نتایج جستجو برای: cyt

تعداد نتایج: 1814  

Journal: :Drug metabolism and disposition: the biological fate of chemicals 2007
Charles W Locuson Larry C Wienkers Jeffrey P Jones Timothy S Tracy

The hemoprotein cytochrome b(5) (cyt b5) has been demonstrated to affect the kinetics of drug oxidation by the microsomal cytochromes P450 (P450s). However, the mechanisms through which cyt b5 exerts these effects are variable and P450 isoform-dependent. Whereas the effects of cyt b5 on the major drug-metabolizing enzymes CYP2D6, CYP2E1, and CYP3A4 are well studied, fewer studies conducted over...

Journal: :The Journal of biological chemistry 1994
C K Mukhopadhyay I B Chatterjee

In this paper we demonstrate that NADPH-initiated oxidative damage of microsomal proteins occurs in the absence of free metal ions and that this protein oxidation is mediated by cytochrome P450 (cyt P450). Oxidized proteins are rapidly degraded by proteases. Ascorbate (AH2) specifically inhibits free metal ion-independent cyt P450-mediated protein oxidation and thereby prevents subsequent prote...

2016
Simone Graf Olga Fedotovskaya Wei-Chun Kao Carola Hunte Pia Ädelroth Michael Bott Christoph von Ballmoos Peter Brzezinski

Complex III in C. glutamicum has an unusual di-heme cyt. c1 and it co-purifies with complex IV in a supercomplex. Here, we investigated the kinetics of electron transfer within this supercomplex and in the cyt. aa3 alone (cyt. bc1 was removed genetically). In the reaction of the reduced cyt. aa3 with O2, we identified the same sequence of events as with other A-type oxidases. However, even thou...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2013
Chris L Bergstrom Paul A Beales Yang Lv T Kyle Vanderlick John T Groves

The release of cytochrome c from mitochondria is a key signaling mechanism in apoptosis. Although extramitochondrial proteins are thought to initiate this release, the exact mechanisms remain unclear. Cytochrome c (cyt c) binds to and penetrates lipid structures containing the inner mitochondrial membrane lipid cardiolipin (CL), leading to protein conformational changes and increased peroxidase...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2009
Luiz C Godoy Cristina Muñoz-Pinedo Laura Castro Simone Cardaci Christopher M Schonhoff Michael King Verónica Tórtora Mónica Marín Qian Miao Jian Fei Jiang Alexandr Kapralov Ronald Jemmerson Gary G Silkstone Jinal N Patel James E Evans Michael T Wilson Douglas R Green Valerian E Kagan Rafael Radi Joan B Mannick

Native cytochrome c (cyt c) has a compact tertiary structure with a hexacoordinated heme iron and functions in electron transport in mitochondria and apoptosis in the cytoplasm. However, the possibility that protein modifications confer additional functions to cyt c has not been explored. Disruption of methionine 80 (M80)-Fe ligation of cyt c under nitrative stress has been reported. To model t...

Journal: :Molecular bioSystems 2014
Zhonghua Wang Yuki Ando Ari Dwi Nugraheni Chunguang Ren Satoshi Nagao Shun Hirota

Met80 of cytochrome c (cyt c) has been shown to dissociate from its heme iron when cyt c interacts with cardiolipin (CL), which triggers the release of cyt c into the cytosol initiating apoptosis. We found that the mass of human cyt c increases by 16 Da in the Met80-Lys86 region by reaction with molecular oxygen in the presence of CL-containing liposomes and dithiothreitol (DTT). To investigate...

2011
Denis Pierron Juan C. Opazo Margit Heiske Zack Papper Monica Uddin Gopi Chand Derek E. Wildman Roberto Romero Morris Goodman Lawrence I. Grossman

Cytochrome c (cyt c) participates in two crucial cellular processes, energy production and apoptosis, and unsurprisingly is a highly conserved protein. However, previous studies have reported for the primate lineage (i) loss of the paralogous testis isoform, (ii) an acceleration and then a deceleration of the amino acid replacement rate of the cyt c somatic isoform, and (iii) atypical biochemic...

Journal: :American journal of physiology. Heart and circulatory physiology 2004
Andrey V Kuznetsov Stefan Schneeberger Rüdiger Seiler Gerald Brandacher Walter Mark Wolfgang Steurer Valdur Saks Yves Usson Raimund Margreiter Erich Gnaiger

Mitochondria play a critical role in myocardial cold ischemia-reperfusion (CIR) and induction of apoptosis. The nature and extent of mitochondrial defects and cytochrome c (Cyt c) release were determined by high-resolution respirometry in permeabilized myocardial fibers. CIR in a rat heart transplant model resulted in variable contractile performance, correlating with the decline of ADP-stimula...

Journal: :Genetics and molecular research : GMR 2013
K J Wu D Wang J Ding S H Yang X H Zhang

Cytochrome b5 (cyt b5) genes encode ubiquitous electron transport hemoproteins found in animals, plants, fungi, and purple bacteria. However, little is known about their evolutionary history in genomes so far. Here, we conducted an extensive genome-wide survey of cyt b5 genes in 20 representative model species and identified 310 of these genes. Both the absolute number and relative proportion o...

Journal: :Molecular and cellular biology 2002
Sonoko Narisawa Norman B Hecht Erwin Goldberg Kelly M Boatright John C Reed José Luis Millán

Differentiating male germ cells express a testis-specific form of cytochrome c (Cyt c(T)) that is distinct from the cytochrome c expressed in somatic cells (Cyt c(S)). To examine the role of Cyt c(T) in germ cells, we generated mice null for Cyt c(T). Homozygous Cyt c(T)(-/-) pups were statistically underrepresented (21%) but developed normally and were fertile. However, spermatozoa isolated fr...

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