Zobrazeno 1 - 10
of 141
pro vyhledávání: '"John C Salerno"'
Autor:
Ellen W Moomaw, Eric Hoffer, Patricia Moussatche, John C Salerno, Morgan Grant, Bridget Immelman, Richard Uberto, Andrew Ozarowski, Alexander Angerhofer
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e57933 (2013)
Ceriporiopsis subvermispora oxalate oxidase (CsOxOx) is the first bicupin enzyme identified that catalyzes manganese-dependent oxidation of oxalate. In previous work, we have shown that the dominant contribution to catalysis comes from the monoproton
Externí odkaz:
https://doaj.org/article/5f6b15c15673425392c4385fb5def7c4
Autor:
Xzaviar K. V. Solone, Amber L. Caldara, Brady Wells, Hao Qiao, Lydia R. Wade, John C. Salerno, Katy A. Helms, Katherine E. R. Smith, Jonathan L. McMurry, Carol A. Chrestensen
Publikováno v:
FEBS Open Bio, Vol 12, Iss 5, Pp 1075-1086 (2022)
Nitric oxide synthase 3 (NOS3) is a major vasoprotective enzyme that catalyzes the conversion of l‐arginine to nitric oxide (NO) in response to a significant number of signaling pathways. Here, we provide evidence that NOS3 interactions with MAP ki
Externí odkaz:
https://doaj.org/article/3992d4b248484859b9a67645dbfb0a3e
Publikováno v:
Journal of Hypertension. 38:2340-2341
Publikováno v:
Mathematical Biosciences. 281:62-73
Nitric Oxide (NO) is a gaseous compound that serves as a signaling molecule in cellular interactions. In the vasculature, NO is synthesized from endogenous agents by endothelial nitric oxide synthase (eNOS) where it plays key roles in several functio
Endothelial and neuronal nitric oxide synthases (eNOS, nNOS) are important signal generators in a number of processes including angiogenesis and neurotransmission. The homologous inducible isoform (iNOS) occupies a multitude of conformational states
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c48bc0793d31a4d48f21d77bcce6e72f
Publikováno v:
Biological chemistryReferences. 399(11)
NADH-quinone oxidoreductase (complex I) is the largest and most complicated enzyme complex of the mitochondrial respiratory chain. It is the entry site into the respiratory chain for most of the reducing equivalents generated during metabolism, coupl
Autor:
Lauren Hutchinson, Zachary McCarty, John C. Salerno, Daniela Tapu, Christopher Ghattas, Mahatab Chowdhury, Don VanDerveer
Publikováno v:
Journal of Organometallic Chemistry. 749:134-141
A new polycyclic N-heterocyclic carbene featuring a fused dibenz[a,c]phenazine moiety was generated in situ from the corresponding tetrafluoroborate salt. The synthesis and NMR data of its corresponding precursors, its sulfur adduct and dimer are rep
Autor:
Jonathan L. McMurry, Allison N. Healey, John C. Salerno, Scott J. Nowak, Carol A. Chrestensen, Verra M. Ngwa
The use of cell penetrating peptides (CPPs) as biomolecular delivery vehicles holds great promise for therapeutic and other applications, but development has been stymied by poor delivery and lack of endosomal escape. We have developed a CPP-adaptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05d6ab3a8c97cca8deab7b09195f59dd
https://europepmc.org/articles/PMC6295119/
https://europepmc.org/articles/PMC6295119/
Publikováno v:
FEBS Journal. 279:1306-1317
Nitric oxide synthases (NOSs) produce NO as a molecular signal in the nervous and cardiovascular systems and as a cytotoxin in the immune response. NO production in the constitutive isoforms is controlled by calmodulin regulation of electron transfer
Autor:
Kyle D. Harris, Elijah W. Lee, Brian J. Forsberg, Jonathan L. McMurry, Allan M. Johansen, Aaron M. Rahn, Israel M. Scott, John C. Salerno, Carol A. Chrestensen
Publikováno v:
FEBS Journal. 278:4943-4954
Using interferometry-based biosensors the binding and release of endothelial and neuronal nitric oxide synthase (eNOS and nNOS) from calmodulin (CaM) was measured. In both isoforms, binding to CaM is diffusion limited and within approximately three o