Results 81 to 90 of about 97,846 (317)

Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation

open access: yesiScience, 2021
Summary: The mammalian endoplasmic reticulum (ER) harbors more than 20 members of the protein disulfide isomerase (PDI) family that act to maintain proteostasis.
Chihiro Hirayama   +7 more
doaj   +1 more source

The cuticle [PDF]

open access: yes, 2007
The nematode cuticle is an extremely flexible and resilient exoskeleton that permits locomotion via attachment to muscle, confers environmental protection and allows growth by molting.
Johnstone, I. J., Page, A. P.
core   +1 more source

A New Vista of Opportunity in Diabetes Management: Natural Product‐Based β‐cell Preservation

open access: yesFood Chemistry International, EarlyView.
Preserving functional β‐cells via natural products offers promising strategy for diabetes treatment. ABSTRACT A defining characteristic of diabetes is β‐cell failure, in which β‐cells cannot modulate insulin secretion to compensate for escalating insulin resistance, pushing forward disease development.
Yi‐San Lee   +4 more
wiley   +1 more source

Characterization of an A-Site Selective Protein Disulfide Isomerase A1 Inhibitor

open access: yesBiochemistry, 2018
Protein disulfide isomerase A1 (PDIA1) is an endoplasmic reticulum (ER)-localized thiol-disulfide oxidoreductase that is an important folding catalyst for secretory pathway proteins.
Kyle S. Cole   +7 more
semanticscholar   +1 more source

Protein Disulfide Isomerase A4 Is Involved in Genome Uncoating during Human Astrovirus Cell Entry

open access: yesViruses, 2020
Although human astroviruses (HAstVs) are important agents of gastroenteritis in young children, the studies aimed at characterizing their biology have been limited, in particular regarding their cell entry process. It has been shown that HAstV serotype 8
Nayeli Aguilar-Hernández   +4 more
doaj   +1 more source

Identification of Protein-disulfide Isomerase Activity in Fibronectin [PDF]

open access: yesJournal of Biological Chemistry, 1999
Assembly and degradation of fibronectin-containing extracellular matrices are dynamic processes that are up-regulated during wound healing, embryogenesis, and metastasis. Although several of the early steps leading to fibronectin deposition have been identified, the mechanisms leading to the accumulation of fibronectin in disulfide-stabilized multimers
K J, Langenbach, J, Sottile
openaire   +2 more sources

Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]

open access: yes, 2014
Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog   +22 more
core   +1 more source

S100A9 promotes pulmonary arterial hypertension by regulating mitochondria–endoplasmic reticulum interaction‐mediated inflammatory injury of endothelial cells

open access: yesInterdisciplinary Medicine, EarlyView.
Macrophage‐derived S100 calcium‐binding protein A9 (S100A9) promotes the pathological progression of pulmonary arterial hypertension (PAH). S100A9 upregulates the interaction between signal‐transducing adaptor protein 2 and leucine‐rich repeat kinase 2, thereby regulating mitochondria–endoplasmic reticulum (ER) contact.
Chen Gong   +15 more
wiley   +1 more source

Inhibitors of the protein disulfide isomerase family for the treatment of multiple myeloma

open access: yesLeukemia, 2018
Multiple Myeloma (MM) is highly sensitive to disruptions in cellular protein homeostasis. Proteasome inhibitors (PIs) are initially effective in the treatment of MM, although cures are not achievable and the emergence of resistance limits the durability ...
Reeder M. Robinson   +12 more
semanticscholar   +1 more source

DsbG, a Protein Disulfide Isomerase with Chaperone Activity [PDF]

open access: yesJournal of Biological Chemistry, 2000
DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase.
F, Shao   +3 more
openaire   +2 more sources

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