Zobrazeno 1 - 10 of 286 pro vyhledávání: '"John P. Richard"'
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Akademický článek
Multifaceted highly targeted sequential multidrug treatment of early ambulatory high-risk SARS-CoV-2 infection (COVID-19)
Autor: Peter A. McCullough, Paul E. Alexander, Robin Armstrong, Cristian Arvinte, Alan F. Bain, Richard P. Bartlett, Robert L. Berkowitz, Andrew C. Berry, Thomas J. Borody, Joseph H. Brewer, Adam M. Brufsky, Teryn Clarke, Roland Derwand, Alieta Eck, John Eck, Richard A. Eisner, George C. Fareed, Angelina Farella, Silvia N. S. Fonseca, Charles E. Geyer Jr., Russell S. Gonnering, Karladine E. Graves, Kenneth B. V. Gross, Sabine Hazan, Kristin S. Held, H. Thomas Hight, Stella Immanuel, Michael M. Jacobs, Joseph A. Ladapo, Lionel H. Lee, John Littell, Ivette Lozano, Harpal S. Mangat, Ben Marble, John E. McKinnon, Lee D. Merritt, Jane M. Orient, Ramin Oskoui, Donald C. Pompan, Brian C. Procter, Chad Prodromos, Juliana Cepelowicz Rajter, Jean-Jacques Rajter, C. Venkata S. Ram, Salete S. Rios , Harvey A. Risch, Michael J. A. Robb, Molly Rutherford, Martin Scholz, Marilyn M. Singleton, James A. Tumlin, Brian M. Tyson, Richard G. Urso, Kelly Victory, Elizabeth Lee Vliet, Craig M. Wax, Alexandre G. Wolkoff, Vicki Wooll, Vladimir Zelenko
Publikováno v: Reviews in Cardiovascular Medicine, Vol 21, Iss 4, Pp 517-530 (2020)
The SARS-CoV-2 virus spreading across the world has led to surges of COVID-19 illness, hospitalizations, and death. The complex and multifaceted pathophysiology of life-threatening COVID-19 illness including viral mediated organ damage, cytokine stor
Externí odkaz: https://doaj.org/article/55365a581aca443eaca2bf710a0a06f8
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3
Glycerol-3-Phosphate Dehydrogenase: The K120 and K204 Side Chains Define an Oxyanion Hole at the Enzyme Active Site
Autor: Judith R. Cristobal, John P. Richard
Publikováno v: Biochemistry. 61(10)
The cationic K120 and K204 side chains lie close to the C-2 carbonyl group of substrate dihydroxyacetone phosphate (DHAP) at the active site of glycerol-3-phosphate dehydrogenase (GPDH), and the K120 side chain is also positioned to form a hydrogen b
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::789f62ccf7d4d8e8f9d66a455824101f
https://pubmed.ncbi.nlm.nih.gov/35502876
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6
Adenylate Kinase-Catalyzed Reaction of AMP in Pieces: Enzyme Activation for Phosphoryl Transfer to Phosphite Dianion
Autor: John P. Richard, Patrick L. Fernandez
Publikováno v: Biochemistry
The binding of adenosine 5’-triphosphate (ATP) and adenosine 5’-monophosphate (AMP) to adenylate kinase (AdK) drives closure of lids over the substrate adenosyl groups. We test the hypothesis that this conformational change activates AdK for cata
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e310666b9e584b04f2d541213942122
https://doi.org/10.1021/acs.biochem.1c00535
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7
Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions
Autor: John P. Richard, Richard W. Nagorski, Patrick L. Fernandez, Judith R. Cristobal, Tina L. Amyes
Publikováno v: Journal of the American Chemical Society. 143:2694-2698
The activation barriers ΔG⧧ for kcat/Km for the reactions of whole substrates catalyzed by 6-phosphogluconate dehydrogenase, glucose 6-phosphate dehydrogenase, and glucose 6-phosphate isomerase are reduced by 11-13 kcal/mol by interactions between
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::724c5904c4197f657ce34d2334461e02
https://doi.org/10.1021/jacs.0c13423
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8
Origin of Free Energy Barriers of Decarboxylation and the Reverse Process of CO2 Capture in Dimethylformamide and in Water
Autor: Bach T. Nguyen, John P. Richard, Shaoyuan Zhou, Jiali Gao, Ronald Kluger
Publikováno v: J Am Chem Soc
In aqueous solution, biological decarboxylation reactions proceed irreversibly to completion, whereas the reverse carboxylation processes are typically powered by the hydrolysis of ATP. The exchange of the carboxylate of ring-substituted arylacetates
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ac1d9fdc7cd3f39cc530fd33865efdb
https://doi.org/10.1021/jacs.0c12414
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9
Hydride Transfer Catalyzed by Glycerol Phosphate Dehydrogenase: Recruitment of an Acidic Amino Acid Side Chain to Rescue a Damaged Enzyme
Autor: John P. Richard, Rui He, Judith R. Cristobal, Naiji Jabin Gong
Publikováno v: Biochemistry
K120 of glycerol 3-phosphate dehydrogenase (GPDH) lies close to the carbonyl group of the bound dihydroxyacetone phosphate (DHAP) dianion. pH rate (pH 4.6–9.0) profiles are reported for kcat and (kcat/Km)dianion for wild type and K120A GPDH-catalyz
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5cb8987bf123c8759c77e7a5cfc9b86
http://europepmc.org/articles/PMC7784668
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10
Orotidine 5′-Monophosphate Decarboxylase: The Operation of Active Site Chains Within and Across Protein Subunits
Autor: John P. Richard, Tiago A. S. Brandão
Publikováno v: Biochemistry
The D37 and T100′ side chains of orotidine 5′-monophosphate decarboxylase (OMPDC) interact with the C-3′ and C-2′ ribosyl hydroxyl groups, respectively, of the bound substrate. We compare the intra-subunit interactions of D37 with the inter-s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7827bca56172c46e8ac9793ed8f3131
https://doi.org/10.1021/acs.biochem.0c00241
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