Zobrazeno 1 - 10 of 17 pro vyhledávání: '"Mb, myoglobin"'
1
Defining the reducing system of the NO dioxygenase cytoglobin in vascular smooth muscle cells and its critical role in regulating cellular NO decay
Autor: Jay L. Zweier, Mohamed A. El-Mahdy, Tapan Kumar Kundu, Sahar A. Khaleel, Craig Hemann, Govindasamy Ilangovan
Publikováno v: The Journal of Biological Chemistry
In smooth muscle, cytoglobin (Cygb) functions as a potent nitric oxide (NO) dioxygenase and regulates NO metabolism and vascular tone. Major questions remain regarding which cellular reducing systems regulate Cygb-mediated NO metabolism. To better de
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::402d29350bd511c71de9574951fdf260
http://europepmc.org/articles/PMC7948950
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2
Allostery in the nitric oxide dioxygenase mechanism of flavohemoglobin
Autor: Anne M. Gardner, Paul R. Gardner
Publikováno v: The Journal of Biological Chemistry
The substrates O2 and NO cooperatively activate the NO dioxygenase function of Escherichia coli flavohemoglobin. Steady-state and transient kinetic measurements support a structure-based mechanistic model in which O2 and NO movements and conserved am
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51b257f48924daea0bfc5e3cf796abda
https://pubmed.ncbi.nlm.nih.gov/34237890
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3
Cardiac biomarkers and COVID-19: A systematic review and meta-analysis
Autor: Ju-Seop Kang, Wen An, Tae Eun Kim, Qiuyang Wang
Publikováno v: Journal of Infection and Public Health
Journal of Infection and Public Health, Vol 14, Iss 9, Pp 1191-1197 (2021)
Objective: To systematically investigate the relationship between cardiac biomarkers and COVID-19 severity and mortality. Methods: We performed a literature search using PubMed, Web of Science, and Google Scholar. The standardized mean difference (SM
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7efdf6f866c0fa4e05226e54f3f0280
https://pubmed.ncbi.nlm.nih.gov/34416596
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4
Androglobin gene expression patterns and FOXJ1-dependent regulation indicate its functional association with ciliogenesis
Autor: Teng Wei, Koay, Carina, Osterhof, Ilaria M C, Orlando, Anna, Keppner, Daniel, Andre, Schayan, Yousefian, María, Suárez Alonso, Miguel, Correia, Robert, Markworth, Johannes, Schödel, Thomas, Hankeln, David, Hoogewijs
Publikováno v: The Journal of Biological Chemistry
Androglobin (ADGB) represents the latest addition to the globin superfamily in metazoans. The chimeric protein comprises a calpain domain and a unique circularly permutated globin domain. ADGB expression levels are most abundant in mammalian testis,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::160109fd9eb4e85097a506a6e38eff46
https://pubmed.ncbi.nlm.nih.gov/33453283
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6
Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes
Autor: Luisa B. Maia, José J. G. Moura
Publikováno v: Redox Biology
Redox Biology, Vol 19, Iss, Pp 274-289 (2018)
Nitric oxide radical (NO) is a signaling molecule involved in several physiological and pathological processes and a new nitrate-nitrite-NO pathway has emerged as a physiological alternative to the "classic" pathway of NO formation from L-arginine. S
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f70c8cca582ae1a397825ccb31c92d2
https://doi.org/10.1016/j.redox.2018.08.020
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7
Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions
Autor: Herald Berghmans, Paolo Ascenzi, Marco Nardini, Cinzia Verde, Daniela Giordano, Francesco Marchesani, Stijn Vermeylen, Stefania Abbruzzetti, Martino Bolognesi, Cristiano Viappiani, Constantí Seira, Guido di Prisco, Sylvia Dewilde, Alessandra Pesce, Stefano Bruno, F. Javier Luque
Publikováno v: Computational and Structural Biotechnology Journal 18 (2020): 2132–2144. doi:10.1016/j.csbj.2020.08.007
info:cnr-pdr/source/autori:Giordano D.; Pesce A.; Vermeylen S.; Abbruzzetti S.; Nardini M.; Marchesani F.; Berghmans H.; Seira C.; Bruno S.; Javier Luque F.; di Prisco G.; Ascenzi P.; Dewilde S.; Bolognesi M.; Viappiani C.; Verde C./titolo:Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions/doi:10.1016%2Fj.csbj.2020.08.007/rivista:Computational and Structural Biotechnology Journal/anno:2020/pagina_da:2132/pagina_a:2144/intervallo_pagine:2132–2144/volume:18
Computational and Structural Biotechnology Journal
Dipòsit Digital de la UB
Universidad de Barcelona
'Computational and Structural Biotechnology Journal ', vol: 18, pages: 2132-2144 (2020)
Computational and Structural Biotechnology Journal, Vol 18, Iss, Pp 2132-2144 (2020)
Graphical abstract 1These authors contributed equally as First Author.
While the functions of the recently discovered cytoglobin, ubiquitously expressed in vertebrate tissues, remain uncertain, Antarctic fish provide unparalleled models to study
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af750df4e2640ee580dfff3ddf04032f
http://www.cnr.it/prodotto/i/433166
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8
A thiol-reactive Ru(II) ion, not CO release, underlies the potent antimicrobial and cytotoxic properties of CO-releasing molecule-3
Autor: Sherif F. El-Khamisy, Jonathan A. Chapman, Michael P. Williamson, Rhiannon L. Lyon, Chunyan Liao, Thomas W. Smith, Hannah M. Southam, Robert K. Poole, Laurence A. Middlemiss, Francesca L. Cox, Michael Hippler, Peter J. F. Henderson, Clare R. Trevitt
Publikováno v: Redox Biology
Redox Biology, Vol 18, Iss, Pp 114-123 (2018)
Carbon monoxide (CO)-releasing molecules (CORMs), mostly metal carbonyl compounds, are extensively used as experimental tools to deliver CO, a biological ‘gasotransmitter’, in mammalian systems. CORMs are also explored as potential novel antimicr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d75f68fb72f1c43fdfc10064d6464139
https://eprints.whiterose.ac.uk/133526/1/RedoxBiology_CORM3_2018.pdf
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9
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution
Autor: Francesca Cutruzzolà, Andrea Brancaccio, Maurizio Brunori, Martino Bolognesi, Menico Rizzi, Alessandro Coda, Carlo Travaglini Allocatelli
Publikováno v: FEBS letters. 320(1)
The three-dimensional structure of sperm whale myoglobin His64(E7)→Val,Thr64(E10)→Arg double mutant has been studied by X-ray crystallography at 1.6 Å resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db0886dc1db6b08746cd48c8299013bf
https://pubmed.ncbi.nlm.nih.gov/8462669
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10
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