two compounds which partially mimic the inhibitory effect of IF1 on ATPase activity of F1, markedly prevented the binding of (14C)MABI-IF1 to F1; on the other hand, aurovertin, a specific ligand of the beta subunit of F1, did not affect the interaction between (14C)MABI-IF1 and F1. Adenylyl Imidodiphosphate 0-25 ATP synthase inhibitory factor subunit 1 Homo sapiens 102-105 6452897-7 1981 Adenylyl imidodiphosphate and quercetin, two compounds which partially mimic the inhibitory effect of IF1 on ATPase activity of F1, markedly prevented the binding of (14C)MABI-IF1 to F1; on the other hand, aurovertin, a specific ligand of the beta subunit of F1, did not affect the interaction between (14C)MABI-IF1 and F1. Adenylyl Imidodiphosphate 0-25 ATP synthase inhibitory factor subunit 1 Homo sapiens 176-179 6452897-7 1981 Adenylyl imidodiphosphate and quercetin, two compounds which partially mimic the inhibitory effect of IF1 on ATPase activity of F1, markedly prevented the binding of (14C)MABI-IF1 to F1; on the other hand, aurovertin, a specific ligand of the beta subunit of F1, did not affect the interaction between (14C)MABI-IF1 and F1. Adenylyl Imidodiphosphate 0-25 ATP synthase inhibitory factor subunit 1 Homo sapiens 176-179 7298393-4 1981 In the cells incubated in a medium devoid of theophylline and containing 5"-AMP instead of AMP-PNP, 5"-nucleotidase activity was observed in the same cell structures as AC activity, Hydrolysis of 5"-AMP in the nucleus was much stronger than that of AMP-PNP. Adenylyl Imidodiphosphate 249-256 5' nucleotidase, ecto Rattus norvegicus 100-115 6102087-6 1980 SHF could be protected by adenyl-5"-yl-imidodiphosphate (AMP-P(NH)P) in the presence of Ca2+ ions, whereas SHD was not. Adenylyl Imidodiphosphate 26-55 SH2 domain-containing adapter protein F Oryctolagus cuniculus 0-3 647108-6 1978 Evidence is presented that addition of AMP-PNP induces slippage of cross bridges on the actin filament by affecting the interaction between myosin and actin. Adenylyl Imidodiphosphate 39-46 myosin heavy chain 14 Homo sapiens 140-146 161792-5 1979 Enhancement of 30S dynein ATPase by metiamide is prevented by low (approximately 1 microM) concentrations of ATP and, less effectively, by AMP-PNP, but not by AMP-PCP even though the latter is a stronger inhibitor of 30S dynein ATPase than is AMP-PNP. Adenylyl Imidodiphosphate 139-146 dynein axonemal heavy chain 8 Homo sapiens 26-32 161792-5 1979 Enhancement of 30S dynein ATPase by metiamide is prevented by low (approximately 1 microM) concentrations of ATP and, less effectively, by AMP-PNP, but not by AMP-PCP even though the latter is a stronger inhibitor of 30S dynein ATPase than is AMP-PNP. Adenylyl Imidodiphosphate 243-250 dynein axonemal heavy chain 8 Homo sapiens 26-32 687772-2 1978 The effect of AMP-PNP was concentration-dependent with an optimum at 0.1 mM corresponding to the dissociation constant of AMP-PNP from the myosin heads. Adenylyl Imidodiphosphate 14-21 myosin heavy chain 14 Homo sapiens 139-145 687772-2 1978 The effect of AMP-PNP was concentration-dependent with an optimum at 0.1 mM corresponding to the dissociation constant of AMP-PNP from the myosin heads. Adenylyl Imidodiphosphate 122-129 myosin heavy chain 14 Homo sapiens 139-145 18351-0 1977 A phosphorus-magnetic-resonance study of the interaction of Mg2+ with adenyl-5"-yl imidodiphosphate. Adenylyl Imidodiphosphate 70-99 mucin 7, secreted Homo sapiens 60-63 18351-2 1977 The interaction of Mg2+ ions with adenyl-5"-yl imidodiphosphate, AMP-P(NH)P, has been studied at basic and acidic pH values by phosphorus magnetic resonance spectroscopy in aqueous solution. Adenylyl Imidodiphosphate 34-63 mucin 7, secreted Homo sapiens 19-22 239944-1 1975 Myosin and subfragment 1 give a maximum burst size of 0.25 to 0.30 protons per active site at pH 8 with ATP, alpha,beta-methylene-ATP, ADP, and adenylyl imidodiphosphate as substrates. Adenylyl Imidodiphosphate 144-169 myosin heavy chain 14 Homo sapiens 0-6 1010856-5 1976 Insulin stimulated allose transport, into or out of the cell, but not basal transport, is inhibited by a brief exposure of isolated fat-cells to exogenous ATP or ADP (but not AMP or AMP-PNP). Adenylyl Imidodiphosphate 182-189 insulin Canis lupus familiaris 0-7 183137-0 1976 X-ray titration of binding of beta, gamma-imido-ATP to myosin in insect flight muscle. Adenylyl Imidodiphosphate 30-51 myosin heavy chain 14 Homo sapiens 55-61 957434-0 1976 Changes in muscle crossbridges when beta, gamma-imido-ATP binds to myosin. Adenylyl Imidodiphosphate 36-57 myosin heavy chain 14 Homo sapiens 67-73 123467-1 1975 Equilibrium binding studies of the interaction of rabbit muscle phosphofructokinase with fructose 6-phosphate and fructose 1,6-bisphosphate have been carried out at 5 degrees in the presence of 1-10 mM potassium phosphate (pH 7.0 and 8.0), 5 mM citrate (pH 7.0), or 0.22 mm adenylyl imidodiphosphate (pH 7.0 and 8.0). Adenylyl Imidodiphosphate 274-299 ATP-dependent 6-phosphofructokinase, muscle type Oryctolagus cuniculus 64-83 4276968-0 1974 Binding of adenylyl imidodiphosphate, an analog of adenosine triphosphate, to myosin and heavy meromyosin. Adenylyl Imidodiphosphate 11-36 myosin heavy chain 14 Homo sapiens 78-84 123760-7 1975 Having adenylyl imidodiphosphate, areversible competitive inhibitor of myosin"s ATPase, present during the inactivation of HMM by S2P-PNP demonstrated that only one cysteine per head needed to be blocked to inactivate the enzyme. Adenylyl Imidodiphosphate 7-32 myosin heavy chain 14 Homo sapiens 71-77