Výsledky vyhledávání - "S. Z. Fisher"

Neutron structure of human carbonic anhydrase II in complex with methazolamide: mapping the solvent and hydrogen-bonding patterns of an effective clinical drug

Autor: Hector A. Velazquez, S. Z. Fisher, Andrey Kovalevsky, Jeremy C. Smith, Robert McKenna, Mayank Aggarwal

Publikováno v: IUCrJ, Vol 3, Iss 5, Pp 319-325 (2016)
IUCrJ

The room-temperature X-ray/neutron structure of human carbonic anhydrase II in complex with methazolamide has been determined. The study provides new insights into the hydrogen-bonding changes that take place within the active site of an enzyme upon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b764f98a2c1cb36012346d0ded8be2f3
http://scripts.iucr.org/cgi-bin/paper?S2052252516010514

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Visualizing the Bohr effect in hemoglobin: neutron structure of equine cyanomethemoglobin in the R state and comparison with human deoxyhemoglobin in the T state

Autor: Paul Langan, Sean Seaver, S. Z. Fisher, B.L. Hanson, Timothy C. Mueser, Andrey Kovalevsky, Steven Dajnowicz

Publikováno v: Acta Crystallographica. Section D, Structural Biology

The determination of the positions of H/D atoms in equine cyanomethemoglobin by neutron diffraction is described.
Neutron crystallography provides direct visual evidence of the atomic positions of deuterium-exchanged H atoms, enabling the accura

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ea2a54e09b64dac17aa3e38d24b0a5f
https://doi.org/10.1107/s2059798316009049

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Direct determination of protonation states and visualization of hydrogen bonding in a glycoside hydrolase with neutron crystallography

Autor: Leighton Coates, Andreas Ostermann, S. Z. Fisher, David E. Graham, Tobias E. Schrader, B. Leif Hanson, Jerry M. Parks, Qun Wan, Andrey Kovalevsky, Paul Langan

Publikováno v: Proceedings of the National Academy of Sciences. 112:12384-12389

Glycoside hydrolase (GH) enzymes apply acid/base chemistry to catalyze the decomposition of complex carbohydrates. These ubiquitous enzymes accept protons from solvent and donate them to substrates at close to neutral pH by modulating the pKa values

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b91d3dbb2902d8fabe01b41973615dc3
https://doi.org/10.1073/pnas.1504986112

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Preliminary time-of-flight neutron diffraction studies ofEscherichia coliABC transport receptor phosphate-binding protein at the Protein Crystallography Station

Autor: Katherine H. Sippel, John-Paul Bacik, S. Z. Fisher, F. A. Quiocho

Publikováno v: Acta Crystallographica Section F Structural Biology Communications. 70:819-822

Inorganic phosphate is an essential molecule for all known life. Organisms have developed many mechanisms to ensure an adequate supply, even in low-phosphate conditions. In prokaryotes phosphate transport is instigated by the phosphate-binding protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cdd431220c054a18892110841f58f2b
https://doi.org/10.1107/s2053230x14009704

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Neutron Diffraction of Acetazolamide-Bound Human Carbonic Anhydrase II Reveals Atomic Details of Drug Binding

Autor: David N. Silverman, Robert McKenna, Andrey Kovalevsky, S. Z. Fisher, Mayank Aggarwal

Publikováno v: Journal of the American Chemical Society. 134:14726-14729

Carbonic anhydrases (CAs) catalyze the hydration of CO(2) forming HCO(3)(-) and a proton, an important reaction for many physiological processes including respiration, fluid secretion, and pH regulation. As such, CA isoforms are prominent clinical ta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29cce2f5e19e6f10bb21d6e83f20d219
https://doi.org/10.1021/ja3068098

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Structural and Kinetic Study of the Extended Active Site for Proton Transfer in Human Carbonic Anhydrase II

Autor: Wilton Williams, David N. Silverman, Robert McKenna, S. Z. Fisher, Mavis Agbandje-McKenna, Chingkuang Tu, John F. Domsic

Publikováno v: Biochemistry. 49:6394-6399

The catalysis of CO2 hydration by human carbonic anhydrase II (HCA II) is limited in maximal velocity by proton transfer from a zinc-bound water molecule to the proton shuttle His64. This proton transfer occurs along a hydrogen-bonded water network,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b3bf11b7c2e109441c222e01713627c
https://doi.org/10.1021/bi1007645

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Preliminary joint neutron and X-ray crystallographic study of human carbonic anhydrase II

Autor: David N. Silverman, Paul Langan, Robert McKenna, Marat Mustyakimov, John F. Domsic, S. Z. Fisher, Andrey Kovalevsky

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:495-498

Carbonic anhydrases catalyze the interconversion of CO(2) to HCO(3)(-), with a subsequent proton-transfer (PT) step. PT proceeds via a proposed hydrogen-bonded water network in the active-site cavity that is stabilized by several hydrophilic residues

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::232b0c24cb2550efe872a4f96421579b
https://doi.org/10.1107/s1744309109013086

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Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4)

Autor: Javier M. González, S. Z. Fisher

Publikováno v: Acta crystallographica. Section F, Structural biology communications. 71(Pt 2)

Inhibition of human adipocyte fatty-acid binding protein (FABP4) has been proposed as a treatment for type 2 diabetes, fatty liver disease and atherosclerosis. However, FABP4 displays a naturally low selectivity towards hydrophobic ligands, leading t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa906b003bd4b02c940c7e2ffccae48f
https://pubmed.ncbi.nlm.nih.gov/25664790

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Preliminary joint neutron time-of-flight and X-ray crystallographic study of human ABO(H) blood group A glycosyltransferase

Autor: Svetlana N. Borisova, Leighton Coates, S. Z. Fisher, Stephen V. Evans, Brock Schuman, Paul Langan, Monica M. Palcic, Andrey Kovalevsky

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications. 67(Pt 2)

The biosyntheses of oligosaccharides and glycoconjugates are conducted by glycosyltransferases. These extraordinarily diverse and widespread enzymes catalyze the formation of glycosidic bonds through the transfer of a monosaccharide from a donor mole

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0d43cc9aad271447b90ece38a61c1ec
https://pubmed.ncbi.nlm.nih.gov/21301100

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