Výsledky vyhledávání - "Steven E. Cohen"

Akademický článek

A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation

Autor: Alireza Ghanbarpour, Steven E. Cohen, Xue Fei, Laurel F. Kinman, Tristan A. Bell, Jia Jia Zhang, Tania A. Baker, Joseph H. Davis, Robert T. Sauer

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)

Abstract AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently

Externí odkaz: https://doaj.org/article/f72b46a348b247609e8481dbe950089a

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Akademický článek

Boosting NAD+ with a small molecule that activates NAMPT

Autor: Stephen J. Gardell, Meghan Hopf, Asima Khan, Mauro Dispagna, E. Hampton Sessions, Rebecca Falter, Nidhi Kapoor, Jeanne Brooks, Jeffrey Culver, Chris Petucci, Chen-Ting Ma, Steven E. Cohen, Jun Tanaka, Emmanuel S. Burgos, Jennifer S. Hirschi, Steven R. Smith, Eduard Sergienko, Anthony B. Pinkerton

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)

Nicotinamide phosphoribosyltransferase (NAMPT) catalyzes the rate determining step for NAD+ synthesis and is of interest as a drug target. Here the authors identify and characterize a small molecule NAMPT activator SBI-797812, elucidate its mode of a

Externí odkaz: https://doaj.org/article/1414d8924adf4074afe7c8dc6bbcf1cf

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Akademický článek

A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state

Autor: Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan, Sean J. Elliott

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)

The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG

Externí odkaz: https://doaj.org/article/43e89e2788134c44bc04e90574efd768

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A Stable Ferryl Porphyrin at the Active Site of Y463M BthA

Autor: Steven E. Cohen, Catherine L. Drennan, Andrew C. Weitz, Michael P. Hendrich, Sean Elliott, Kimberly Rizzolo

Publikováno v: J Am Chem Soc

BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)=O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::268c0ef2e799e45188d81663fbeac15d
https://doi.org/10.1021/jacs.0c04023

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Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase

Autor: Mériem Merrouch, Catherine L. Drennan, Vincent Fourmond, Elizabeth C. Wittenborn, Steven E. Cohen, Sébastien Dementin, Christophe Léger

Publikováno v: J Biol Chem
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩

The nickel-dependent carbon monoxide dehydrogenase (CODH) employs a unique heterometallic nickel–iron–sulfur cluster, termed the C-cluster, to catalyze the interconversion of CO and CO(2). Like other complex metalloenzymes, CODH requires dedicate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9b47de955c61cc33bdfa835481fd473
https://doi.org/10.1074/jbc.ra119.009610

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Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Autor: Catherine L. Drennan, Edward J. Brignole, Elizabeth C. Wittenborn, Samuel Thompson, Mehmet Can, Stephen W. Ragsdale, Steven E. Cohen

Publikováno v: Structure

The nickel-iron-sulfur-containing A-cluster of acetyl-CoA synthase (ACS) assembles acetyl-CoA from carbon monoxide (CO), a methyl group (CH(3)(+)), and coenzyme A (CoA). To accomplish this feat, ACS must bind CoA and interact with two other proteins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee7c92f39b921c5614068d47f021e31e
https://pubmed.ncbi.nlm.nih.gov/32937101

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Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Autor: Catherine L. Drennan, Elizabeth C. Wittenborn, Rachel A Hendrickson, Steven E. Cohen, Mehmet Can, Stephen W. Ragsdale

Publikováno v: ACS
ACS Catalysis

Copyright © 2020 American Chemical Society. The Wood-Ljungdahl pathway allows for autotrophic bacterial growth on carbon dioxide, with the last step in acetyl-CoA synthesis catalyzed by the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-Co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bad420ef5ad7fde53ec5ef673f2ee99
https://hdl.handle.net/1721.1/133251

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Optimization of a urea-containing series of nicotinamide phosphoribosyltransferase (NAMPT) activators

Autor: Mayuko Akiu, Steven E. Cohen, Chen-Ting Ma, E. Hampton Sessions, Layton H. Smith, Michael R. Jackson, Paul Hershberger, Stephen J. Gardell, Patrick R. Maloney, Takashi Tsuji, Eduard Sergienko, Satyamaheshwar Peddibhotla, Jun Tanaka, Anthony B. Pinkerton, Tsuyoshi Nakamura, Meghan E. Hopf

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 41:128007

NAD+ is a crucial cellular factor that plays multifaceted roles in wide ranging biological processes. Low levels of NAD+ have been linked to numerous diseases including metabolic disorders, cardiovascular disease, neurodegeneration, and muscle wastin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2e4dbfbf4d7a8be49608d581c3278b1
https://doi.org/10.1016/j.bmcl.2021.128007

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Boosting NAD+ with a small molecule that activates NAMPT

Autor: Jun Tanaka, Emmanuel S. Burgos, Rebecca Falter, E. Hampton Sessions, Jeanne Brooks, Stephen J. Gardell, Steven E. Cohen, Anthony B. Pinkerton, Asima Khan, Jennifer S. Hirschi, Meghan E. Hopf, Nidhi Kapoor, Jeffrey A. Culver, Chris Petucci, Steven R. Smith, Eduard Sergienko, Chen Ting Ma, Mauro Dispagna

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)

Pharmacological strategies that boost intracellular NAD+ are highly coveted for their therapeutic potential. One approach is activation of nicotinamide phosphoribosyltransferase (NAMPT) to increase production of nicotinamide mononucleotide (NMN), the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::585eec1c791ac237c67f377064693612
https://doi.org/10.1038/s41467-019-11078-z

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A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state

Autor: Steven E. Cohen, Catherine L. Drennan, Madeline M. López Muñoz, Andrew C. Weitz, Sean Elliott, Michael P. Hendrich, Kimberly Rizzolo

Publikováno v: Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)

Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H2O2) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a33ed2a3060de56bdcfc0858acfd7f16
https://doi.org/10.1038/s41467-019-09020-4

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