Results 11 to 20 of about 2,436,389 (378)

Mitochondrial Group II Introns, Cytochrome c Oxidase, and Senescence in Podospora anserina [PDF]

open access: closedMolecular and Cellular Biology, 1999
Podospora anserina is a filamentous fungus with a limited life span. It expresses a degenerative syndrome called senescence, which is always associated with the accumulation of circular molecules (senDNAs) containing specific regions of the mitochondrial chromosome.
Odile Begel   +4 more
semanticscholar   +4 more sources

Cerebrospinal Fluid Levels of High-Mobility Group Box 1 and Cytochrome C Predict Outcome after Pediatric Traumatic Brain Injury [PDF]

open access: closedJournal of Neurotrauma, 2012
High-mobility group box 1 (HMGB1) is a ubiquitous nuclear protein that is passively released from damaged and necrotic cells, and actively released from immune cells. In contrast, cytochrome c is released from mitochondria in apoptotic cells, and is considered a reliable biomarker of apoptosis.
Alicia K. Au   +8 more
semanticscholar   +4 more sources

Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c‐type cytochromes [PDF]

open access: bronzeMolecular Microbiology, 2006
SummaryIn all organisms, haem is post‐translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c‐type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem–apocytochrome ligation per se.
Serdar Turkarslan   +2 more
openalex   +3 more sources

Structure of an electron transfer complex. II. Chemical modification of carboxyl groups of cytochrome c peroxidase in presence and absence of cytochrome c.

open access: hybridJournal of Biological Chemistry, 1985
Cytochrome c peroxidase forms an electron transfer complex with cytochrome c. The complex is governed by ionic bonds between side chain amino groups of cytochrome c and carboxyl groups of peroxidase. To localize the binding site for cytochrome c on the peroxidase, we have used the method of differential chemical modification.
Rolf Bechtold, Hans Rudolf Bosshard
openalex   +3 more sources

Is cytochrome c oxidase subunit I (COI) the right DNA barcoding marker for the Chaetopteryx villosa group? [PDF]

open access: diamondARPHA Conference Abstracts, 2021
Chaetopteryx villosa (Fabricius, 1798) is a caddisfly species distributed throughout Europe, except in the Balkan and Apennine Peninsula. However, phylogenetically close species belonging to the C. villosa group are widespread throughout entire Europe. Species of this group (C. villosa, C. gessneri, C. fusca, C. sahlbergi, C. atlantica, C. bosniaca, C.
Dalila Destanović   +4 more
openalex   +3 more sources

Thermodynamic Data for Myoglobin, Hæmoglobin and Cytochrome-c Reactions, and the Position of the Hæm Groups [PDF]

open access: bronzeNature, 1955
CONANT1 first put forward the idea that the haems in haemoglobin are held by two bonds of unequal strength between the iron and groups in the protein on both sides of the haem disk, the weaker bond breaking when combination with oxygen, carbon monoxide, etc., occurs.
Philip George, G. I. H. Hanania
openalex   +3 more sources

Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groups [PDF]

open access: goldCurrent Issues in Molecular Biology
Neuroglobin (Ngb) is a cytosolic heme protein that plays an important role in protecting cells from apoptosis through interaction with oxidized cytochrome c (Cyt c) released from mitochondria. The interaction of reduced Ngb and oxidized Cyt c is accompanied by electron transfer between them and the reduction in Cyt c.
Marina A. Semenova   +7 more
openalex   +4 more sources

The Functional Role of Thiol Groups in Protease-Solubilized NADPH-Cytochrome c Reductase from Pork-Liver Microsomes [PDF]

open access: bronzeEuropean Journal of Biochemistry, 1977
The total —SH content of protease-solubilized NADPH—cytochrome c reductase (EC 1.6.2.4) from pork liver microsomes was determined to be 5.9 ± 0.3 mol thiol groups per mol of protein. Only three —SH groups of the protease-solubilized NADPH – cytochrome c reductase could be modified by 0.34 or 1.0 mM 5,5′-dithio-bis(2-nitrobenzoate) at pH 7.5 and + 4°C ...
Tibor LAZAR, Helga EHRIG, L Lumper
openalex   +4 more sources

Pentamycin Biosynthesis in Philippine Streptomyces sp. S816: Cytochrome P450-Catalyzed Installation of the C-14 Hydroxyl Group [PDF]

open access: greenACS Chemical Biology, 2019
ABSTRACTPentamycin is a polyene antibiotic, registered in Switzerland for the treatment of vaginal candidiasis, trichomo-niasis and mixed infections. Chemical instability has hindered its wide-spread application and development as a drug. Here we report the identification ofStreptomycessp.
Shanshan Zhou   +10 more
openalex   +5 more sources

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