| Year |
Citation |
Score |
| 2023 |
Srivastava G, Choy MS, Bolik-Coulon N, Page R, Peti W. Inhibitor-3 inhibits Protein Phosphatase 1 via a metal binding dynamic protein-protein interaction. Nature Communications. 14: 1798. PMID 37002212 DOI: 10.1038/s41467-023-37372-5 |
0.323 |
|
| 2022 |
Srivastava G, Bajaj R, Kumar GS, Gaudreau-Lapierre A, Nicolas H, Chamousset D, Kreitler D, Peti W, Trinkle-Mulcahy L, Page R. The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs. Cell Reports. 41: 111726. PMID 36450254 DOI: 10.1016/j.celrep.2022.111726 |
0.347 |
|
| 2021 |
Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. Elife. 10. PMID 34661528 DOI: 10.7554/eLife.63181 |
0.305 |
|
| 2021 |
Kumar GS, Page R, Peti W. H, N and C sequence specific backbone assignment of the MAP kinase binding domain of the dual specificity phosphatase 1 and its interaction with the MAPK p38. Biomolecular Nmr Assignments. PMID 34101142 DOI: 10.1007/s12104-021-10012-z |
0.336 |
|
| 2020 |
Li Y, Sheftic SR, Grigoriu S, Schwieters CD, Page R, Peti W. The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin. Science Advances. 6. PMID 32936779 DOI: 10.1126/Sciadv.Aba3681 |
0.34 |
|
| 2020 |
Torgeson KR, Clarkson MW, Kumar GS, Page R, Peti W. Cooperative dynamics across distinct structural elements regulate PTP1B activity. The Journal of Biological Chemistry. PMID 32737198 DOI: 10.1074/Jbc.Ra120.014652 |
0.384 |
|
| 2020 |
Sok P, Gógl G, Kumar GS, Alexa A, Singh N, Kirsch K, Sebő A, Drahos L, Gáspári Z, Peti W, Reményi A. MAP Kinase-Mediated Activation of RSK1 and MK2 Substrate Kinases. Structure (London, England : 1993). PMID 32649858 DOI: 10.1016/J.Str.2020.06.007 |
0.335 |
|
| 2020 |
Wang X, Garvanska DH, Nasa I, Ueki Y, Zhang G, Kettenbach AN, Peti W, Nilsson J, Page R. A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment. Elife. 9. PMID 32195664 DOI: 10.7554/Elife.55966 |
0.338 |
|
| 2019 |
Brauer BL, Moon TM, Sheftic SR, Nasa I, Page R, Peti W, Kettenbach AN. Leveraging new definitions of the LxVP SLiM to discover novel Calcineurin regulators and substrates. Acs Chemical Biology. PMID 31633908 DOI: 10.1021/Acschembio.9B00606 |
0.37 |
|
| 2019 |
Lin X, Ammosova T, Choy MS, Pietzsch CA, Ivanov A, Ahmad A, Saygideğer Y, Kumari N, Kovalskyy D, Üren A, Peti W, Bukreyev A, Nekhai S. Targeting the Non-catalytic RVxF Site of Protein Phosphatase-1 With Small Molecules for Ebola Virus Inhibition. Frontiers in Microbiology. 10: 2145. PMID 31572348 DOI: 10.3389/Fmicb.2019.02145 |
0.404 |
|
| 2019 |
Lixa C, Clarkson MW, Iqbal A, Moon TM, Almeida FCL, Peti W, Pinheiro AS. Retinoic acid binding leads to CRABP2 rigidification and dimerization. Biochemistry. PMID 31566355 DOI: 10.1021/Acs.Biochem.9B00672 |
0.388 |
|
| 2019 |
Choy MS, Moon TM, Ravindran R, Bray JA, Robinson LC, Archuleta TL, Shi W, Peti W, Tatchell K, Page R. SDS22 selectively recognizes and traps metal-deficient inactive PP1. Proceedings of the National Academy of Sciences of the United States of America. PMID 31548429 DOI: 10.1073/Pnas.1908718116 |
0.323 |
|
| 2019 |
Hendus-Altenburger R, Wang X, Sjøgaard-Frich LM, Pedraz-Cuesta E, Sheftic SR, Bendsøe AH, Page R, Kragelund BB, Pedersen SF, Peti W. Molecular basis for the binding and selective dephosphorylation of Na/H exchanger 1 by calcineurin. Nature Communications. 10: 3489. PMID 31375679 DOI: 10.1038/S41467-019-11391-7 |
0.407 |
|
| 2019 |
Bertran MT, Mouilleron S, Zhou Y, Bajaj R, Uliana F, Kumar GS, van Drogen A, Lee R, Banerjee JJ, Hauri S, O'Reilly N, Gstaiger M, Page R, Peti W, Tapon N. ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail. Nature Communications. 10: 771. PMID 30770806 DOI: 10.1038/S41467-019-08686-0 |
0.444 |
|
| 2019 |
Kumar GS, Page R, Peti W. Preparation of Phosphorylated Proteins for NMR Spectroscopy. Methods in Enzymology. 614: 187-205. PMID 30611424 DOI: 10.1016/Bs.Mie.2018.07.004 |
0.391 |
|
| 2018 |
Heroes E, Van der Hoeven G, Choy MS, Garcia JDP, Ferreira M, Nys M, Derua R, Beullens M, Ulens C, Peti W, Van Meervelt L, Page R, Bollen M. Structure-Guided Exploration of SDS22 Interactions with Protein Phosphatase PP1 and the Splicing Factor BCLAF1. Structure (London, England : 1993). PMID 30661852 DOI: 10.1016/J.Str.2018.12.002 |
0.472 |
|
| 2018 |
Choy MS, Bolik-Coulon N, Archuleta TL, Peti W, Page R. The structure of SDS22 provides insights into the mechanism of heterodimer formation with PP1. Acta Crystallographica. Section F, Structural Biology Communications. 74: 817-824. PMID 30511677 DOI: 10.1107/S2053230X18016503 |
0.501 |
|
| 2018 |
Kumar GS, Choy MS, Koveal DM, Lorinsky MK, Lyons SP, Kettenbach AN, Page R, Peti W. Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme. Science Advances. 4: eaau6044. PMID 30443599 DOI: 10.2210/Pdb6Dno/Pdb |
0.367 |
|
| 2018 |
Moon TM, D'Andréa ÉD, Lee CW, Soares A, Jakoncic J, Desbonnet C, Solache MG, Rice LB, Page R, Peti W. The structures of penicillin binding protein 4 (PBP4) and PBP5 from Enterococci provide structural insights into β-lactam resistance. The Journal of Biological Chemistry. PMID 30355734 DOI: 10.1074/Jbc.Ra118.006052 |
0.352 |
|
| 2018 |
Lyons SP, Jenkins NP, Nasa I, Choy MS, Adamo ME, Page R, Peti W, Moorhead GB, Kettenbach AN. A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans. Molecular & Cellular Proteomics : McP. PMID 30228194 DOI: 10.1074/Mcp.Ra118.000822 |
0.392 |
|
| 2018 |
Bajaj R, Bollen M, Peti W, Page R. KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive. Structure (London, England : 1993). PMID 30100357 DOI: 10.2210/Pdb6Czo/Pdb |
0.412 |
|
| 2018 |
Kumar GS, Clarkson MW, Kunze MBA, Granata D, Wand AJ, Lindorff-Larsen K, Page R, Peti W. Dynamic activation and regulation of the mitogen-activated protein kinase p38. Proceedings of the National Academy of Sciences of the United States of America. PMID 29666261 DOI: 10.1073/Pnas.1721441115 |
0.4 |
|
| 2018 |
Crespillo-Casado A, Claes Z, Choy MS, Peti W, Bollen M, Ron D. A Sephin1-insensitive tripartite holophosphatase dephosphorylates translation initiation factor 2α. The Journal of Biological Chemistry. PMID 29618508 DOI: 10.1074/Jbc.Ra118.002325 |
0.378 |
|
| 2018 |
Rice LB, Desbonnet C, Tait-Kamradt A, Garcia-Solache M, Lonks J, Moon TM, D'Andréa ÉD, Page R, Peti W. Structural and Regulatory Changes in PBP4 Trigger Decreased β-Lactam Susceptibility in Enterococcus faecalis. Mbio. 9. PMID 29615500 DOI: 10.1128/Mbio.00361-18 |
0.307 |
|
| 2018 |
Peti W, Page R, Boura E, Różycki B. Structures of Dynamic Protein Complexes: Hybrid Techniques to Study MAP Kinase Complexes and the ESCRT System. Methods in Molecular Biology (Clifton, N.J.). 1688: 375-389. PMID 29151218 DOI: 10.1007/978-1-4939-7386-6_17 |
0.421 |
|
| 2017 |
Zhang R, Lord DM, Bajaj R, Peti W, Page R, Sello JK. A peculiar IclR family transcription factor regulates para-hydroxybenzoate catabolism in Streptomyces coelicolor. Nucleic Acids Research. PMID 29240934 DOI: 10.1093/Nar/Gkx1234 |
0.342 |
|
| 2017 |
Choy MS, Swingle M, D'Arcy B, Abney K, Rusin SF, Kettenbach AN, Page R, Honkanen RE, Peti W. The PP1:tautomycetin complex reveals a path towards the development of PP1-specific inhibitors. Journal of the American Chemical Society. PMID 29156132 DOI: 10.1021/Jacs.7B09368 |
0.38 |
|
| 2017 |
Machado LESF, Page R, Peti W. (1)H, (15)N and (13)C sequence specific backbone assignment of the vanadate inhibited hematopoietic tyrosine phosphatase. Biomolecular Nmr Assignments. PMID 28856606 DOI: 10.1007/S12104-017-9770-7 |
0.438 |
|
| 2017 |
Machado LE, Shen TL, Page R, Peti W. The KIM-family Protein Tyrosine Phosphatases use distinct reversible oxidation intermediates: intramolecular or intermolecular disulfide bond formation. The Journal of Biological Chemistry. PMID 28389559 DOI: 10.1074/Jbc.M116.774174 |
0.351 |
|
| 2017 |
Choy MS, Li Y, Machado LE, Kunze MB, Connors CR, Wei X, Lindorff-Larsen K, Page R, Peti W. Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery. Molecular Cell. 65: 644-658.e5. PMID 28212750 DOI: 10.1016/J.Molcel.2017.01.014 |
0.436 |
|
| 2017 |
Machado LEdSF, Page R, Peti W. Sequence Specific Backbone Assignment of the catalytic domain of HePTP (residues 44-339) at pH 7.8 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27121 |
0.312 |
|
| 2016 |
Wang X, Bajaj R, Bollen M, Peti W, Page R. Expanding the PP2A Interactome by Defining a B56-Specific SLiM. Structure (London, England : 1993). 24: 2174-2181. PMID 27998540 DOI: 10.1016/J.Str.2016.09.010 |
0.432 |
|
| 2016 |
Sheftic SR, Page R, Peti W. Investigating the human Calcineurin Interaction Network using the πɸLxVP SLiM. Scientific Reports. 6: 38920. PMID 27974827 DOI: 10.1038/Srep38920 |
0.41 |
|
| 2016 |
Chen E, Choy MS, Petrényi K, Kónya Z, Erdődi F, Dombrádi V, Peti W, Page R. Molecular Insights into the Fungus-Specific Serine/Threonine Protein Phosphatase Z1 in Candida albicans. Mbio. 7. PMID 27578752 DOI: 10.1128/Mbio.00872-16 |
0.468 |
|
| 2016 |
Kumar GS, Gokhan E, De Munter S, Bollen M, Vagnarelli P, Peti W, Page R. The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism. Elife. 5. PMID 27572260 DOI: 10.7554/Elife.16539 |
0.372 |
|
| 2016 |
Peti W, Page R. NMR Spectroscopy to Study MAP Kinase Binding to MAP Kinase Phosphatases. Methods in Molecular Biology (Clifton, N.J.). 1447: 181-96. PMID 27514807 DOI: 10.1007/978-1-4939-3746-2_11 |
0.406 |
|
| 2015 |
Krishnan N, Krishnan K, Connors CR, Choy MS, Page R, Peti W, Van Aelst L, Shea SD, Tonks NK. PTP1B inhibition suggests a therapeutic strategy for Rett syndrome. The Journal of Clinical Investigation. 125: 3163-77. PMID 26214522 DOI: 10.1172/Jci80323 |
0.328 |
|
| 2015 |
Choy MS, Yusoff P, Lee IC, Newton JC, Goh CW, Page R, Shenolikar S, Peti W. Structural and Functional Analysis of the GADD34:PP1 eIF2α Phosphatase. Cell Reports. 11: 1885-91. PMID 26095357 DOI: 10.1016/J.Celrep.2015.05.043 |
0.425 |
|
| 2015 |
Peti W, Page R. Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable: Achieving specificity by targeting substrate and regulatory protein interaction sites. Bioorganic & Medicinal Chemistry. 23: 2781-5. PMID 25771485 DOI: 10.1016/J.Bmc.2015.02.040 |
0.419 |
|
| 2015 |
Harpole K, Ganesan SK, Peti W, Wand AJ. Probing the Role of Conformational Entropy in Protein-Inhibitor Binding Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.328 |
0.455 |
|
| 2014 |
Lord DM, Uzgoren Baran A, Soo VW, Wood TK, Peti W, Page R. McbR/YncC: implications for the mechanism of ligand and DNA binding by a bacterial GntR transcriptional regulator involved in biofilm formation. Biochemistry. 53: 7223-31. PMID 25376905 DOI: 10.1021/Bi500871A |
0.377 |
|
| 2014 |
Lord DM, Baran AU, Wood TK, Peti W, Page R. BdcA, a protein important for Escherichia coli biofilm dispersal, is a short-chain dehydrogenase/reductase that binds specifically to NADPH. Plos One. 9: e105751. PMID 25244619 DOI: 10.1371/Journal.Pone.0105751 |
0.421 |
|
| 2014 |
Krishnan N, Koveal D, Miller DH, Xue B, Akshinthala SD, Kragelj J, Jensen MR, Gauss CM, Page R, Blackledge M, Muthuswamy SK, Peti W, Tonks NK. Targeting the disordered C terminus of PTP1B with an allosteric inhibitor. Nature Chemical Biology. 10: 558-66. PMID 24845231 DOI: 10.1038/Nchembio.1528 |
0.345 |
|
| 2014 |
Francis DM, Koveal D, Tortajada A, Page R, Peti W. Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2. Plos One. 9: e91934. PMID 24637728 DOI: 10.1371/Journal.Pone.0091934 |
0.413 |
|
| 2014 |
Choy MS, Hieke M, Kumar GS, Lewis GR, Gonzalez-DeWhitt KR, Kessler RP, Stein BJ, Hessenberger M, Nairn AC, Peti W, Page R. Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code. Proceedings of the National Academy of Sciences of the United States of America. 111: 4097-102. PMID 24591642 DOI: 10.1073/Pnas.1317395111 |
0.489 |
|
| 2014 |
Francis DM, Page R, Peti W. Sequence-specific backbone ¹H, ¹³C and ¹âµN assignments of the 34 kDa catalytic domain of PTPN5 (STEP). Biomolecular Nmr Assignments. 8: 185-8. PMID 23640000 DOI: 10.1007/S12104-013-9480-8 |
0.437 |
|
| 2014 |
Koveal D, Miller D, Page R, Peti W. Sequence specific backbone assignment of protein phosphatase 1B (PTP1B) residues 1-393 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19224 |
0.393 |
|
| 2013 |
Peti W, Page R. Molecular basis of MAP kinase regulation. Protein Science : a Publication of the Protein Society. 22: 1698-710. PMID 24115095 DOI: 10.1002/Pro.2374 |
0.399 |
|
| 2013 |
Francis DM, Kumar GS, Koveal D, Tortajada A, Page R, Peti W. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993). 21: 1612-23. PMID 23932588 DOI: 10.1016/J.Str.2013.07.003 |
0.428 |
|
| 2013 |
Kumar GS, Zettl H, Page R, Peti W. Structural basis for the regulation of the mitogen-activated protein (MAP) kinase p38α by the dual specificity phosphatase 16 MAP kinase binding domain in solution. The Journal of Biological Chemistry. 288: 28347-56. PMID 23926106 DOI: 10.1074/Jbc.M113.499178 |
0.476 |
|
| 2013 |
Koveal D, Clarkson MW, Wood TK, Page R, Peti W. Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa. Journal of Molecular Biology. 425: 2219-31. PMID 23524133 DOI: 10.1016/J.Jmb.2013.03.023 |
0.397 |
|
| 2013 |
Grigoriu S, Bond R, Cossio P, Chen JA, Ly N, Hummer G, Page R, Cyert MS, Peti W. The molecular mechanism of substrate engagement and immunosuppressant inhibition of calcineurin. Plos Biology. 11: e1001492. PMID 23468591 DOI: 10.1371/Journal.Pbio.1001492 |
0.392 |
|
| 2013 |
Minnebo N, Görnemann J, O'Connell N, Van Dessel N, Derua R, Vermunt MW, Page R, Beullens M, Peti W, Van Eynde A, Bollen M. NIPP1 maintains EZH2 phosphorylation and promoter occupancy at proliferation-related target genes. Nucleic Acids Research. 41: 842-54. PMID 23241245 DOI: 10.1093/Nar/Gks1255 |
0.357 |
|
| 2013 |
Brown BL, Lord DM, Grigoriu S, Peti W, Page R. The Escherichia coli toxin MqsR destabilizes the transcriptional repression complex formed between the antitoxin MqsA and the mqsRA operon promoter. The Journal of Biological Chemistry. 288: 1286-94. PMID 23172222 DOI: 10.1074/Jbc.M112.421008 |
0.317 |
|
| 2013 |
Koveal D, Jayasundera TB, Wood TK, Peti W, Page R. Backbone and sidechain (1)H, (15)N and (13)C assignments of Tyrosine Phosphatase related to Biofilm formation A (TpbA) of Pseudomonas aeruginosa. Biomolecular Nmr Assignments. 7: 57-9. PMID 22392344 DOI: 10.1007/S12104-012-9376-Z |
0.355 |
|
| 2013 |
Peti W, Nairn AC, Page R. Structural basis for protein phosphatase 1 regulation and specificity. The Febs Journal. 280: 596-611. PMID 22284538 DOI: 10.1111/J.1742-4658.2012.08509.X |
0.454 |
|
| 2012 |
Koveal D, Schuh-Nuhfer N, Ritt D, Page R, Morrison DK, Peti W. A CC-SAM, for coiled coil-sterile α motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane. Science Signaling. 5: ra94. PMID 23250398 DOI: 10.1126/Scisignal.2003289 |
0.378 |
|
| 2012 |
Piserchio A, Francis DM, Koveal D, Dalby KN, Page R, Peti W, Ghose R. Docking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38α. Biochemistry. 51: 8047-9. PMID 23030599 DOI: 10.1021/Bi3012725 |
0.342 |
|
| 2012 |
Choy MS, Page R, Peti W. Regulation of protein phosphatase 1 by intrinsically disordered proteins. Biochemical Society Transactions. 40: 969-74. PMID 22988849 DOI: 10.1042/Bst20120094 |
0.476 |
|
| 2012 |
O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. Structure (London, England : 1993). 20: 1746-56. PMID 22940584 DOI: 10.1016/J.Str.2012.08.003 |
0.484 |
|
| 2012 |
Eibl C, Grigoriu S, Hessenberger M, Wenger J, Puehringer S, Pinheiro AS, Wagner RN, Proell M, Reed JC, Page R, Diederichs K, Peti W. Structural and functional analysis of the NLRP4 pyrin domain. Biochemistry. 51: 7330-41. PMID 22928810 DOI: 10.1021/Bi3007059 |
0.427 |
|
| 2012 |
Peti W, Nairn AC, Page R. Folding of Intrinsically Disordered Protein Phosphatase 1 Regulatory Proteins. Current Physical Chemistry. 2: 107-114. PMID 22866172 DOI: 10.2174/1877946811202010107 |
0.47 |
|
| 2011 |
Francis DM, Różycki B, Koveal D, Hummer G, Page R, Peti W. Structural basis of p38α regulation by hematopoietic tyrosine phosphatase. Nature Chemical Biology. 7: 916-24. PMID 22057126 DOI: 10.1038/Nchembio.707 |
0.434 |
|
| 2011 |
Francis DM, Różycki B, Tortajada A, Hummer G, Peti W, Page R. Resting and active states of the ERK2:HePTP complex. Journal of the American Chemical Society. 133: 17138-41. PMID 21985012 DOI: 10.1021/Ja2075136 |
0.337 |
|
| 2011 |
Pinheiro AS, Eibl C, Ekman-Vural Z, Schwarzenbacher R, Peti W. The NLRP12 pyrin domain: structure, dynamics, and functional insights. Journal of Molecular Biology. 413: 790-803. PMID 21978668 DOI: 10.1016/J.Jmb.2011.09.024 |
0.427 |
|
| 2011 |
Dancheck B, Ragusa MJ, Allaire M, Nairn AC, Page R, Peti W. Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex. Biochemistry. 50: 1238-46. PMID 21218781 DOI: 10.1021/Bi101774G |
0.785 |
|
| 2011 |
Pinheiro AS, Marsh JA, Forman-Kay JD, Peti W. Structural signature of the MYPT1-PP1 interaction. Journal of the American Chemical Society. 133: 73-80. PMID 21142030 DOI: 10.1021/Ja107810R |
0.461 |
|
| 2011 |
Ragusa MJ, Allaire M, Nairn AC, Page R, Peti W. Flexibility in the PP1:spinophilin holoenzyme. Febs Letters. 585: 36-40. PMID 21094159 DOI: 10.1016/J.Febslet.2010.11.022 |
0.432 |
|
| 2011 |
Brown BL, Wood TK, Peti W, Page R. Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation. The Journal of Biological Chemistry. 286: 2285-96. PMID 21068382 DOI: 10.1074/Jbc.M110.172643 |
0.382 |
|
| 2011 |
Ma Q, Yang Z, Pu M, Peti W, Wood TK. Engineering a novel c-di-GMP-binding protein for biofilm dispersal. Environmental Microbiology. 13: 631-42. PMID 21059164 DOI: 10.1111/J.1462-2920.2010.02368.X |
0.306 |
|
| 2011 |
Koveal D, Pinheiro AS, Peti W, Page R. Backbone and side chain 1H, 15N and 13C assignments of the KSR1 CA1 domain. Biomolecular Nmr Assignments. 5: 39-41. PMID 20737253 DOI: 10.1007/S12104-010-9262-5 |
0.329 |
|
| 2011 |
Pinheiro A, Peti W. Three-dimensional structure of the N-terminal effector PYRIN domain of NLRP12 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2L6A/Pdb |
0.332 |
|
| 2010 |
Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. Structure (London, England : 1993). 18: 1094-103. PMID 20826336 DOI: 10.1016/J.Str.2010.05.015 |
0.787 |
|
| 2010 |
Pinheiro AS, Proell M, Eibl C, Page R, Schwarzenbacher R, Peti W. Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity. The Journal of Biological Chemistry. 285: 27402-10. PMID 20547486 DOI: 10.1074/Jbc.M110.113191 |
0.377 |
|
| 2010 |
Bollen M, Peti W, Ragusa MJ, Beullens M. The extended PP1 toolkit: designed to create specificity. Trends in Biochemical Sciences. 35: 450-8. PMID 20399103 DOI: 10.1016/J.Tibs.2010.03.002 |
0.424 |
|
| 2010 |
Ragusa MJ, Dancheck B, Critton DA, Nairn AC, Page R, Peti W. Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nature Structural & Molecular Biology. 17: 459-64. PMID 20305656 DOI: 10.1038/Nsmb.1786 |
0.774 |
|
| 2010 |
Kim Y, Wang X, Zhang XS, Grigoriu S, Page R, Peti W, Wood TK. Escherichia coli toxin/antitoxin pair MqsR/MqsA regulate toxin CspD. Environmental Microbiology. 12: 1105-21. PMID 20105222 DOI: 10.1111/J.1462-2920.2009.02147.X |
0.332 |
|
| 2009 |
Brown BL, Grigoriu S, Kim Y, Arruda JM, Davenport A, Wood TK, Peti W, Page R. Three dimensional structure of the MqsR:MqsA complex: a novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties. Plos Pathogens. 5: e1000706. PMID 20041169 DOI: 10.1371/Journal.Ppat.1000706 |
0.37 |
|
| 2009 |
de Sa Pinheiro A, Ehart A, Ebner N, Proell M, Schwarzenbacher R, Peti W. Backbone and sidechain (1)H, (15)N and (13)C assignments of the NLRP7 pyrin domain. Biomolecular Nmr Assignments. 3: 207-9. PMID 19888692 DOI: 10.1007/S12104-009-9176-2 |
0.369 |
|
| 2009 |
Kelker MS, Page R, Peti W. Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors. Journal of Molecular Biology. 385: 11-21. PMID 18992256 DOI: 10.1016/J.Jmb.2008.10.053 |
0.412 |
|
| 2008 |
Critton DA, Tortajada A, Stetson G, Peti W, Page R. Structural basis of substrate recognition by hematopoietic tyrosine phosphatase. Biochemistry. 47: 13336-45. PMID 19053285 DOI: 10.1021/Bi801724N |
0.412 |
|
| 2008 |
Dancheck B, Nairn AC, Peti W. Detailed structural characterization of unbound protein phosphatase 1 inhibitors. Biochemistry. 47: 12346-56. PMID 18954090 DOI: 10.1021/Bi801308Y |
0.789 |
|
| 2008 |
Hopson RE, Peti W. Microcoil NMR spectroscopy: a novel tool for biological high throughput NMR spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 426: 447-58. PMID 18542883 DOI: 10.1007/978-1-60327-058-8_30 |
0.335 |
|
| 2008 |
Schüler H, Peti W. Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin. The Febs Journal. 275: 59-68. PMID 18028445 DOI: 10.1111/J.1742-4658.2007.06171.X |
0.421 |
|
| 2007 |
Ju T, Peti W. Backbone and sidechain (1)H, (15)N and (13)C assignments of the human G-actin binding protein profilin IIa. Biomolecular Nmr Assignments. 1: 205-7. PMID 19636866 DOI: 10.1007/S12104-007-9057-5 |
0.378 |
|
| 2007 |
Lee J, Page R, García-Contreras R, Palermino JM, Zhang XS, Doshi O, Wood TK, Peti W. Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. Journal of Molecular Biology. 373: 11-26. PMID 17765265 DOI: 10.1016/J.Jmb.2007.07.037 |
0.393 |
|
| 2007 |
Placzek WJ, Etezady-Esfarjani T, Herrmann T, Pedrini B, Peti W, Alimenti C, Luporini P, Wüthrich K. Cold-adapted signal proteins: NMR structures of pheromones from the Antarctic ciliate Euplotes nobilii. Iubmb Life. 59: 578-85. PMID 17701553 DOI: 10.1080/15216540701258165 |
0.479 |
|
| 2007 |
Ju T, Ragusa MJ, Hudak J, Nairn AC, Peti W. Structural characterization of the neurabin sterile alpha motif domain. Proteins. 69: 192-8. PMID 17600833 DOI: 10.1002/Prot.21513 |
0.311 |
|
| 2007 |
Kelker MS, Dancheck B, Ju T, Kessler RP, Hudak J, Nairn AC, Peti W. Structural basis for spinophilin-neurabin receptor interaction. Biochemistry. 46: 2333-44. PMID 17279777 DOI: 10.1021/Bi602341C |
0.78 |
|
| 2007 |
Peti W, Page R. Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expression and Purification. 51: 1-10. PMID 16904906 DOI: 10.1016/J.Pep.2006.06.024 |
0.328 |
|
| 2006 |
Wirmer J, Peti W, Schwalbe H. Motional properties of unfolded ubiquitin: a model for a random coil protein. Journal of Biomolecular Nmr. 35: 175-86. PMID 16865418 DOI: 10.1007/S10858-006-9026-9 |
0.57 |
|
| 2006 |
Kelker MS, Peti W. NMR assignment of the spinophilin PDZ domain (493-602). Journal of Biomolecular Nmr. 36: 24. PMID 16607467 DOI: 10.1007/S10858-006-0006-X |
0.323 |
|
| 2006 |
Johnson MA, Peti W, Herrmann T, Wilson IA, Wüthrich K. Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence. Protein Science : a Publication of the Protein Society. 15: 1030-41. PMID 16597827 DOI: 10.1110/Ps.051964606 |
0.576 |
|
| 2006 |
Baker KA, Hilty C, Peti W, Prince A, Pfaffinger PJ, Wider G, Wüthrich K, Choe S. NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain. Biochemistry. 45: 1663-72. PMID 16460013 DOI: 10.1021/Bi0516430 |
0.673 |
|
| 2006 |
Peti W, Smith L, Redfield C, Schwalbe H. 1H, 13C and 15N Assignments of Ubiquitin Unfolded in 8M Urea, pH2 and Analysis of Chemical shift Dispersion in Unfolded Proteins Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4375 |
0.51 |
|
| 2005 |
Peti W, Page R, Moy K, O'Neil-Johnson M, Wilson IA, Stevens RC, Wüthrich K. Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR. Journal of Structural and Functional Genomics. 6: 259-67. PMID 16283429 DOI: 10.1007/S10969-005-9000-X |
0.54 |
|
| 2005 |
Almeida MS, Herrmann T, Peti W, Wilson IA, Wüthrich K. NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins. Protein Science : a Publication of the Protein Society. 14: 2880-6. PMID 16199668 DOI: 10.1110/Ps.051755805 |
0.496 |
|
| 2005 |
Peti W, Johnson MA, Herrmann T, Neuman BW, Buchmeier MJ, Nelson M, Joseph J, Page R, Stevens RC, Kuhn P, Wüthrich K. Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7. Journal of Virology. 79: 12905-13. PMID 16188992 DOI: 10.1128/Jvi.79.20.12905-12913.2005 |
0.466 |
|
| 2005 |
Columbus L, Peti W, Etezady-Esfarjani T, Herrmann T, Wüthrich K. NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima. Proteins. 60: 552-7. PMID 15937903 DOI: 10.1002/Prot.20465 |
0.693 |
|
| 2005 |
Peti W, Herrmann T, Zagnitko O, Grzechnik SK, Wüthrich K. NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima Proteins: Structure, Function and Genetics. 59: 387-390. PMID 15723348 DOI: 10.1002/Prot.20352 |
0.588 |
|
| 2005 |
Page R, Peti W, Wilson IA, Stevens RC, Wüthrich K. NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline. Proceedings of the National Academy of Sciences of the United States of America. 102: 1901-5. PMID 15677718 DOI: 10.1073/Pnas.0408490102 |
0.539 |
|
| 2004 |
Kelker MS, Foss TR, Peti W, Teyton L, Kelly JW, Wüthrich K, Wilson IA. Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 A. Journal of Molecular Biology. 342: 1237-48. PMID 15351648 DOI: 10.1016/j.jmb.2004.07.089 |
0.399 |
|
| 2004 |
Griesinger C, Peti W, Meiler J, Brüschweiler R. Projection angle restraints for studying structure and dynamics of biomolecules Methods in Molecular Biology (Clifton, N.J.). 278: 107-121. PMID 15317994 DOI: 10.1385/1-59259-809-9:107 |
0.594 |
|
| 2004 |
Peti W, Etezady-Esfarjani T, Herrmann T, Klock HE, Lesley SA, Wüthrich K. NMR for structural proteomics of Thermotoga maritima: Screening and structure determination Journal of Structural and Functional Genomics. 5: 205-215. PMID 15263836 DOI: 10.1023/B:Jsfg.0000029055.84242.9F |
0.566 |
|
| 2004 |
Almeida MS, Peti W, Wüthrich K. Letter to the editor: 1H-, 13C- and 15N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima [29] Journal of Biomolecular Nmr. 29: 453-454. PMID 15213465 DOI: 10.1023/B:Jnmr.0000032522.43753.F1 |
0.52 |
|
| 2004 |
Etezady-Esfarjani T, Herrmann T, Peti W, Klock HE, Lesley SA, Wüthrich K. Letter to the editor: NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis [5] Journal of Biomolecular Nmr. 29: 403-406. PMID 15213441 DOI: 10.1023/B:Jnmr.0000032615.51536.1A |
0.542 |
|
| 2004 |
Peti W, Norcross J, Eldridge G, O'Neil-Johnson M. Biomolecular NMR using a microcoil NMR probe--new technique for the chemical shift assignment of aromatic side chains in proteins. Journal of the American Chemical Society. 126: 5873-8. PMID 15125680 DOI: 10.1021/Ja039779D |
0.401 |
|
| 2003 |
Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, Peti W, Zweckstetter M, Unden G, Griesinger C. The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli. The Journal of Biological Chemistry. 278: 39185-8. PMID 12907689 DOI: 10.1074/Jbc.C300344200 |
0.54 |
|
| 2003 |
Meiler J, Peti W, Griesinger C. Dipolar couplings in multiple alignments suggest α helical motion in ubiquitin Journal of the American Chemical Society. 125: 8072-8073. PMID 12837055 DOI: 10.1021/Ja029816L |
0.603 |
|
| 2003 |
Hus JC, Peti W, Griesinger C, Brüschweiler R. Self-consistency analysis of dipolar couplings in multiple alignments of ubiquitin. Journal of the American Chemical Society. 125: 5596-7. PMID 12733874 DOI: 10.1021/Ja029719S |
0.518 |
|
| 2003 |
Etezady-Esfarjani T, Peti W, Wüthrich K. NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima [6] Journal of Biomolecular Nmr. 25: 167-168. PMID 12652129 DOI: 10.1023/A:1022215901456 |
0.575 |
|
| 2002 |
Peti W, Meiler J, Brüschweiler R, Griesinger C. Model-free analysis of protein backbone motion from residual dipolar couplings Journal of the American Chemical Society. 124: 5822-5833. PMID 12010057 DOI: 10.1021/Ja011883C |
0.609 |
|
| 2001 |
Meiler J, Prompers JJ, Peti W, Griesinger C, Brüschweiler R. Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins Journal of the American Chemical Society. 123: 6098-6107. PMID 11414844 DOI: 10.1021/Ja010002Z |
0.61 |
|
| 2001 |
Peti W, Smith LJ, Redfield C, Schwalbe H. Chemical shifts in denatured proteins: resonance assignments for denatured ubiquitin and comparisons with other denatured proteins. Journal of Biomolecular Nmr. 19: 153-65. PMID 11256811 DOI: 10.1023/A:1008307323283 |
0.559 |
|
| 2001 |
Parac TN, Zientz E, Unden G, Coligaev B, Peti W, Griesinger C. Assignment of 1H, 13C and 15N resonances to the sensory domain of the membraneous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli. Journal of Biomolecular Nmr. 19: 91-92. PMID 11246864 DOI: 10.1023/A:1008301425100 |
0.493 |
|
| 2000 |
Peti W, Griesinger C, Bermel W. Adiabatic TOCSY for C,C and H,H J-transfer. Journal of Biomolecular Nmr. 18: 199-205. PMID 11142510 DOI: 10.1023/A:1026785725363 |
0.438 |
|
| 2000 |
Meiler J, Peti W, Griesinger C. DipoCoup: A versatile program for 3D-structure homology comparison based on residual dipolar couplings and pseudocontact shifts Journal of Biomolecular Nmr. 17: 283-294. PMID 11014592 DOI: 10.1023/A:1008362931964 |
0.636 |
|
| 2000 |
Carlomagno T, Peti W, Griesinger C. A new method for the simultaneous measurement of magnitude and sign of 1D(CH) and 1D(HH) dipolar couplings in methylene groups Journal of Biomolecular Nmr. 17: 99-109. PMID 10921775 DOI: 10.1023/A:1008346902500 |
0.499 |
|
| 2000 |
Peti W, Griesinger C. Measurement of Magnitude and Sign of H,H-Dipolar Couplings in Proteins. Journal of the American Chemical Society. 122: 3975-3976. DOI: 10.1021/Ja992997F |
0.485 |
|
| 2000 |
Peti W, Hennig M, Smith LJ, Schwalbe H. NMR Spectroscopic Investigation of ψ Torsion Angle Distribution in Unfolded Ubiquitin from Analysis of3J(Cα,Cα) Coupling Constants and Cross-Correlated Relaxation Rates Journal of the American Chemical Society. 122: 12017-12018. DOI: 10.1021/Ja001390S |
0.463 |
|
| Show low-probability matches. |