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Mark E. Bowen - Publications

Affiliations: 
Biochemistry and Structural Biology Stony Brook University, Stony Brook, NY, United States 
Area:
Biochemistry, General Biophysics
Website:
https://renaissance.stonybrookmedicine.edu/neurobiology/gradprogram/faculty/bowen
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23 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Basak S, Saikia N, Kwun D, Choi UB, Ding F, Bowen ME. Different Forms of Disorder in NMDA-Sensitive Glutamate Receptor Cytoplasmic Domains Are Associated with Differences in Condensate Formation. Biomolecules. 13. PMID 36671389 DOI: 10.3390/biom13010004  0.657
2022 Hamilton GL, Saikia N, Basak S, Welcome FS, Wu F, Kubiak J, Zhang C, Hao Y, Seidel CAM, Ding F, Sanabria H, Bowen ME.. Fuzzy supertertiary interactions within PSD-95 enable ligand binding Elife Sciences. 11: e77242. PMID 36069777 DOI: 10.7554/eLife.77242  0.662
2022 Chen B, Basak S, Chen P, Zhang C, Perry K, Tian S, Yu C, Dong M, Huang L, Bowen ME, Jin R. Structure and conformational dynamics of toxin A. Life Science Alliance. 5. PMID 35292538 DOI: 10.26508/lsa.202201383  0.652
2020 Basak S, Sakia N, Dougherty L, Guo Z, Wu F, Mindlin F, Lary JW, Cole JL, Ding F, Bowen ME. Probing interdomain linkers and protein supertertiary structure in vitro and in live cells with fluorescent protein resonance energy transfer. Journal of Molecular Biology. 166793. PMID 33388290 DOI: 10.1016/j.jmb.2020.166793  0.657
2019 Chen P, Lam KH, Liu Z, Mindlin FA, Chen B, Gutierrez CB, Huang L, Zhang Y, Hamza T, Feng H, Matsui T, Bowen ME, Perry K, Jin R. Structure of the full-length Clostridium difficile toxin B. Nature Structural & Molecular Biology. PMID 31308519 DOI: 10.2210/Pdb6Oq6/Pdb  0.344
2019 Choi UB, Sanabria H, Smirnova T, Bowen ME, Weninger KR. Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins. Biomolecules. 9. PMID 30909517 DOI: 10.3390/biom9030114  0.383
2018 Yanez Orozco IS, Mindlin FA, Ma J, Wang B, Levesque B, Spencer M, Rezaei Adariani S, Hamilton G, Ding F, Bowen ME, Sanabria H. Identifying weak interdomain interactions that stabilize the supertertiary structure of the N-terminal tandem PDZ domains of PSD-95. Nature Communications. 9: 3724. PMID 30214057 DOI: 10.1038/S41467-018-06133-0  0.423
2014 McCann JJ, Choi UB, Bowen ME. Reconstitution of multivalent PDZ domain binding to the scaffold protein PSD-95 reveals ternary-complex specificity of combinatorial inhibition. Structure (London, England : 1993). 22: 1458-66. PMID 25220472 DOI: 10.1016/J.Str.2014.08.006  0.347
2013 Choi UB, Kazi R, Stenzoski N, Wollmuth LP, Uversky VN, Bowen ME. Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartate-sensitive glutamate receptor. The Journal of Biological Chemistry. 288: 22506-15. PMID 23782697 DOI: 10.1074/Jbc.M113.477810  0.378
2012 McCann JJ, Zheng L, Rohrbeck D, Felekyan S, Kühnemuth R, Sutton RB, Seidel CA, Bowen ME. Supertertiary structure of the synaptic MAGuK scaffold proteins is conserved. Proceedings of the National Academy of Sciences of the United States of America. 109: 15775-80. PMID 23019361 DOI: 10.1073/Pnas.1200254109  0.469
2012 Choi UB, Weninger KR, Bowen ME. Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics. Methods in Molecular Biology (Clifton, N.J.). 896: 3-20. PMID 22821514 DOI: 10.1007/978-1-4614-3704-8_1  0.396
2012 McCann JJ, Sutton RB, Bowen ME. Structural Modeling of PSD-95 and other MAGUKs using Single-Molecule FRET Biophysical Journal. 102: 445a. DOI: 10.1016/J.Bpj.2011.11.2438  0.393
2011 Choi UB, Xiao S, Wollmuth LP, Bowen ME. Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein. The Journal of Biological Chemistry. 286: 29904-12. PMID 21712388 DOI: 10.1074/Jbc.M111.258897  0.32
2011 McCann JJ, Zheng L, Chiantia S, Bowen ME. Domain orientation in the N-Terminal PDZ tandem from PSD-95 is maintained in the full-length protein. Structure (London, England : 1993). 19: 810-20. PMID 21645852 DOI: 10.1016/J.Str.2011.02.017  0.472
2011 Choi UB, McCann JJ, Weninger KR, Bowen ME. Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. Structure (London, England : 1993). 19: 566-76. PMID 21481779 DOI: 10.1016/J.Str.2011.01.011  0.414
2011 Choi UB, Bowen ME. Native State Conformational Dynamics of Disordered Protein Respond to Chemical Environment Biophysical Journal. 100: 61a. DOI: 10.1016/J.Bpj.2010.12.529  0.461
2006 Bowen M, Brunger AT. Conformation of the synaptobrevin transmembrane domain. Proceedings of the National Academy of Sciences of the United States of America. 103: 8378-83. PMID 16709671 DOI: 10.1073/pnas.0602644103  0.381
2005 Bowen ME, Weninger K, Ernst J, Chu S, Brunger AT. Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex. Biophysical Journal. 89: 690-702. PMID 15821166 DOI: 10.1529/Biophysj.104.054064  0.301
2004 Bowen ME, Weninger K, Brunger AT, Chu S. Single molecule observation of liposome-bilayer fusion thermally induced by soluble N-ethyl maleimide sensitive-factor attachment protein receptors (SNAREs). Biophysical Journal. 87: 3569-84. PMID 15347585 DOI: 10.1529/Biophysj.104.048637  0.31
2003 Weninger K, Bowen ME, Chu S, Brunger AT. Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations. Proceedings of the National Academy of Sciences of the United States of America. 100: 14800-5. PMID 14657376 DOI: 10.1073/Pnas.2036428100  0.329
2002 Bowen ME, Engelman DM, Brunger AT. Mutational analysis of synaptobrevin transmembrane domain oligomerization. Biochemistry. 41: 15861-6. PMID 12501216 DOI: 10.1021/Bi0269411  0.318
1998 Bowen ME, Gettins PG. Bait region involvement in the dimer-dimer interface of human alpha 2-macroglobulin and in mediating gross conformational change. Evidence from cysteine variants that form interdimer disulfides. The Journal of Biological Chemistry. 273: 1825-31. PMID 9430734 DOI: 10.1074/Jbc.273.3.1825  0.583
1997 Bowen ME, Armstrong PB, Quigley JP, Gettins PG. Comparison of Limulus alpha-macroglobulin with human alpha2-macroglobulin: thiol ester characterization, subunit organization, and conformational change. Archives of Biochemistry and Biophysics. 337: 191-201. PMID 9016813 DOI: 10.1006/Abbi.1996.9760  0.615
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