Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Transmembrane electron transfer by the membrane DsbD occurs via a disulfide bond cascade

Article Abstract:

Research demonstrates the ability of the cytoplasmic membrane protein DsbD to mediate electron transfer from the cytoplasm to the periplasm in Escherichia coli. Data point out that the transfer involves interactions between thioredoxin and DsbD and periplasmic substrates.

Author: Katzen, Federico, Beckwith, Jon
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
Escherichia coli, Membrane proteins, Oxidation-reduction reaction, Oxidation-reduction reactions, Electron transport

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Bridge over troubled waters: sensing stress by disulfide bond formation

Article Abstract:

Previous studies have established that disulfide bond formation has the capability to regulate protein activity. In addition, some experiments found evidences that prove that disulfide bond formation may also be a consequence of cellular stress. This has been particularly observed in experiments with eukaryotic cells where it was seen that disulfide bonds are created in response to oxidative stress.

Author: Beckwith, Jon, Aslund, Fredrik
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
Chemical bonds, Mechanical chemistry, Mechanochemistry, Disulfiram

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Electron Avenue: pathways of disulfide bond formation and isomerization

Article Abstract:

Pathways of disulfide bond isomerization and formation are discussed in this review article. The mechanism elaborated by cells for oxidation of cysteine residues is extremely intricate compared to that earlier thought to exist and to the uncomplicated primary reaction. Topics discussed include folding of proteins involving covalent links between pairs of cysteines to form disulfide bonds, eukaryotes/prokaryotes and electron movements in both disulfide bond formation and protein disulfide bond isomerization.

Author: Beckwith, Jon, Debarbieux, Laurent
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
Statistical Data Included, Prokaryotes, Cytochemistry, Protein folding, Chemistry, Physical and theoretical, Physical chemistry, Isomerization, Catalysis, Cysteine

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: United States, Physiological aspects, Research, Eukaryotic cells, Cells (Biology), Eukaryotes
Similar abstracts:
  • Abstracts: Penetrance and expressivity of the gene for double podding in chickpea. A major gene for time of flowering in Chickpea
  • Abstracts: RAD51-independent break-induced replication to repair a broken chromosome depends on a distant enhancer site
  • Abstracts: Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast. The early evolution of the genetic code
  • Abstracts: Chembiosynthesis of novel 6-deoxyerythronolide B analogues by mutation of the loading module of 6-deoxyerythronolide B synthase 1
  • Abstracts: Fungal biotransformation of the antihistamine azatadine by Cunninghamella elegans. Transformation of amoxapine by Cunninghamella elegans
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.