Year |
Citation |
Score |
2024 |
Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. Elife. 12. PMID 38526948 DOI: 10.7554/eLife.90259 |
0.56 |
|
2022 |
Smyth S, Zhang Z, Bah A, Tsangaris TE, Dawson J, Forman-Kay JD, Gradinaru CC. Multisite Phosphorylation and Binding Alter Conformational Dynamics of the 4E-BP2 Protein. Biophysical Journal. PMID 35841142 DOI: 10.1016/j.bpj.2022.07.015 |
0.373 |
|
2020 |
Dawson JE, Bah A, Zhang Z, Vernon RM, Lin H, Chong PA, Vanama M, Sonenberg N, Gradinaru CC, Forman-Kay JD. Non-cooperative 4E-BP2 folding with exchange between eIF4E-binding and binding-incompatible states tunes cap-dependent translation inhibition. Nature Communications. 11: 3146. PMID 32561718 DOI: 10.1038/S41467-020-16783-8 |
0.452 |
|
2019 |
Tsang B, Arsenault J, Vernon RM, Lin H, Sonenberg N, Wang LY, Bah A, Forman-Kay JD. Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation. Proceedings of the National Academy of Sciences of the United States of America. PMID 30765518 DOI: 10.1073/Pnas.1814385116 |
0.354 |
|
2018 |
Yuwen T, Bah A, Brady JP, Ferrage F, Bouvignies G, Kay LE. Measuring Solvent Hydrogen Exchange Rates by Multi-Frequency Excitation N CEST. The Journal of Physical Chemistry. B. PMID 30179470 DOI: 10.1021/Acs.Jpcb.8B06820 |
0.322 |
|
2018 |
Vernon RM, Chong PA, Tsang B, Kim TH, Bah A, Farber P, Lin H, Forman-Kay JD. Pi-Pi contacts are an overlooked protein feature relevant to phase separation. Elife. 7. PMID 29424691 DOI: 10.7554/Elife.31486 |
0.418 |
|
2018 |
Vernon RM, Chong PA, Tsang B, Kim TH, Bah A, Farber P, Lin H, Forman-Kay JD. Author response: Pi-Pi contacts are an overlooked protein feature relevant to phase separation Elife. DOI: 10.7554/Elife.31486.045 |
0.302 |
|
2018 |
Smyth S, Zhang Z, Bah A, Forman-Kay JD, Gradinaru CC. Probing the Conformational Dynamics of the Disordered 4E-BP2 Protein in Different Phosphorylation States using Single-Molecule Fluorescence Biophysical Journal. 114: 368a. DOI: 10.1016/J.Bpj.2017.11.2038 |
0.362 |
|
2017 |
Brady JP, Farber PJ, Sekhar A, Lin YH, Huang R, Bah A, Nott TJ, Chan HS, Baldwin AJ, Forman-Kay JD, Kay LE. Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28894006 DOI: 10.1073/Pnas.1706197114 |
0.419 |
|
2017 |
Scanlon DP, Bah A, Krzeminski M, Zhang W, Leduc-Pessah HL, Dong YN, Forman-Kay JD, Salter MW. An evolutionary switch in ND2 enables Src kinase regulation of NMDA receptors. Nature Communications. 8: 15220. PMID 28508887 DOI: 10.1038/Ncomms15220 |
0.331 |
|
2017 |
Csizmok V, Orlicky S, Cheng J, Song J, Bah A, Delgoshaie N, Lin H, Mittag T, Sicheri F, Chan HS, Tyers M, Forman-Kay JD. An allosteric conduit facilitates dynamic multisite substrate recognition by the SCF(Cdc4) ubiquitin ligase. Nature Communications. 8: 13943. PMID 28045046 DOI: 10.1038/Ncomms13943 |
0.424 |
|
2017 |
Zhang Z, Bah A, Forman-Kay JD, Gradinaru CC. Interplay Among Binding, Phosphorylation and Denaturation in Disordered 4E-BP2 as Probed by Single Molecule Fluorescence Biophysical Journal. 112: 510a. DOI: 10.1016/J.Bpj.2016.11.2756 |
0.357 |
|
2016 |
Bah A, Forman-Kay JD. Modulation of Intrinsically Disordered Protein Function by Post-Translational Modifications. The Journal of Biological Chemistry. PMID 26851279 DOI: 10.1074/Jbc.R115.695056 |
0.365 |
|
2016 |
Zhang Z, Bah A, Sajjad H, Forman-Kay JD, Gradinaru CC. Single-Molecule Dissection of the Conformations, Dynamics and Binding of the Disordered 4E-BP2 Protein Biophysical Journal. 110: 556a-557a. DOI: 10.1016/J.Bpj.2015.11.2976 |
0.467 |
|
2015 |
Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. Nature. 519: 106-9. PMID 25533957 DOI: 10.1038/Nature13999 |
0.452 |
|
2014 |
Bah A, Forman-Kay J. Phosphorylated 4E-BP2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19905 |
0.326 |
|
2013 |
Lukhele S, Bah A, Lin H, Sonenberg N, Forman-Kay JD. Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface. Structure (London, England : 1993). 21: 2186-96. PMID 24207126 DOI: 10.1016/J.Str.2013.08.030 |
0.435 |
|
2011 |
Bouvignies G, Vallurupalli P, Hansen DF, Correia BE, Lange O, Bah A, Vernon RM, Dahlquist FW, Baker D, Kay LE. Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature. 477: 111-4. PMID 21857680 DOI: 10.1038/Nature10349 |
0.327 |
|
2011 |
Pozzi N, Chen R, Chen Z, Bah A, Di Cera E. Rigidification of the autolysis loop enhances Na(+) binding to thrombin. Biophysical Chemistry. 159: 6-13. PMID 21536369 DOI: 10.1016/J.Bpc.2011.04.003 |
0.604 |
|
2010 |
Vogt AD, Bah A, Di Cera E. Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa. The Journal of Physical Chemistry. B. 114: 16125-30. PMID 20809655 DOI: 10.1021/Jp105502C |
0.611 |
|
2009 |
Niu W, Chen Z, Bush-Pelc LA, Bah A, Gandhi PS, Di Cera E. Mutant N143P reveals how Na+ activates thrombin. The Journal of Biological Chemistry. 284: 36175-85. PMID 19846563 DOI: 10.1074/Jbc.M109.069500 |
0.597 |
|
2009 |
Bah A, Carrell CJ, Chen Z, Gandhi PS, Di Cera E. Stabilization of the E* form turns thrombin into an anticoagulant. The Journal of Biological Chemistry. 284: 20034-40. PMID 19473969 DOI: 10.1074/Jbc.M109.012344 |
0.603 |
|
2008 |
Papaconstantinou ME, Gandhi PS, Chen Z, Bah A, Di Cera E. Na+ binding to meizothrombin desF1. Cellular and Molecular Life Sciences : Cmls. 65: 3688-97. PMID 18854941 DOI: 10.1007/S00018-008-8502-7 |
0.628 |
|
2008 |
Papaconstantinou ME, Bah A, Di Cera E. Role of the A chain in thrombin function. Cellular and Molecular Life Sciences : Cmls. 65: 1943-7. PMID 18470478 DOI: 10.1007/S00018-008-8179-Y |
0.574 |
|
2007 |
Gianni S, Ivarsson Y, Bah A, Bush-Pelc LA, Di Cera E. Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics. Biophysical Chemistry. 131: 111-4. PMID 17935858 DOI: 10.1016/J.Bpc.2007.09.009 |
0.572 |
|
2007 |
Bah A, Chen Z, Bush-Pelc LA, Mathews FS, Di Cera E. Crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4. Proceedings of the National Academy of Sciences of the United States of America. 104: 11603-8. PMID 17606903 DOI: 10.1073/Pnas.0704409104 |
0.595 |
|
2007 |
Di Cera E, Page MJ, Bah A, Bush-Pelc LA, Garvey LC. Thrombin allostery. Physical Chemistry Chemical Physics : Pccp. 9: 1291-306. PMID 17347701 DOI: 10.1039/b616819a |
0.529 |
|
2006 |
Bah A, Garvey LC, Ge J, Di Cera E. Rapid kinetics of Na+ binding to thrombin. The Journal of Biological Chemistry. 281: 40049-56. PMID 17074754 DOI: 10.1074/Jbc.M608600200 |
0.622 |
|
2006 |
Pineda AO, Chen ZW, Bah A, Garvey LC, Mathews FS, Di Cera E. Crystal structure of thrombin in a self-inhibited conformation. The Journal of Biological Chemistry. 281: 32922-8. PMID 16954215 DOI: 10.1074/Jbc.M605530200 |
0.623 |
|
Show low-probability matches. |