Year |
Citation |
Score |
2017 |
Stiers KM, Xu J, Lee Y, Addison ZR, Van Doren SR, Beamer LJ. Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from . Acs Omega. 2: 8445-8452. PMID 31457382 DOI: 10.1021/acsomega.7b01490 |
0.381 |
|
2017 |
Xu J, Sarma AVS, Wei Y, Beamer LJ, Van Doren SR. Multiple Ligand-Bound States of a Phosphohexomutase Revealed by Principal Component Analysis of NMR Peak Shifts. Scientific Reports. 7: 5343. PMID 28706231 DOI: 10.1038/s41598-017-05557-w |
0.321 |
|
2017 |
Fulcher YG, Prior SH, Masuko S, Li L, Pu D, Zhang F, Linhardt RJ, Van Doren SR. Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7. Structure (London, England : 1993). PMID 28648610 DOI: 10.1016/J.Str.2017.05.019 |
0.379 |
|
2015 |
Zhao Y, Marcink TC, Sanganna Gari RR, Marsh BP, King GM, Stawikowska R, Fields GB, Van Doren SR. Transient collagen triple helix binding to a key metalloproteinase in invasion and development. Structure (London, England : 1993). 23: 257-69. PMID 25651059 DOI: 10.1016/J.Str.2014.11.021 |
0.432 |
|
2015 |
Xu J, Lee Y, Beamer LJ, Van Doren SR. Phosphorylation in the catalytic cleft stabilizes and attracts domains of a phosphohexomutase. Biophysical Journal. 108: 325-37. PMID 25606681 DOI: 10.1016/j.bpj.2014.12.003 |
0.437 |
|
2014 |
Wei Y, Marcink TC, Xu J, Sirianni AG, Sarma AV, Prior SH, Beamer LJ, Van Doren SR. Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface. Biomolecular Nmr Assignments. 8: 329-33. PMID 23893395 DOI: 10.1007/S12104-013-9511-5 |
0.465 |
|
2012 |
Sarma AV, Anbanandam A, Kelm A, Mehra-Chaudhary R, Wei Y, Qin P, Lee Y, Berjanskii MV, Mick JA, Beamer LJ, Van Doren SR. Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect. Biochemistry. 51: 807-19. PMID 22242625 DOI: 10.1021/Bi201609N |
0.693 |
|
2011 |
Fulcher YG, Van Doren SR. Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation. Biochemistry. 50: 9488-99. PMID 21967233 DOI: 10.1021/bi2009807 |
0.345 |
|
2010 |
Palmier MO, Fulcher YG, Bhaskaran R, Duong VQ, Fields GB, Van Doren SR. NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices. The Journal of Biological Chemistry. 285: 30918-30. PMID 20663866 DOI: 10.1074/Jbc.M110.136903 |
0.328 |
|
2010 |
Schramm AM, Karr D, Mehra-Chaudhary R, Van Doren SR, Furdui CM, Beamer LJ. Breaking the covalent connection: Chain connectivity and the catalytic reaction of PMM/PGM. Protein Science : a Publication of the Protein Society. 19: 1235-42. PMID 20512975 DOI: 10.1002/Pro.402 |
0.4 |
|
2008 |
Liang X, Van Doren SR. Mechanistic insights into phosphoprotein-binding FHA domains. Accounts of Chemical Research. 41: 991-9. PMID 18656966 DOI: 10.1021/ar700148u |
0.507 |
|
2007 |
Bhaskaran R, Palmier MO, Bagegni NA, Liang X, Van Doren SR. Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment. Journal of Molecular Biology. 374: 1333-44. PMID 17997411 DOI: 10.1016/j.jmb.2007.10.028 |
0.349 |
|
2007 |
Ding Z, Wang H, Liang X, Morris ER, Gallazzi F, Pandit S, Skolnick J, Walker JC, Van Doren SR. Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase. Biochemistry. 46: 2684-96. PMID 17302430 DOI: 10.1021/Bi061763N |
0.643 |
|
2006 |
Liang X, Lee GI, Van Doren SR. Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase. Journal of Molecular Biology. 364: 225-40. PMID 17007879 DOI: 10.1016/J.Jmb.2006.08.090 |
0.599 |
|
2006 |
Coaker G, Zhu G, Ding Z, Van Doren SR, Staskawicz B. Eukaryotic cyclophilin as a molecular switch for effector activation. Molecular Microbiology. 61: 1485-96. PMID 16968222 DOI: 10.1111/J.1365-2958.2006.05335.X |
0.538 |
|
2006 |
Garimella R, Liu X, Qiao W, Liang X, Zuiderweg ER, Riley MI, Van Doren SR. Hsc70 contacts helix III of the J domain from polyomavirus T antigens: addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb. Biochemistry. 45: 6917-29. PMID 16734427 DOI: 10.1021/bi060411d |
0.41 |
|
2005 |
Ding Z, Lee GI, Liang X, Gallazzi F, Arunima A, Van Doren SR. PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase. Biochemistry. 44: 10119-34. PMID 16042389 DOI: 10.1021/Bi050414A |
0.693 |
|
2003 |
Lee GI, Ding Z, Walker JC, Van Doren SR. NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase. Proceedings of the National Academy of Sciences of the United States of America. 100: 11261-6. PMID 14500786 DOI: 10.1073/Pnas.2031918100 |
0.707 |
|
2003 |
Lee GI, Li J, Walker JC, Van Doren SR. 1H, 13C and 15N resonance assignments of the kinase-interacting FHA domain of Arabidopsis thaliana kinase-associated protein phosphatase. Journal of Biomolecular Nmr. 25: 253-4. PMID 12652139 DOI: 10.1023/A:1022806811627 |
0.574 |
|
2003 |
Arumugam S, Gao G, Patton BL, Semenchenko V, Brew K, Van Doren SR. Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3. Journal of Molecular Biology. 327: 719-34. PMID 12634064 DOI: 10.1016/S0022-2836(03)00180-3 |
0.382 |
|
2002 |
Berjanskii M, Riley M, Van Doren SR. Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in ps to ns and micros to ms. Journal of Molecular Biology. 321: 503-16. PMID 12162962 DOI: 10.1016/S0022-2836(02)00631-9 |
0.678 |
|
2002 |
Leeper TC, Martin MB, Kim H, Cox S, Semenchenko V, Schmidt FJ, Van Doren SR. Structure of the UGAGAU hexaloop that braces Bacillus RNase P for action. Nature Structural Biology. 9: 397-403. PMID 11927952 DOI: 10.1038/Nsb775 |
0.625 |
|
2000 |
Li J, Lee GI, Van Doren SR, Walker JC. The FHA domain mediates phosphoprotein interactions. Journal of Cell Science. 113: 4143-9. PMID 11069759 |
0.636 |
|
2000 |
Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR. NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens. The Journal of Biological Chemistry. 275: 36094-103. PMID 10950962 DOI: 10.1074/Jbc.M006572200 |
0.708 |
|
2000 |
Gao G, Semenchenko V, Arumugam S, Van Doren SR. Tissue inhibitor of metalloproteinases-1 undergoes microsecond to millisecond motions at sites of matrix metalloproteinase-induced fit Journal of Molecular Biology. 301: 537-552. PMID 10926526 DOI: 10.1006/jmbi.2000.3976 |
0.311 |
|
2000 |
Wu B, Arumugam S, Gao G, Lee GI, Semenchenko V, Huang W, Brew K, Van Doren SR. NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases. Journal of Molecular Biology. 295: 257-68. PMID 10623524 DOI: 10.1006/Jmbi.1999.3362 |
0.609 |
|
1998 |
Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR. TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe Biochemistry. 37: 9650-9657. PMID 9657677 DOI: 10.1021/Bi980128H |
0.651 |
|
1996 |
Huang W, Suzuki K, Nagase H, Arumugam S, Van Doren SR, Brew K. Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in E. coli Febs Letters. 384: 155-161. PMID 8612814 DOI: 10.1016/0014-5793(96)00304-3 |
0.4 |
|
1995 |
Van Doren SR, Kurochkin AV, Hu W, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER. Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Protein Science : a Publication of the Protein Society. 4: 2487-98. PMID 8580839 DOI: 10.1002/pro.5560041205 |
0.445 |
|
1993 |
Van Doren SR, Kurochkin AV, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER. Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments. Biochemistry. 32: 13109-22. PMID 8241165 DOI: 10.1021/bi00211a021 |
0.357 |
|
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