Year |
Citation |
Score |
2024 |
Raveh B, Eliasian R, Rashkovits S, Russel D, Hayama R, Sparks SE, Singh D, Lim R, Villa E, Rout MP, Cowburn D, Sali A. Integrative spatiotemporal map of nucleocytoplasmic transport. Biorxiv : the Preprint Server For Biology. PMID 38260487 DOI: 10.1101/2023.12.31.573409 |
0.52 |
|
2023 |
Cowburn D, Rout M. Improving the hole picture: towards a consensus on the mechanism of nuclear transport. Biochemical Society Transactions. 51: 871-886. PMID 37099395 DOI: 10.1042/BST20220494 |
0.557 |
|
2023 |
Cowburn D, Rout M. Improving the Hole Picture: Towards a Consensus on the Mechanism of Nuclear Transport. Arxiv. PMID 37064528 |
0.558 |
|
2022 |
Sekar G, Stevens AJ, Mostafavi AZ, Sashi P, Muir TW, Cowburn D. A Conserved Histidine Residue Drives Extein Dependence in an Enhanced Atypically Split Intein. Journal of the American Chemical Society. 144: 19196-19203. PMID 36194550 DOI: 10.1021/jacs.2c08985 |
0.807 |
|
2021 |
Bravo-Ferreira JFS, Cowburn D, Khoo Y, Singer A. NMR Assignment through Linear Programming. Journal of Global Optimization : An International Journal Dealing With Theoretical and Computational Aspects of Seeking Global Optima and Their Applications in Science, Management and Engineering. 83: 3-28. PMID 35528138 DOI: 10.1007/s10898-021-01004-3 |
0.515 |
|
2020 |
Sparks S, Hayama R, Rout MP, Cowburn D. Analysis of Multivalent IDP Interactions: Stoichiometry, Affinity, and Local Concentration Effect Measurements. Methods in Molecular Biology (Clifton, N.J.). 2141: 463-475. PMID 32696372 DOI: 10.1007/978-1-0716-0524-0_23 |
0.808 |
|
2019 |
Cowburn D, Sparks S, Temel DB, Rout MP. Deciphering the 'fuzzy' interaction of FG nucleoporins and transport factors using SANS Acta Crystallographica Section a Foundations and Advances. 75: a395-a395. DOI: 10.1107/S0108767319096144 |
0.763 |
|
2018 |
Stevens AJ, Sekar G, Gramespacher JA, Cowburn D, Muir TW. An Atypical Mechanism of Split Intein Molecular Recognition and Folding. Journal of the American Chemical Society. PMID 30156841 DOI: 10.1021/Jacs.8B07334 |
0.808 |
|
2018 |
Sparks S, Temel DB, Rout MP, Cowburn D. Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering. Structure (London, England : 1993). PMID 29429880 DOI: 10.1016/J.Str.2018.01.010 |
0.795 |
|
2018 |
Hayama R, Sparks S, Hecht LM, Dutta K, Cabana CM, Karp JM, Rout MP, Cowburn D. Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex. The Journal of Biological Chemistry. PMID 29374059 DOI: 10.1074/Jbc.Ac117.001649 |
0.8 |
|
2018 |
Sekar G, Stevens AJ, Muir TW, Cowburn D. Consensus engineered intein (Cat) with atypical split site Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr30480 |
0.753 |
|
2018 |
Sparks S, Hayama R, Rout MP, Cowburn D. The molecular basis of rapid and selective diffusion in the nuclear pore complex The Faseb Journal. 31. DOI: 10.1096/Fasebj.31.1_Supplement.758.4 |
0.77 |
|
2017 |
Warren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D. Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. Nature Communications. 8: 2215. PMID 29263320 DOI: 10.1038/S41467-017-02308-3 |
0.755 |
|
2017 |
Stevens AJ, Sekar G, Shah NH, Mostafavi AZ, Cowburn D, Muir TW. A promiscuous split intein with expanded protein engineering applications. Proceedings of the National Academy of Sciences of the United States of America. PMID 28739907 DOI: 10.1073/Pnas.1701083114 |
0.788 |
|
2017 |
Khoo Y, Singer A, Cowburn D. Integrating NOE and RDC using sum-of-squares relaxation for protein structure determination. Journal of Biomolecular Nmr. PMID 28616711 DOI: 10.1007/S10858-017-0108-7 |
0.573 |
|
2017 |
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J. Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure (London, England : 1993). PMID 28162953 DOI: 10.1016/J.Str.2017.01.006 |
0.766 |
|
2017 |
Karp JM, Sparks S, Cowburn D. Effects of FGFR2 kinase activation loop dynamics on catalytic activity. Plos Computational Biology. 13: e1005360. PMID 28151998 DOI: 10.1371/Journal.Pcbi.1005360 |
0.784 |
|
2017 |
Liu D, Cowburn D. Segmental Isotopic Labeling of Proteins for NMR Study Using Intein Technology. Methods in Molecular Biology (Clifton, N.J.). 1495: 131-145. PMID 27714614 DOI: 10.1007/978-1-4939-6451-2_9 |
0.57 |
|
2017 |
Sekar G, Cowburn D. Fused Npu DnaE GEP loop mutant from Nostoc punctiforme with Phe +2 Extein Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26981 |
0.762 |
|
2017 |
Sekar G, Cowburn D. Wild type fused Npu DnaE from Nostoc punctiforme with Gly +2 Extein Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26980 |
0.753 |
|
2017 |
Raveh B, Karp J, Sparks S, Timney B, Cowburn D, Rout MP, Sali A. Striking the Balance between Selectivity and Efficiency: An Integrative Model of Nucleocytoplasmic Transport Biophysical Journal. 112: 239a. DOI: 10.1016/J.Bpj.2016.11.1308 |
0.785 |
|
2016 |
Liu D, Cowburn D. Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase. Biophysics Reports. 2: 33-43. PMID 27819029 DOI: 10.1007/S41048-016-0025-4 |
0.584 |
|
2016 |
Liu D, Yuan Y, Xu R, Cowburn D. Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling. Protein & Cell. PMID 27815825 DOI: 10.1007/S13238-016-0333-Y |
0.63 |
|
2016 |
Raveh B, Karp JM, Sparks S, Dutta K, Rout MP, Sali A, Cowburn D. Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex. Proceedings of the National Academy of Sciences of the United States of America. PMID 27091992 DOI: 10.1073/Pnas.1522663113 |
0.793 |
|
2016 |
Stevens AJ, Brown ZZ, Shah NH, Sekar G, Cowburn D, Muir TW. Design of a Split Intein with Exceptional Protein Splicing Activity. Journal of the American Chemical Society. PMID 26854538 DOI: 10.1021/Jacs.5B13528 |
0.797 |
|
2016 |
Karp JM, Cowburn D. Simulations of FGFR2 Kinase Activation Loop Dynamics and their Effects on Catalytic Activity Biophysical Journal. 110: 177a. DOI: 10.1016/J.Bpj.2015.11.987 |
0.742 |
|
2016 |
Maguire LK, Wall K, Armstrong G, Dutta K, Sparks S, Temel DB, Kamal A, Tetenbaum-Novatt J, Rout MP, Cowburn D, Hough L. The Role of Intrinsic Disorder in the Molecular Mechanism of Nuclear Transport Biophysical Journal. 110: 558a. DOI: 10.1016/J.Bpj.2015.11.2983 |
0.782 |
|
2015 |
Ferrage F, Dutta K, Cowburn D. Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy. Molecules (Basel, Switzerland). 20: 21992-9. PMID 26690112 DOI: 10.3390/Molecules201219824 |
0.78 |
|
2015 |
Xia Y, Eryilmaz E, Zhang Q, Cowburn D, Putterman C. Anti-DNA antibody mediated catalysis is isotype dependent. Molecular Immunology. 69: 33-43. PMID 26655427 DOI: 10.1016/J.Molimm.2015.11.001 |
0.759 |
|
2015 |
Xia Y, Eryilmaz E, Der E, Pawar RD, Guo X, Cowburn D, Putterman C. A peptide mimic blocks the cross reaction of anti-DNA antibodies with glomerular antigens. Clinical and Experimental Immunology. PMID 26482679 DOI: 10.1111/Cei.12734 |
0.759 |
|
2015 |
Hough LE, Dutta K, Sparks S, Temel DB, Kamal A, Tetenbaum-Novatt J, Rout MP, Cowburn D. The molecular mechanism of nuclear transport revealed by atomic-scale measurements. Elife. 4. PMID 26371551 DOI: 10.7554/Elife.10027 |
0.79 |
|
2015 |
Karp JM, Eryilmaz E, Cowburn D. Erratum to: Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins. Journal of Biomolecular Nmr. 62: 119. PMID 25749870 DOI: 10.1007/S10858-015-9915-X |
0.78 |
|
2015 |
Wilner SE, Sparks SE, Cowburn D, Girvin ME, Levy M. Controlling lipid micelle stability using oligonucleotide headgroups. Journal of the American Chemical Society. 137: 2171-4. PMID 25634639 DOI: 10.1021/Ja512012M |
0.708 |
|
2015 |
Karp JM, Erylimaz E, Cowburn D. Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins. Journal of Biomolecular Nmr. 61: 35-45. PMID 25416617 DOI: 10.1007/S10858-014-9879-2 |
0.751 |
|
2015 |
Hough LE, Dutta K, Sparks S, Temel DB, Kamal A, Tetenbaum-Novatt J, Rout MP, Cowburn D. Author response: The molecular mechanism of nuclear transport revealed by atomic-scale measurements Elife. DOI: 10.7554/Elife.10027.019 |
0.76 |
|
2015 |
Karp JM, Cowburn D. Regulation of the Molecular Brake Region in FGFR2 Kinase Biophysical Journal. 108: 530a. DOI: 10.1016/J.Bpj.2014.11.2907 |
0.743 |
|
2014 |
Eryilmaz E, Shah NH, Muir TW, Cowburn D. Structural and dynamical features of inteins and implications on protein splicing. The Journal of Biological Chemistry. 289: 14506-11. PMID 24695731 DOI: 10.1074/Jbc.R113.540302 |
0.803 |
|
2014 |
Eryilmaz E, Shah NH, Muir TW, Cowburn D. Structural and dynamical features of inteins and implications on protein splicing (Journal of Biological Chemistry (2014) 289 (14506-14511)) Journal of Biological Chemistry. 289: 19278. DOI: 10.1074/Jbc.A113.540302 |
0.787 |
|
2013 |
Shah NH, Eryilmaz E, Cowburn D, Muir TW. Naturally split inteins assemble through a "capture and collapse" mechanism. Journal of the American Chemical Society. 135: 18673-81. PMID 24236406 DOI: 10.1021/Ja4104364 |
0.8 |
|
2013 |
Eryilmaz E, Janda A, Kim J, Cordero RJ, Cowburn D, Casadevall A. Global structures of IgG isotypes expressing identical variable regions. Molecular Immunology. 56: 588-98. PMID 23911417 DOI: 10.1016/J.Molimm.2013.06.006 |
0.786 |
|
2013 |
Chen H, Huang Z, Dutta K, Blais S, Neubert TA, Li X, Cowburn D, Traaseth NJ, Mohammadi M. Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations. Cell Reports. 4: 376-84. PMID 23871672 DOI: 10.1016/J.Celrep.2013.06.025 |
0.688 |
|
2013 |
Bhattacharya S, Ju JH, Orlova N, Khajeh JA, Cowburn D, Bu Z. Ligand-induced dynamic changes in extended PDZ domains from NHERF1. Journal of Molecular Biology. 425: 2509-28. PMID 23583913 DOI: 10.1016/J.Jmb.2013.04.001 |
0.706 |
|
2013 |
Shah NH, Eryilmaz E, Cowburn D, Muir TW. Extein residues play an intimate role in the rate-limiting step of protein trans-splicing. Journal of the American Chemical Society. 135: 5839-47. PMID 23506399 DOI: 10.1021/Ja401015P |
0.812 |
|
2013 |
Bhattacharya S, Ju J, Cowburn D, Bu Z. Structural characterization of the extended PDZ1 domain from NHERF1. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2M0T/Pdb |
0.301 |
|
2013 |
Bhattacharya S, Ju J, Cowburn D, Bu Z. Complex structure of C-terminal CFTR peptide and extended PDZ2 domain from NHERF1. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr18826 |
0.322 |
|
2013 |
Hough L, Dutta K, Kamal A, Temel D, Sparks S, Tetenbaum-Novatt J, Cowburn D, Cowburn D, Rout M. The Behavior of the Intrinsically Disordered FG Nups Determined by in Cell NMR Biophysical Journal. 104: 120a. DOI: 10.1016/J.Bpj.2012.11.692 |
0.789 |
|
2012 |
Cucuringu M, Singer A, Cowburn D. Eigenvector synchronization, graph rigidity and the molecule problem. Information and Inference : a Journal of the Ima. 1: 21. PMID 24432187 DOI: 10.1093/Imaiai/Ias002 |
0.524 |
|
2012 |
Janda A, Eryilmaz E, Nakouzi A, Cowburn D, Casadevall A. Variable region identical immunoglobulins differing in isotype express different paratopes. The Journal of Biological Chemistry. 287: 35409-17. PMID 22930758 DOI: 10.1074/Jbc.M112.404483 |
0.782 |
|
2012 |
Xu R, Liu D, Cowburn D. Abl kinase constructs expressed in bacteria: facilitation of structural and functional studies including segmental labeling by expressed protein ligation. Molecular Biosystems. 8: 1878-85. PMID 22592215 DOI: 10.1039/C2Mb25051A |
0.615 |
|
2012 |
Kalinina J, Dutta K, Ilghari D, Beenken A, Goetz R, Eliseenkova AV, Cowburn D, Mohammadi M. The alternatively spliced acid box region plays a key role in FGF receptor autoinhibition. Structure (London, England : 1993). 20: 77-88. PMID 22244757 DOI: 10.1016/J.Str.2011.10.022 |
0.704 |
|
2012 |
Bhattacharya S, Zhang H, Cowburn D, Debnath AK. Novel structures of self-associating stapled peptides. Biopolymers. 97: 253-64. PMID 22170623 DOI: 10.1002/Bip.22015 |
0.681 |
|
2012 |
Piserchio A, Cowburn D, Ghose R. Expression and purification of Src-family kinases for solution NMR studies. Methods in Molecular Biology (Clifton, N.J.). 831: 111-31. PMID 22167671 DOI: 10.1007/978-1-61779-480-3_7 |
0.667 |
|
2012 |
Burz DS, Cowburn D, Dutta K, Shekhtman A. In-Cell Protein NMR Spectroscopy Nmr of Biomolecules: Towards Mechanistic Systems Biology. 478-494. DOI: 10.1002/9783527644506.ch29 |
0.695 |
|
2011 |
Zhang H, Curreli F, Zhang X, Bhattacharya S, Waheed AA, Cooper A, Cowburn D, Freed EO, Debnath AK. Antiviral activity of α-helical stapled peptides designed from the HIV-1 capsid dimerization domain. Retrovirology. 8: 28. PMID 21539734 DOI: 10.1186/1742-4690-8-28 |
0.659 |
|
2011 |
Zhao F, Ilbert M, Varadan R, Cremers CM, Hoyos B, Acin-Perez R, Vinogradov V, Cowburn D, Jakob U, Hammerling U. Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation? Antioxidants & Redox Signaling. 14: 757-66. PMID 21067413 DOI: 10.1089/Ars.2010.3773 |
0.784 |
|
2011 |
Hough L, Dutta K, Tetenbaum-Novatt J, Cowburn D, Rout M. The Solution and Binding Behavior of the Intrinsically Disordered FG Nups Determined by STINT-NMR Biophysical Journal. 100: 185a. DOI: 10.1016/J.Bpj.2010.12.1229 |
0.808 |
|
2010 |
Ferrage F, Reichel A, Battacharya S, Cowburn D, Ghose R. On the measurement of ¹⁵N-{¹H} nuclear Overhauser effects. 2. Effects of the saturation scheme and water signal suppression. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 207: 294-303. PMID 20951618 DOI: 10.1016/J.Jmr.2010.09.014 |
0.764 |
|
2010 |
Tait S, Dutta K, Cowburn D, Warwicker J, Doig AJ, McCarthy JE. Local control of a disorder-order transition in 4E-BP1 underpins regulation of translation via eIF4E. Proceedings of the National Academy of Sciences of the United States of America. 107: 17627-32. PMID 20880835 DOI: 10.1073/Pnas.1008242107 |
0.653 |
|
2010 |
Nicholas MP, Eryilmaz E, Ferrage F, Cowburn D, Ghose R. Nuclear spin relaxation in isotropic and anisotropic media. Progress in Nuclear Magnetic Resonance Spectroscopy. 57: 111-58. PMID 20633361 DOI: 10.1016/J.Pnmrs.2010.04.003 |
0.761 |
|
2010 |
Frutos S, Goger M, Giovani B, Cowburn D, Muir TW. Branched intermediate formation stimulates peptide bond cleavage in protein splicing. Nature Chemical Biology. 6: 527-33. PMID 20495572 DOI: 10.1038/Nchembio.371 |
0.797 |
|
2010 |
Ferrage F, Dutta K, Shekhtman A, Cowburn D. Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density. Journal of Biomolecular Nmr. 47: 41-54. PMID 20372977 DOI: 10.1007/S10858-010-9409-9 |
0.803 |
|
2010 |
Bhattacharya S, Dai Z, Li J, Baxter S, Callaway DJE, Cowburn D, Bu Z. A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation Journal of Biological Chemistry. 285: 9981-9994. PMID 20042604 DOI: 10.1074/Jbc.M109.074005 |
0.718 |
|
2009 |
Liu D, Xu R, Cowburn D. Segmental isotopic labeling of proteins for nuclear magnetic resonance. Methods in Enzymology. 462: 151-75. PMID 19632474 DOI: 10.1016/S0076-6879(09)62008-5 |
0.652 |
|
2009 |
Piserchio A, Ghose R, Cowburn D. Optimized bacterial expression and purification of the c-Src catalytic domain for solution NMR studies. Journal of Biomolecular Nmr. 44: 87-93. PMID 19399371 DOI: 10.1007/S10858-009-9318-Y |
0.666 |
|
2009 |
Ferrage F, Cowburn D, Ghose R. Accurate sampling of high-frequency motions in proteins by steady-state (15)N-{(1)H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation. Journal of the American Chemical Society. 131: 6048-9. PMID 19358609 DOI: 10.1021/Ja809526Q |
0.762 |
|
2008 |
Schwartz EC, Shekhtman A, Dutta K, Pratt MR, Cowburn D, Darst S, Muir TW. A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding. Chemistry & Biology. 15: 1091-103. PMID 18940669 DOI: 10.1016/J.Chembiol.2008.09.008 |
0.782 |
|
2008 |
Bhattacharya S, Zhang H, Debnath AK, Cowburn D. Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid. The Journal of Biological Chemistry. 283: 16274-8. PMID 18417468 DOI: 10.1074/Jbc.C800048200 |
0.702 |
|
2008 |
Ferrage F, Piserchio A, Cowburn D, Ghose R. On the measurement of 15N-{1H} nuclear Overhauser effects. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 192: 302-13. PMID 18417394 DOI: 10.1016/J.Jmr.2008.03.011 |
0.757 |
|
2008 |
Zhang H, Zhao Q, Bhattacharya S, Waheed AA, Tong X, Hong A, Heck S, Curreli F, Goger M, Cowburn D, Freed EO, Debnath AK. A cell-penetrating helical peptide as a potential HIV-1 inhibitor. Journal of Molecular Biology. 378: 565-80. PMID 18374356 DOI: 10.1016/J.Jmb.2008.02.066 |
0.783 |
|
2008 |
Liu D, Xu R, Dutta K, Cowburn D. N-terminal cysteinyl proteins can be prepared using thrombin cleavage. Febs Letters. 582: 1163-7. PMID 18331839 DOI: 10.1016/J.Febslet.2008.02.078 |
0.756 |
|
2008 |
Xiong X, Cui P, Hossain S, Xu R, Warner B, Guo X, An X, Debnath AK, Cowburn D, Kotula L. Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1. Biochimica Et Biophysica Acta. 1783: 737-47. PMID 18328268 DOI: 10.1016/J.Bbamcr.2008.01.028 |
0.442 |
|
2007 |
Cowburn D. Moving parts: how the adaptor protein CRK is regulated, and regulates. Nature Structural & Molecular Biology. 14: 465-6. PMID 17549081 DOI: 10.1038/Nsmb0607-465 |
0.347 |
|
2007 |
Valentine ER, Ferrage F, Massi F, Cowburn D, Palmer AG. Joint composite-rotation adiabatic-sweep isotope filtration. Journal of Biomolecular Nmr. 38: 11-22. PMID 17353973 DOI: 10.1007/S10858-006-9131-9 |
0.629 |
|
2007 |
Xu R, Cahill S, Cowburn D. Triple Resonance Assignment for Abl SH(32) and One in the Complex with a Consolidated Ligand Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4252 |
0.417 |
|
2006 |
Burz DS, Dutta K, Cowburn D, Shekhtman A. In-cell NMR for protein-protein interactions (STINT-NMR). Nature Protocols. 1: 146-52. PMID 17406226 DOI: 10.1038/Nprot.2006.23 |
0.804 |
|
2006 |
Ferrage F, Pelupessy P, Cowburn D, Bodenhausen G. Protein backbone dynamics through 13C′-13C α cross-relaxation in NMR spectroscopy Journal of the American Chemical Society. 128: 11072-11078. PMID 16925424 DOI: 10.1021/Ja0600577 |
0.698 |
|
2006 |
Muralidharan V, Dutta K, Cho J, Vila-Perello M, Raleigh DP, Cowburn D, Muir TW. Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry. 45: 8874-84. PMID 16846230 DOI: 10.1021/Bi060590Z |
0.713 |
|
2006 |
Ji H, Shekhtman A, Ghose R, McDonnell JM, Cowburn D. NMR determination that an extended BH3 motif of pro-apoptotic BID is specifically bound to BCL-XL. Magnetic Resonance in Chemistry : Mrc. 44: S101-7. PMID 16826547 DOI: 10.1002/Mrc.1856 |
0.787 |
|
2006 |
Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO. NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition. Protein Science : a Publication of the Protein Society. 15: 1342-55. PMID 16731969 DOI: 10.1110/Ps.051844006 |
0.642 |
|
2006 |
Burz DS, Dutta K, Cowburn D, Shekhtman A. Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR). Nature Methods. 3: 91-3. PMID 16432517 DOI: 10.1038/Nmeth851 |
0.799 |
|
2004 |
Cowburn D, Shekhtman A, Xu R, Ottesen JJ, Muir TW. Segmental isotopic labeling for structural biological applications of NMR. Methods in Molecular Biology (Clifton, N.J.). 278: 47-56. PMID 15317990 DOI: 10.1385/1-59259-809-9:047 |
0.77 |
|
2004 |
Romanelli A, Shekhtman A, Cowburn D, Muir TW. Semisynthesis of a segmental isotopically labeled protein splicing precursor: NMR evidence for an unusual peptide bond at the N-extein-intein junction. Proceedings of the National Academy of Sciences of the United States of America. 101: 6397-402. PMID 15087498 DOI: 10.1073/Pnas.0306616101 |
0.767 |
|
2003 |
Goger MJ, McDonnell JM, Cowburn D. Using cryoprobes to decrease acquisition times of triple-resonance experiments used for protein resonance assignments Spectroscopy. 17: 161-167. DOI: 10.1155/2003/462471 |
0.791 |
|
2002 |
Shekhtman A, Cowburn D. A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins. Biochemical and Biophysical Research Communications. 296: 1222-7. PMID 12207904 DOI: 10.1016/S0006-291X(02)02006-5 |
0.724 |
|
2002 |
Shekhtman A, Ghose R, Goger M, Cowburn D. NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins. Febs Letters. 524: 177-82. PMID 12135763 DOI: 10.1016/S0014-5793(02)03051-X |
0.8 |
|
2002 |
Camarero JA, Shekhtman A, Campbell EA, Chlenov M, Gruber TM, Bryant DA, Darst SA, Cowburn D, Muir TW. Autoregulation of a bacterial sigma factor explored by using segmental isotopic labeling and NMR. Proceedings of the National Academy of Sciences of the United States of America. 99: 8536-41. PMID 12084914 DOI: 10.1073/Pnas.132033899 |
0.742 |
|
2001 |
Shekhtman A, Ghose R, Wang D, Cole PA, Cowburn D. Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis. Journal of Molecular Biology. 314: 129-38. PMID 11724538 DOI: 10.1006/Jmbi.2001.5126 |
0.796 |
|
2001 |
Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D. A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Nature Structural Biology. 8: 998-1004. PMID 11685249 DOI: 10.1038/Nsb1101-998 |
0.798 |
|
2001 |
Camarero JA, Fushman D, Cowburn D, Muir TW. Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain. Bioorganic & Medicinal Chemistry. 9: 2479-84. PMID 11553489 DOI: 10.1016/S0968-0896(01)00217-6 |
0.754 |
|
2001 |
Cowburn D, Muir TW. Segmental isotopic labeling using expressed protein ligation. Methods in Enzymology. 339: 41-54. PMID 11462824 DOI: 10.1016/S0076-6879(01)39308-4 |
0.478 |
|
2001 |
Fushman D, Cowburn D. Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy. Methods in Enzymology. 339: 109-26. PMID 11462809 DOI: 10.1016/S0076-6879(01)39312-6 |
0.724 |
|
2001 |
Pfeiffer S, Fushman D, Cowburn D. Simulated and NMR-derived backbone dynamics of a protein with significant flexibility: a comparison of spectral densities for the betaARK1 PH domain. Journal of the American Chemical Society. 123: 3021-36. PMID 11457013 DOI: 10.1021/Ja0031117 |
0.694 |
|
2001 |
Camarero JA, Fushman D, Sato S, Giriat I, Cowburn D, Raleigh DP, Muir TW. Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308: 1045-62. PMID 11352590 DOI: 10.1006/Jmbi.2001.4631 |
0.761 |
|
2001 |
McDonnell JM, Calvert R, Beavil RL, Beavil AJ, Henry AJ, Sutton BJ, Gould HJ, Cowburn D. The structure of the IgE Cepsilon2 domain and its role in stabilizing the complex with its high-affinity receptor FcepsilonRIalpha. Nature Structural Biology. 8: 437-41. PMID 11323720 DOI: 10.1038/87603 |
0.331 |
|
2001 |
Ghose R, Fushman D, Cowburn D. Determination of the rotational diffusion tensor of macromolecules in solution from nmr relaxation data with a combination of exact and approximate methods--application to the determination of interdomain orientation in multidomain proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 149: 204-17. PMID 11318619 DOI: 10.1006/Jmre.2001.2295 |
0.781 |
|
2000 |
Nicholas P, Fushman D, Ruchinsky V, Cowburn D. The virtual NMR spectrometer: a computer program for efficient simulation of NMR experiments involving pulsed field gradients. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 145: 262-75. PMID 10910695 DOI: 10.1006/Jmre.2000.2108 |
0.676 |
|
2000 |
Fushman D, Ghose R, Cowburn D. The effect of finite sampling on the determination of orientational properties: A theoretical treatment with application to interatomic vectors in proteins Journal of the American Chemical Society. 122: 10640-10649. DOI: 10.1021/Ja001128J |
0.771 |
|
1999 |
Fushman D, Xu R, Cowburn D. Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32). Biochemistry. 38: 10225-30. PMID 10441115 DOI: 10.1021/Bi990897G |
0.759 |
|
1999 |
Xu R, Cahill S, Cowburn D. Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand. Journal of Biomolecular Nmr. 14: 187-8. PMID 10427746 DOI: 10.1023/A:1008350823354 |
0.419 |
|
1999 |
Oda Y, Huang K, Cross FR, Cowburn D, Chait BT. Accurate quantitation of protein expression and site-specific phosphorylation. Proceedings of the National Academy of Sciences of the United States of America. 96: 6591-6. PMID 10359756 DOI: 10.1073/Pnas.96.12.6591 |
0.518 |
|
1999 |
Pfeiffer S, Fushman D, Cowburn D. Impact of Cl- and Na+ ions on simulated structure and dynamics of betaARK1 PH domain. Proteins. 35: 206-17. PMID 10223293 DOI: 10.1002/(Sici)1097-0134(19990501)35:2<206::Aid-Prot7>3.0.Co;2-A |
0.684 |
|
1999 |
Xu Q, Zheng J, Xu R, Barany G, Cowburn D. Flexibility of interdomain contacts revealed by topological isomers of bivalent consolidated ligands to the dual Src homology domain SH(32) of abelson. Biochemistry. 38: 3491-7. PMID 10090735 DOI: 10.1021/Bi982744J |
0.674 |
|
1999 |
McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell. 96: 625-34. PMID 10089878 DOI: 10.1016/S0092-8674(00)80573-5 |
0.739 |
|
1999 |
Fushman D, Cowburn D. The effect of noncollinearity of 15N-1H dipolar and 15N CSA tensors and rotational anisotropy on 15N relaxation, CSA/dipolar cross correlation, and TROSY. Journal of Biomolecular Nmr. 13: 139-47. PMID 10070755 DOI: 10.1023/A:1008349331773 |
0.7 |
|
1999 |
Xu R, Ayers B, Cowburn D, Muir TW. Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proceedings of the National Academy of Sciences of the United States of America. 96: 388-93. PMID 9892643 DOI: 10.1073/Pnas.96.2.388 |
0.636 |
|
1999 |
Fushman D, Tjandra N, Cowburn D. An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions Journal of the American Chemical Society. 121: 8577-8582. DOI: 10.1021/Ja9904991 |
0.699 |
|
1998 |
Lee CH, Cowburn D, Kuriyan J. Peptide recognition mechanisms of eukaryotic signaling modules. Methods in Molecular Biology (Clifton, N.J.). 84: 3-31. PMID 9666439 DOI: 10.1385/0-89603-488-7:3 |
0.498 |
|
1998 |
McDonnell JM, Fushman D, Cahill SM, Zhou W, Wolven A, Wilson CB, Nelle TD, Resh MD, Wills J, Cowburn D. Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus. Journal of Molecular Biology. 279: 921-8. PMID 9642071 DOI: 10.1006/Jmbi.1998.1788 |
0.689 |
|
1998 |
Posern G, Zheng J, Knudsen BS, Kardinal C, Müller KB, Voss J, Shishido T, Cowburn D, Cheng G, Wang B, Kruh GD, Burrell SK, Jacobson CA, Lenz DM, Zamborelli TJ, et al. Development of highly selective SH3 binding peptides for Crk and CRKL which disrupt Crk-complexes with DOCK180, SoS and C3G. Oncogene. 16: 1903-12. PMID 9591773 DOI: 10.1038/Sj.Onc.1201714 |
0.468 |
|
1998 |
Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H, Cowburn D. The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. The Journal of Biological Chemistry. 273: 2835-43. PMID 9446593 DOI: 10.1074/Jbc.273.5.2835 |
0.731 |
|
1998 |
Cowburn D. Peptide recognition by PTB and PDZ domains. Current Opinion in Structural Biology. 7: 835-8. PMID 9434904 DOI: 10.1016/S0959-440X(97)80155-8 |
0.327 |
|
1998 |
Fushman D, Tjandra N, Cowburn D. Direct measurement of 15N chemical shift anisotropy in solution Journal of the American Chemical Society. 120: 10947-10952. DOI: 10.1021/Ja981686M |
0.692 |
|
1998 |
Fushman D, Cowburn D. Model-independent analysis of 15N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example [5] Journal of the American Chemical Society. 120: 7109-7110. DOI: 10.1021/Ja980565J |
0.685 |
|
1997 |
Zheng J, Chen RH, Corblan-Garcia S, Cahill SM, Bar-Sagi D, Cowburn D. The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains Journal of Biological Chemistry. 272: 30340-30344. PMID 9374522 DOI: 10.1074/Jbc.272.48.30340 |
0.415 |
|
1997 |
Kuriyan J, Cowburn D. Modular peptide recognition domains in eukaryotic signaling Annual Review of Biophysics and Biomolecular Structure. 26: 259-288. PMID 9241420 DOI: 10.1146/Annurev.Biophys.26.1.259 |
0.554 |
|
1997 |
Fushman D, Cahill S, Cowburn D. The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration. Journal of Molecular Biology. 266: 173-94. PMID 9054979 DOI: 10.1006/Jmbi.1996.0771 |
0.716 |
|
1997 |
Cowburn D. Much more than the sum of the parts: structures of the dual SH2 domains of ZAP-70 and Syp. Chemistry & Biology. 3: 79-82. PMID 8807831 DOI: 10.1016/S1074-5521(96)90281-1 |
0.337 |
|
1997 |
McDonnell JM, Fushman D, Cahill SM, Sutton BJ, Cowburn D. Solution structures of FcεRI α-chain mimics: A β-hairpin peptide and its retroenantiomer Journal of the American Chemical Society. 119: 5321-5328. DOI: 10.1021/Ja963884O |
0.702 |
|
1996 |
Cowburn D. Adaptors and integrators. Structure (London, England : 1993). 4: 1005-8. PMID 8805586 DOI: 10.1016/S0969-2126(96)00106-2 |
0.312 |
|
1996 |
Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D. Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity. Journal of Molecular Biology. 255: 14-21. PMID 8568861 DOI: 10.1006/Jmbi.1996.0002 |
0.786 |
|
1996 |
Xu Q, Zheng J, Cowburn D, Barany G. Synthesis and characterization of branched phosphopeptides: Prototype consolidated ligands for SH(32) domains Letters in Peptide Science. 3: 31-36. DOI: 10.1007/Bf00131083 |
0.606 |
|
1995 |
Gosser YQ, Zheng J, Overduin M, Mayer BJ, Cowburn D. The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct. Structure (London, England : 1993). 3: 1075-86. PMID 8590002 DOI: 10.1016/S0969-2126(01)00243-X |
0.639 |
|
1995 |
Fushman D, Cahill S, Lemmon MA, Schlessinger J, Cowburn D. Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 92: 816-20. PMID 7846058 DOI: 10.1073/Pnas.92.3.816 |
0.8 |
|
1995 |
Knudsen BS, Zheng J, Feller SM, Mayer JP, Burrell SK, Cowburn D, Hanafusa H. Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins. The Embo Journal. 14: 2191-8. PMID 7774577 DOI: 10.1002/J.1460-2075.1995.Tb07213.X |
0.442 |
|
1995 |
Wu X, Knudsen B, Feller SM, Zheng J, Sali A, Cowburn D, Hanafusa H, Kuriyan J. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure (London, England : 1993). 3: 215-26. PMID 7735837 DOI: 10.1016/S0969-2126(01)00151-4 |
0.691 |
|
1995 |
Cowburn D. Src homology adaptor proteins: more than the sum of the parts? Structure (London, England : 1993). 3: 429-30. PMID 7663939 DOI: 10.1016/S0969-2126(01)00175-7 |
0.381 |
|
1995 |
Cowburn D, Zheng J, Xu Q, Barany G. Enhanced affinities and specificities of consolidated ligands for the Src homology (SH) 3 and SH2 domains of Abelson protein-tyrosine kinase. The Journal of Biological Chemistry. 270: 26738-41. PMID 7592905 DOI: 10.1074/Jbc.270.45.26738 |
0.624 |
|
1995 |
Lee CH, Leung B, Lemmon MA, Zheng J, Cowburn D, Kuriyan J, Saksela K. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein Embo Journal. 14: 5006-5015. PMID 7588629 |
0.658 |
|
1995 |
Glushka J, Lee M, Coffin S, Cowburn D. 15N Chemical Shifts of Backbone Amides in Bovine Pancreatic Trypsin Inhibitor and Apamin [Additions and Corrections to J. Am. Chem. Soc. 1989 111,7716-7722] Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr485 |
0.588 |
|
1995 |
Glushka J, Lee M, Coffin S, Cowburn D. 15N Chemical Shifts of Backbone Amides in Bovine Pancreatic Trypsin Inhibitor Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr338 |
0.584 |
|
1995 |
Lee C, Leung B, Lemmon MA, Zheng J, Cowburn D, Kuriyan J, Saksela K. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein The Embo Journal. 14: 5006-5015. DOI: 10.1002/J.1460-2075.1995.Tb00183.X |
0.708 |
|
1994 |
Sandros J, Rozdzinski E, Zheng J, Cowburn D, Tuomanen E. Lectin domains in the toxin of Bordetella pertussis: selectin mimicry linked to microbial pathogenesis Glycoconjugate Journal. 11: 501-506. PMID 7535138 DOI: 10.1007/Bf00731300 |
0.387 |
|
1994 |
Shuai K, Horvath CM, Huang LH, Qureshi SA, Cowburn D, Darnell JE. Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. Cell. 76: 821-8. PMID 7510216 DOI: 10.1016/0092-8674(94)90357-3 |
0.529 |
|
1993 |
Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 72: 779-90. PMID 7680960 DOI: 10.1016/0092-8674(93)90405-F |
0.678 |
|
1993 |
Overduin M, Mayer B, Rios CB, Baltimore D, Cowburn D. Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution. Proceedings of the National Academy of Sciences of the United States of America. 89: 11673-7. PMID 1281542 DOI: 10.1073/Pnas.89.24.11673 |
0.641 |
|
1993 |
Kuriyan J, Cowburn D. Structures of SH2 and SH3 domains. Current opinion in structural biology 1993, 3:828-837 Current Opinion in Structural Biology. 3: 828-837. DOI: 10.1016/0959-440X(93)90145-B |
0.584 |
|
1992 |
Overduin M, Rios CB, Mayer BJ, Baltimore D, Cowburn D. Three-dimensional solution structure of the src homology 2 domain of c-abl. Cell. 70: 697-704. PMID 1505033 DOI: 10.1016/0092-8674(92)90437-H |
0.63 |
|
1992 |
Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, Birge RB, Cowburn D, Hanafusa H, Mayer BJ, Overduin M, Resh MD, Rios CB, Silverman L, Kuriyan J. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides Nature. 358: 646-653. PMID 1379696 DOI: 10.1038/358646A0 |
0.78 |
|
1991 |
Koutcher JA, Sawyer RC, Kornblith AB, Stolfi RL, Martin DS, Devitt ML, Cowburn D, Young CW. In vivo monitoring of changes in 5-fluorouracil metabolism induced by methotrexate measured by 19F NMR spectroscopy. Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine. 19: 113-23. PMID 2046526 DOI: 10.1002/Mrm.1910190111 |
0.486 |
|
1991 |
Ashcroft J, Live DH, Patel DJ, Cowburn D. Heteronuclear two-dimensional 15N- and 13C-NMR studies of DNA oligomers and their netropsin complexes using indirect proton detection. Biopolymers. 31: 45-55. PMID 1851045 DOI: 10.1002/Bip.360310105 |
0.783 |
|
1990 |
Koutcher JA, Barnett D, Kornblith AB, Cowburn D, Brady TJ, Gerweck LE. Relationship of changes in pH and energy status to hypoxic cell fraction and hyperthermia sensitivity International Journal of Radiation Oncology, Biology, Physics. 18: 1429-1435. PMID 2370193 DOI: 10.1016/0360-3016(90)90318-E |
0.477 |
|
1990 |
Glushka J, Bârzu O, Sarfati RS, Kansal VK, Cowburn D. The binding of ATP and AMP to Escherichia coli adenylate kinase investigated by 1H and 15N NMR spectroscopy. Biochemical and Biophysical Research Communications. 172: 432-8. PMID 2241944 DOI: 10.1016/0006-291X(90)90691-F |
0.614 |
|
1990 |
Henderson GB, Glushka J, Cowburn D, Cerami A. Synthesis and NMR characterization of the trypanosomatid metabolite, N 1,N8-bis(glutathionyl)spermidine disulphide (trypanothione disulphide) Journal of the Chemical Society, Perkin Transactions 1. 911-914. DOI: 10.1039/P19900000911 |
0.619 |
|
1990 |
Glushka J, Lee M, Coffin S, Cowburn D. Nitrogen-15 chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin [Erratum to document cited in CA111(17):149076x] Journal of the American Chemical Society. 112: 2843-2843. DOI: 10.1021/Ja00163A081 |
0.566 |
|
1990 |
HENDERSON GB, GLUSHKA J, COWBURN D, CERAMI A. ChemInform Abstract: Synthesis and NMR Characterization of the Trypanosomatid Metabolite, N1,N8-Bis(glutathionyl)spermidine Disulfide (Trypanothione Disulfide). Cheminform. 21. DOI: 10.1002/chin.199031279 |
0.544 |
|
1989 |
Glushka J, Barany F, Cowburn D. Observation of arginyl-deoxyoligonucleotide interactions in Taq I endonuclease by detection of specific 1H NMR signals from 140kD [N eta 1, N eta 2, 15N Arg]Taq I/oligomer complexes. Biochemical and Biophysical Research Communications. 164: 88-93. PMID 2679559 DOI: 10.1016/0006-291X(89)91686-0 |
0.618 |
|
1989 |
Glushka J, Lee M, Coffin S, Cowburn D. Nitrogen-15 chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin Journal of the American Chemical Society. 111: 7716-7722. DOI: 10.1021/Ja00202A009 |
0.579 |
|
1989 |
Ashcroft J, LaPlante SR, Borer PN, Cowburn D. Sequence specific carbon-13 NMR assignment of non-protonated carbons in [d(TAGCGCTA)]2 using proton detection Journal of the American Chemical Society. 111: 363-365. DOI: 10.1021/Ja00183A054 |
0.782 |
|
1988 |
LaPlante SR, Ashcroft J, Cowburn D, Levy GC, Borer PN. 13C NMR assignments of the protonated carbons of [d(TAGCGCTA)]2 by two-dimensional proton-detected heteronuclear correlation. Journal of Biomolecular Structure & Dynamics. 5: 1089-99. PMID 3271498 DOI: 10.1080/07391102.1988.10506450 |
0.783 |
|
1988 |
LaPlante SR, Boudreau EA, Zanatta N, Levy GC, Borer PN, Ashcroft J, Cowburn D. 13C NMR of the bases of three DNA oligonucleotide duplexes: assignment methods and structural features. Biochemistry. 27: 7902-9. PMID 3207718 DOI: 10.1021/Bi00420A048 |
0.791 |
|
1987 |
Live DH, Cowburn D, Breslow E. Binding of oxytocin and 8-arginine-vasopressin to neurophysin studied by 15N NMR using magnetization transfer and indirect detection via protons. Biochemistry. 26: 6415-22. PMID 3427016 DOI: 10.1021/Bi00394A018 |
0.774 |
|
1987 |
Glushka J, Cowburn D. Assignment of nitrogen-15 NMR signals in bovine pancreatic trypsin inhibitor Journal of the American Chemical Society. 109: 7879-7881. DOI: 10.1021/Ja00259A045 |
0.582 |
|
1987 |
Koutcher J, Alfieri A, Barnett D, Cowburn D, Fuks Z, Kim J. P NMR studies of a murine fibrosarcoma: Relationship of tumor size, pH and high energy phosphates with thermal sensitivity International Journal of Radiation Oncology*Biology*Physics. 13: 117-118. DOI: 10.1016/0360-3016(87)91076-5 |
0.482 |
|
1986 |
Kubiak T, Cowburn D. Enzymatic semisynthesis of porcine despentapeptide (B26-30) insulin using unprotected desoctapeptide (B23-30) insulin as a substrate. Model studies. International Journal of Peptide and Protein Research. 27: 514-21. PMID 3525439 DOI: 10.1111/J.1399-3011.1986.Tb01050.X |
0.759 |
|
1986 |
Kubiak T, Cowburn D. Trypsin-catalysed formation of pig des-(23-63)-proinsulin from desoctapeptide-(B23-30)-insulin. The Biochemical Journal. 234: 665-70. PMID 3521594 DOI: 10.1042/Bj2340665 |
0.765 |
|
1986 |
Ortiz-Polo G, Krishnamoorthi R, Markley JL, Live DH, Davis DG, Cowburn D. Natural-abundance 15N NMR studies of Turkey ovomucoid third domain. Assignment of peptide 15N resonances to the residues at the reactive site region via proton-detected multiple-quantum coherence Journal of Magnetic Resonance (1969). 68: 303-310. DOI: 10.1016/0022-2364(86)90246-5 |
0.361 |
|
1985 |
Live DH, Kojiro CL, Cowburn D, Markley JL. Identification of proton NMR signals from the metal ligands in cadmium-substituted plastocyanin via two-dimensional multiple-quantum detection in the absence of explicitly resolved proton-cadmium-113 coupling Journal of the American Chemical Society. 107: 3043-3045. DOI: 10.1021/Ja00297A008 |
0.632 |
|
1985 |
Live D, Armitage IM, Dalgarno DC, Cowburn D. Two-dimensional 1H-113Cd chemical-shift correlation maps by 1H-detected multiple-quantum NMR in metal complexes and metalloproteins Journal of the American Chemical Society. 107: 1775-1777. DOI: 10.1021/Ja00292A062 |
0.616 |
|
1985 |
LIVE D, ARMITAGE IM, DALGARNO DC, COWBURN D. ChemInform Abstract: TWO-DIMENSIONAL PROTON-CADMIUM-113 CHEMICAL-SHIFT CORRELATION MAPS BY PROTON-DETECTED MULTIPLE-QUANTUM NMR IN METAL COMPLEXES AND METALLOPROTEINS Chemischer Informationsdienst. 16. DOI: 10.1002/chin.198530051 |
0.598 |
|
1985 |
LIVE DH, DAVIS DG, AGOSTA WC, COWBURN D. ChemInform Abstract: OBSERVATION OF 1000-FOLD ENHANCEMENT OF NITROGEN-15 NMR VIA PROTON-DETECTED MULTIQUANTUM COHERENCES: STUDIES OF LARGE PEPTIDES Chemischer Informationsdienst. 16. DOI: 10.1002/Chin.198503051 |
0.721 |
|
1984 |
Live DH, Davis DG, Agosta WC, Cowburn D. Observation of 1000-fold enhancement of 15N NMR via proton-detected multiquantum coherences: Studies of large peptides Journal of the American Chemical Society. 106: 6104-6105. DOI: 10.1021/Ja00332A071 |
0.541 |
|
1984 |
Live DH, Davis DG, Agosta WC, Cowburn D. LONG RANGE HYDROGEN BOND MEDIATED EFFECTS IN PEPTIDES: **1**5N NMR STUDY OF GRAMICIDIN S IN WATER AND ORGANIC SOLVENTS Journal of the American Chemical Society. 106: 1939-1941. DOI: 10.1021/Ja00319A006 |
0.506 |
|
1984 |
LIVE DH, DAVIS DG, AGOSTA WC, COWBURN D. ChemInform Abstract: LONG RANGE HYDROGEN BOND MEDIATED EFFECTS IN PEPTIDES: NITROGEN-15 NMR STUDY OF GRAMICIDIN S IN WATER AND ORGANIC SOLVENTS Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198427056 |
0.677 |
|
1984 |
Live DH, Davis DG, Agosta WC, Cowburn D. Long range hydrogen bond mediated effects in peptides: nitrogen-15 NMR study of gramicidin S in water and organic solvents Journal of the American Chemical Society. 106: 1939-1941. DOI: 10.1002/Chin.198427056 |
0.501 |
|
1984 |
COWBURN D, LIVE DH, FISCHMAN AJ, AGOSTA WC. ChemInform Abstract: SIDE CHAIN CONFORMATIONS OF OXYTOCIN AND VASOPRESSIN STUDIED BY NMR OBSERVATION OF ISOTOPIC ISOMERS Chemischer Informationsdienst. 15. DOI: 10.1002/Chin.198412061 |
0.717 |
|
1983 |
Engel AK, Cowburn D. Approaches to the complete determination of the rotation axes and flexibility in the methylene segments of phospholipids: deuterium, carbon-13, and proton NMR studies of dipalmitoyl phosphatidyl choline. Journal of Biomolecular Structure & Dynamics. 1: 319-35. PMID 6400876 DOI: 10.1080/07391102.1983.10507442 |
0.53 |
|
1983 |
Cowburn D, Live DH, Fischman AJ, Agosta WC. Side chain conformations of oxytoxin and vasopressin studied by NMR observation of isotopic isomers Journal of the American Chemical Society. 105: 7435-7442. DOI: 10.1021/Ja00363A038 |
0.718 |
|
1983 |
Davis DG, Agosta WC, Cowburn D. Long-range proton-nitrogen spin coupling constants via polarization-enhanced two-dimensional 15N NMR Journal of the American Chemical Society. 105: 6189-6190. DOI: 10.1021/Ja00357A058 |
0.509 |
|
1983 |
Davis DG, Live DH, Agosta WC, Cowburn D. Spin connectivities to protons in 13C and 15N NMR spectra by selective suppression Journal of Magnetic Resonance (1969). 53: 350-354. DOI: 10.1016/0022-2364(83)90038-0 |
0.525 |
|
1983 |
DAVIS DG, AGOSTA WC, COWBURN D. ChemInform Abstract: LONG-RANGE PROTON-NITROGEN SPIN COUPLING CONSTANTS VIA POLARIZATION-ENHANCED TWO-DIMENSIONAL NITROGEN-15 NMR Chemischer Informationsdienst. 14. DOI: 10.1002/chin.198352044 |
0.451 |
|
1983 |
Davis DG, Agosta WC, Cowburn D. Long-range proton-nitrogen spin coupling constants via polarization-enhanced two-dimensional nitrogen-15 NMR Journal of the American Chemical Society. 105: 6189-6190. DOI: 10.1002/Chin.198352044 |
0.512 |
|
1982 |
Live DH, Davis DG, Agosta WC, Cowburn D. Conformations of side chains of somatostatin very high field proton NMR studies Organic Magnetic Resonance. 19: 211-215. DOI: 10.1002/Mrc.1270190410 |
0.542 |
|
1981 |
Engel AK, Cowburn D. The origin of multiple quadrupole couplings in the deuterium NMR spectra of the 2 chain of 1,2 dipalmitoyl-sn-glycero-3-phosphorylcholine. Febs Letters. 126: 169-71. PMID 6894577 DOI: 10.1016/0014-5793(81)80233-5 |
0.534 |
|
1981 |
Krauss EM, Cowburn D. Hydrogen--deuterium exchange kinetics of the amide protons of oxytocin studied by nuclear magnetic resonance. Biochemistry. 20: 671-9. PMID 6260137 DOI: 10.1021/Bi00507A001 |
0.318 |
|
1981 |
Krauss EM, Cowburn D. Anomalous exchange kinetics of peptide amide protons in aqueous solutions. International Journal of Peptide and Protein Research. 17: 42-7. PMID 6164656 DOI: 10.1111/J.1399-3011.1981.Tb01966.X |
0.307 |
|
1980 |
Fischman AJ, Live DH, Wyssbrod HR, Agosta WC, Cowburn D. Torsion angles in the cystine bridge of oxytocin in aqueous solution. Measurements of circumjacent vicinal couplings between proton, carbon-13, and nitrogen-15 Journal of the American Chemical Society. 102: 2533-2539. DOI: 10.1021/Ja00528A004 |
0.7 |
|
1980 |
FISCHMAN AJ, LIVE DH, WYSSBROD HR, AGOSTA WC, COWBURN D. ChemInform Abstract: TORSION ANGLES IN THE CYSTINE BRIDGE OF OXYTOCIN IN AQUEOUS SOLUTION. MEASUREMENTS OF CIRCUMJACENT VICINAL COUPLINGS BETWEEN PROTON, CARBON-13, AND NITROGEN-15 Chemischer Informationsdienst. 11. DOI: 10.1002/chin.198029344 |
0.68 |
|
1979 |
Live DH, Wyssbrod HR, Fischman AJ, Agosta WC, Bradley CH, Cowburn D. A study of the peptide hormone oxytocin and of prolylleucylglycinamide by nitrogen-15 NMR Journal of the American Chemical Society. 101: 474-479. DOI: 10.1021/Ja00496A035 |
0.701 |
|
1978 |
Fischman AJ, Riemen MW, Cowburn D. Averaging of phi2 and phi3 in [5-leucyl]-enkephalin: NMR study of two isotopic isomers. Febs Letters. 94: 236-40. PMID 700146 DOI: 10.1016/0014-5793(78)80945-4 |
0.304 |
|
1978 |
Fischman AJ, Wyssbrod HR, Agosta WC, Cowburn D. Heteronuclear vicinal coupling constants and site-specific isotopic substitution in the investigation of rotational isomerism in leucine Journal of the American Chemical Society. 100: 54-58. DOI: 10.1021/Ja00469A009 |
0.497 |
|
1978 |
FISCHMAN AJ, WYSSBROD HR, AGOSTA WC, COWBURN D. ChemInform Abstract: HETERONUCLEAR VICINAL COUPLING CONSTANTS AND SITE-SPECIFIC ISOTOPIC SUBSTITUTION IN THE INVESTIGATION OF ROTATIONAL ISOMERISM IN LEUCINE Chemischer Informationsdienst. 9. DOI: 10.1002/Chin.197817059 |
0.498 |
|
1978 |
LIVE DH, AGOSTA WC, COWBURN D. ChemInform Abstract: A RAPID, EFFICIENT SYNTHESIS OF OXYTOCIN AND (8-ARGININE)-VASOPRESSIN. COMPARISON OF BENZYL, P-METHOXYBENZYL, AND P-METHYLBENZYL AS PROTECTING GROUPS FOR CYSTEINE Chemischer Informationsdienst. 9. DOI: 10.1002/Chin.197810337 |
0.674 |
|
1977 |
Live DH, Agosta WC, Cowburn D. A rapid, efficient synthesis of oxytocin and 8-arginine-vasopressin. Comparison of benzyl, p-methoxybenzyl, and p-methylbenzyl as protecting groups for cysteine. The Journal of Organic Chemistry. 42: 3556-61. PMID 915577 DOI: 10.1021/Jo00442A025 |
0.673 |
|
1977 |
Wyssbrod HR, Ballardin A, Schwartz IL, Walter R, Van Binst G, Gibbons WA, Agosta WC, Field FH, Cowburn D. Side chain torsional angles and rotational isomerism of oxytocin in aqueous solution. Journal of the American Chemical Society. 99: 5273-6. PMID 886105 DOI: 10.1002/Chin.197745081 |
0.687 |
|
1977 |
Fischman AJ, Wyssbrod HR, Agosta WC, Field FH, Gibbons WA, Cowburn D. Rotational isomerism in leucine: proton magnetic resonance study of [gamma-2H]leucine and thermodynamic analysis. Journal of the American Chemical Society. 99: 2953-7. PMID 850043 DOI: 10.1021/Ja00451A017 |
0.701 |
|
1977 |
Wouters JM, Petersson GA, Agosta WC, Field FH, Gibbons WA, Wyssbrod H, Cowburn D. Reference lineshape adjusted difference NMR spectroscopy. II. experimental verification Journal of Magnetic Resonance (1969). 28: 93-104. DOI: 10.1016/0022-2364(77)90259-1 |
0.709 |
|
1977 |
WYSSBROD HR, BALLARDIN A, SCHWARTZ IL, WALTER R, VAN BINST G, GIBBONS WA, AGOSTA WC, FIELD FH, COWBURN D. ChemInform Abstract: SIDE CHAIN TORSIONAL ANGLES AND ROTATIONAL ISOMERISM OF OXYTOCIN IN AQUEOUS SOLUTION Chemischer Informationsdienst. 8. DOI: 10.1002/chin.197745081 |
0.578 |
|
1977 |
FISCHMAN AJ, WYSSBROD HR, AGOSTA WC, FIELD FH, GIBBONS WA, COWBURN D. ChemInform Abstract: ROTATIONAL ISOMERISM IN LEUCINE- PROTON MAGNETIC RESONANCE STUDY OF (Γ-2H)LEUCINE AND THERMODYNAMIC ANALYSIS Chemischer Informationsdienst. 8: no-no. DOI: 10.1002/Chin.197729070 |
0.631 |
|
1975 |
Craig LC, Cowburn D, Bleich H. Methods for the study of the conformation of small peptide hormones and antibiotics in solution. Annual Review of Biochemistry. 44: 477-90. PMID 1094917 DOI: 10.1146/Annurev.Bi.44.070175.002401 |
0.54 |
|
1975 |
Stoner E, Cowburn D, Craig LC. Volatile metabolites in plasma Analytical Chemistry. 47: 344-346. DOI: 10.1021/Ac60352A004 |
0.474 |
|
1973 |
Karlin A, Cowburn D. The affinity-labeling of partially purified acetylcholine receptor from electric tissue of Electrophorus. Proceedings of the National Academy of Sciences of the United States of America. 70: 3636-40. PMID 4519650 DOI: 10.1073/Pnas.70.12.3636 |
0.53 |
|
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