Year |
Citation |
Score |
2018 |
Daffern N, Chen Z, Zhang Y, Pick L, Radhakrishnan I. Solution NMR Studies of the Ligand-Binding Domain of an Orphan Nuclear Receptor Reveals a Dynamic Helix in the Ligand-Binding Pocket. Biochemistry. PMID 29547262 DOI: 10.1021/Acs.Biochem.8B00069 |
0.304 |
|
2015 |
Clark MD, Zhang Y, Radhakrishnan I. Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex. Journal of Molecular Biology. PMID 26522936 DOI: 10.1016/J.Jmb.2015.10.018 |
0.343 |
|
2015 |
Clark M, Kumar GS, Marcum R, Luo Q, Zhang Y, Radhakrishnan I. Molecular Basis for the Mechanism of Constitutive CBP/p300 Coactivator Recruitment by CRTC1-MAML2 and its Implications in cAMP Signaling. Biochemistry. PMID 26274502 DOI: 10.1021/Acs.Biochem.5B00332 |
0.342 |
|
2015 |
Clark MD, Marcum R, Graveline R, Chan CW, Xie T, Chen Z, Ding Y, Zhang Y, Mondragón A, David G, Radhakrishnan I. Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex. Proceedings of the National Academy of Sciences of the United States of America. PMID 26124119 DOI: 10.1073/Pnas.1504021112 |
0.314 |
|
2015 |
Xie T, Zmyslowski AM, Zhang Y, Radhakrishnan I. Structural Basis for Multi-specificity of MRG Domains. Structure (London, England : 1993). 23: 1049-57. PMID 25960410 DOI: 10.1016/J.Str.2015.03.020 |
0.336 |
|
2015 |
Xie T, Zmysloski A, Zhang Y, Radhakrishnan I. Solution structure of the MRG15-MRGBP complex Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2N1D/Pdb |
0.323 |
|
2012 |
Xie T, Graveline R, Kumar GS, Zhang Y, Krishnan A, David G, Radhakrishnan I. Structural basis for molecular interactions involving MRG domains: implications in chromatin biology. Structure (London, England : 1993). 20: 151-60. PMID 22244764 DOI: 10.1016/J.Str.2011.10.019 |
0.353 |
|
2011 |
Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I. Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding. The Journal of Biological Chemistry. 286: 27814-24. PMID 21676866 DOI: 10.1074/Jbc.M111.252494 |
0.363 |
|
2011 |
Kumar GS, Xie T, Zhang Y, Radhakrishnan I. Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex. Journal of Molecular Biology. 408: 987-1000. PMID 21440557 DOI: 10.1016/J.Jmb.2011.03.043 |
0.317 |
|
2011 |
Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I. solution structure of the mSin3A PAH3-SAP30 SID complex Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Ld7/Pdb |
0.324 |
|
2011 |
Kumar GS, Xie T, Zhang Y, Radhakrishnan I. Solution structure of Pf1 SID1-mSin3A PAH2 Complex Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2L9S/Pdb |
0.321 |
|
2011 |
Xie T, Patel A, Krishnan A, Zhang Y, Radhakrishnan I. Structure-Function Analysis of MRG15, a Chromatin-Targeting Protein Invovled in Cell Growth and Aging Biophysical Journal. 100: 603a. DOI: 10.1016/J.Bpj.2010.12.3472 |
0.346 |
|
2011 |
Ganesan SK, Xie T, Velagapudi C, Zhang Y, Radhakrishnan I. Structural Analysis of the Pf1 Subunit of the Sin3S/Rpd3S Complex and its Implications in Chromatin Targeting and Complex Assembly Biophysical Journal. 100: 603a. DOI: 10.1016/J.Bpj.2010.12.3471 |
0.323 |
|
2009 |
Bhattacharya A, Kurochkin AV, Yip GN, Zhang Y, Bertelsen EB, Zuiderweg ER. Allostery in Hsp70 chaperones is transduced by subdomain rotations. Journal of Molecular Biology. 388: 475-90. PMID 19361428 DOI: 10.1016/J.Jmb.2009.01.062 |
0.323 |
|
2007 |
Sommerhalter M, Zhang Y, Rosenzweig AC. Solution structure of the COMMD1 N-terminal domain. Journal of Molecular Biology. 365: 715-21. PMID 17097678 DOI: 10.1016/J.Jmb.2006.10.030 |
0.345 |
|
2006 |
Zhang Y, Zhang Z, Demeler B, Radhakrishnan I. Coupled unfolding and dimerization by the PAH2 domain of the mammalian Sin3A corepressor. Journal of Molecular Biology. 360: 7-14. PMID 16813833 DOI: 10.1016/J.Jmb.2006.04.069 |
0.332 |
|
2005 |
Revington M, Zhang Y, Yip GN, Kurochkin AV, Zuiderweg ER. NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone. Journal of Molecular Biology. 349: 163-83. PMID 15876376 DOI: 10.1016/J.Jmb.2005.03.033 |
0.321 |
|
2004 |
Zhang Y, Zuiderweg ER. The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains. Proceedings of the National Academy of Sciences of the United States of America. 101: 10272-7. PMID 15232009 DOI: 10.1073/Pnas.0401313101 |
0.334 |
|
2004 |
Hou L, Shao H, Zhang Y, Li H, Menon NK, Neuhaus EB, Brewer JM, Byeon IJ, Ray DG, Vitek MP, Iwashita T, Makula RA, Przybyla AB, Zagorski MG. Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. Journal of the American Chemical Society. 126: 1992-2005. PMID 14971932 DOI: 10.1021/Ja036813F |
0.669 |
|
2004 |
Zagorski MG, Hou L, Shao H, Zhang Y, Menon N. P1-200 Solution NMR studies of the AB(1-40) and AB(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation Neurobiology of Aging. 25: S153. DOI: 10.1016/S0197-4580(04)80513-X |
0.666 |
|
2001 |
Poeggeler B, Miravalle L, Zagorski MG, Wisniewski T, Chyan YJ, Zhang Y, Shao H, Bryant-Thomas T, Vidal R, Frangione B, Ghiso J, Pappolla MA. Melatonin reverses the profibrillogenic activity of apolipoprotein E4 on the Alzheimer amyloid Abeta peptide. Biochemistry. 40: 14995-5001. PMID 11732920 DOI: 10.1021/Bi0114269 |
0.631 |
|
2001 |
Zeng H, Zhang Y, Peng L, Shao H, Menon NK, Yang J, Salomon AR, Freidland RP, Zagorski MG. Nicotine and amyloid formation. Biological Psychiatry. 49: 248-57. PMID 11230876 DOI: 10.1016/S0006-3223(00)01111-2 |
0.652 |
|
2000 |
Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sönnichsen FD. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. The Journal of Biological Chemistry. 275: 33650-4. PMID 10954699 DOI: 10.1074/Jbc.C000483200 |
0.606 |
|
2000 |
Zagorski MG, Shao H, Ma K, Yang J, Li H, Zeng H, Zhang Y, Papolla M. Amyloid AB (1–40) and AB(1–42) adopt remarkably stable, monomeric, and extended structures in water solution at neutral pH Neurobiology of Aging. 21: 10-11. DOI: 10.1016/S0197-4580(00)82724-4 |
0.61 |
|
1999 |
Ma K, Clancy EL, Zhang Y, Ray DG, Wollenberg K, Zagorski MG. Residue-specific pK(a) measurements of the β-peptide and mechanism of pH-induced amyloid formation Journal of the American Chemical Society. 121: 8698-8706. DOI: 10.1021/Ja990864O |
0.609 |
|
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