Michael H. B. Stowell, PhD - Publications

Affiliations: 
University of Colorado, Boulder, Boulder, CO, United States 
Area:
Structure and Mechanism at the Chemical Synapse
Website:
http://dosequis.colorado.edu/

22 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
2020 Maity K, Heumann JM, McGrath AP, Kopcho NJ, Hsu P, Krishnan S, Medrano-Soto A, Saier MH, Piñeros MA, Komives EA, Schroeder JI, Chang G, Stowell MH. cryo-EM Structure of Rice OSCA1.2 Elucidates the Mechanical Basis of Membrane Hyperosmolality Gating in Plants Biophysical Journal. 118: 211a. DOI: 10.1016/J.Bpj.2019.11.1262  0.326
2015 Adams DJ, Arthur CP, Stowell MH. Architecture of the Synaptophysin/Synaptobrevin Complex: Structural Evidence for an Entropic Clustering Function at the Synapse. Scientific Reports. 5: 13659. PMID 26333660 DOI: 10.1038/Srep13659  0.653
2014 Basta T, Wu HJ, Morphew MK, Lee J, Ghosh N, Lai J, Heumann JM, Wang K, Lee YC, Rees DC, Stowell MH. Self-assembled lipid and membrane protein polyhedral nanoparticles. Proceedings of the National Academy of Sciences of the United States of America. 111: 670-4. PMID 24379376 DOI: 10.1073/Pnas.1321936111  0.632
2013 Pieper U, Schlessinger A, Kloppmann E, Chang GA, Chou JJ, Dumont ME, Fox BG, Fromme P, Hendrickson WA, Malkowski MG, Rees DC, Stokes DL, Stowell MH, Wiener MC, Rost B, et al. Coordinating the impact of structural genomics on the human α-helical transmembrane proteome. Nature Structural & Molecular Biology. 20: 135-8. PMID 23381628 DOI: 10.1038/Nsmb.2508  0.544
2010 Arthur CP, Dean C, Pagratis M, Chapman ER, Stowell MH. Loss of synaptotagmin IV results in a reduction in synaptic vesicles and a distortion of the Golgi structure in cultured hippocampal neurons. Neuroscience. 167: 135-42. PMID 20138128 DOI: 10.1016/J.Neuroscience.2010.01.056  0.625
2007 Arthur CP, Stowell MH. Structure of synaptophysin: a hexameric MARVEL-domain channel protein. Structure (London, England : 1993). 15: 707-14. PMID 17562317 DOI: 10.1016/J.Str.2007.04.011  0.662
2007 Arthur CP, Serrell DB, Pagratis M, Potter DL, Finch DS, Stowell MH. Electron tomographic methods for studying the chemical synapse. Methods in Cell Biology. 79: 241-57. PMID 17327160 DOI: 10.1016/S0091-679X(06)79010-0  0.629
2006 Yeh AP, McMillan A, Stowell MH. Rapid and simple protein-stability screens: application to membrane proteins. Acta Crystallographica. Section D, Biological Crystallography. 62: 451-7. PMID 16552147 DOI: 10.1107/S0907444906005233  0.369
2004 Tierney ML, Osborn KE, Milburn PJ, Stowell MH, Howitt SM. Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays. The Journal of Experimental Biology. 207: 3581-90. PMID 15339954 DOI: 10.1242/Jeb.01204  0.303
2001 Marks B, Stowell MH, Vallis Y, Mills IG, Gibson A, Hopkins CR, McMahon HT. GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature. 410: 231-5. PMID 11242086 DOI: 10.1038/35065645  0.363
1999 Miyazawa A, Fujiyoshi Y, Stowell M, Unwin N. Nicotinic acetylcholine receptor at 4.6 A resolution: transverse tunnels in the channel wall. Journal of Molecular Biology. 288: 765-86. PMID 10329178 DOI: 10.1006/Jmbi.1999.2721  0.616
1999 Miyazawa A, Fujiyoshi Y, Stowell M, Unwin N. Nicotinic acetylcholine receptor at 4.6 A resolution Seibutsu Butsuri. 39: S108. DOI: 10.2142/Biophys.39.S108_2  0.552
1998 Stowell MH, Miyazawa A, Unwin N. Macromolecular structure determination by electron microscopy: new advances and recent results. Current Opinion in Structural Biology. 8: 595-600. PMID 9818263 DOI: 10.1016/S0959-440X(98)80150-4  0.561
1997 Waldeck AR, Stowell MH, Lee HK, Hung SC, Matsson M, Hederstedt L, Ackrell BA, Chan SI. Electron paramagnetic resonance studies of succinate:ubiquinone oxidoreductase from Paracoccus denitrificans. Evidence for a magnetic interaction between the 3Fe-4S cluster and cytochrome b. The Journal of Biological Chemistry. 272: 19373-82. PMID 9235936 DOI: 10.1074/Jbc.272.31.19373  0.48
1997 Stowell MH, McPhillips TM, Rees DC, Soltis SM, Abresch E, Feher G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science (New York, N.Y.). 276: 812-6. PMID 9115209 DOI: 10.1126/Science.276.5313.812  0.537
1997 Peters JW, Stowell MH, Soltis SM, Finnegan MG, Johnson MK, Rees DC. Redox-dependent structural changes in the nitrogenase P-cluster. Biochemistry. 36: 1181-7. PMID 9063865 DOI: 10.1021/Bi9626665  0.447
1997 Musser SM, Stowell MH, Lee HK, Rumbley JN, Chan SI. Uncompetitive substrate inhibition and noncompetitive inhibition by 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-nonyl-4-hydroxyquinoline-N-oxide (NQNO) is observed for the cytochrome bo3 complex: implications for a Q(H2)-loop proton translocation mechanism. Biochemistry. 36: 894-902. PMID 9020789 DOI: 10.1021/Bi961723R  0.639
1996 Peters JW, Stowell MH, Rees DC. A leucine-rich repeat variant with a novel repetitive protein structural motif. Nature Structural Biology. 3: 991-4. PMID 8946850 DOI: 10.1038/Nsb1296-991  0.526
1995 Musser SM, Stowell MH, Chan SI. Cytochrome c oxidase: chemistry of a molecular machine. Advances in Enzymology and Related Areas of Molecular Biology. 71: 79-208. PMID 8644492 DOI: 10.1002/9780470123171.Ch3  0.642
1995 Stowell MH, Rees DC. Structure and stability of membrane proteins. Advances in Protein Chemistry. 46: 279-311. PMID 7771322 DOI: 10.1016/S0065-3233(08)60338-1  0.535
1993 Musser SM, Stowell MH, Chan SI. Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view. Febs Letters. 327: 131-6. PMID 8392948 DOI: 10.1016/0014-5793(93)80156-O  0.617
1993 Musser SM, Stowell MH, Chan SI. Further comparison of ubiquinol and cytochrome c terminal oxidases. Febs Letters. 335: 296-8. PMID 8253216 DOI: 10.1016/0014-5793(93)80751-F  0.672
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