chaperone

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Related to Chaperone protein: GroEL

chap·e·rone

(shap-ĕ-rōn),
1. A protein required for the proper folding and/or assembly of another protein or protein complex.
2. One who accompanies a physician during physical examination of a patient of the opposite gender (from the physician).
[Eng. escort, protector, fr. Fr. chaperon, hood, fr. chape, cape, fr. L.L. cappa, fr. L. caput, head]

chaperone

or

chaperon

(shăp′ə-rōn′)
n.
Any of a diverse group of proteins that assist macromolecules, such as proteins and nucleic acids, to assemble and fold into the proper three-dimensional structure as they are being synthesized. Also called molecular chaperone.

chap′er·on′age (-rō′nĭj) n.

chaperone

Cell biology
Any of a class of cytoplasmic proteins found in both prokaryotes and eukaryotes, which facilitate the correct assembly or disassembly of newly synthesised oligomeric protein complexes, participating in transmembrane targeting and protein folding.

Medspeak-UK
A person, generally employed by a medical doctor or (NHS) hospital trust, who stays with the patient while the doctor is examining a patient or performing a procedure.
 
Vox populi
A person who accompanies a child or adolescent under the age of majority (adulthood) during an event such as a date or a school dance.

chap·e·rone

(shap'ĕ-rōn)
1. A protein required for the proper folding and/or assembly of another protein or protein complex.
2. One who accompanies a physician during physical examination of a patient of the opposite gender (from that of the physician).
[Eng. escort, protector, fr. Fr. chaperon, hood, fr. chape, cape, fr. L.L. cappa, fr. L. caput, head]

chaperone

a PROTEIN MOLECULE which can assist in the folding, assembly or transport of other proteins in a CELL.
References in periodicals archive ?
Keeping the importance of cupric Cu in biological function, an elaborate mechanism is set forth by Nature for maintaining Cu homeostasis, which includes a wide array of proteins namely (i) family of Cu bearing proteins, (ii) cuproenzymes, (iii) Cu transporters and (iv) Cu chaperone proteins. It is not surprising for the redundant machinery that Cu is enjoying out of several heavy metals for its transport and participation in cellular metabolism, which guarantees the survival of living organisms as conditioned by the strategies and mechanisms of the evolution of metallic proteins.
In addition, Hsp27 can only be effective in helping maintain healthy tau turnover if the chaperone protein interacts with tau while it's still soluble-before tau has developed into solid nerve-killing tangles.
Under physiological conditions, the aim of chaperone proteins is to provide protection against aggregation of newly emerging polypeptides and to mediate their correct folding.
This is a highly selective and constitutive subtype of autophagy that utilizes chaperone proteins and lysosomal receptors to directly target proteins into the lysosomal lumen for their degradation, under both physiological and pathological conditions to maintain cellular homeostasis [69-73].
The pathogenic G2019S, R1441C, and Y1699C LRRK2 mutations were shown to enhance the clearance of the trans-Golgi network (TGN) via a protein complex including the chaperone proteins Hsp70 and BAG5 plus Rab7L1 and Cyclin G Associated Kinase (GAK), which are both located in risk loci for sporadic
DNAJ/Hsp40 proteins are indeed important for protein translation, folding, unfolding, translocation and degradation, primarily by stimulating the ATPase activity of chaperone proteins, Hsp70 (Qui et al., 2006).
Ways of targeting chaperone proteins and other elements of the protein quality control (PQC) system are discussed, followed by sequential treatment of proteasomal degradation, unselective and selective disposal systems, particularly autophagic mechanisms.
As a constituent of the endoplasmic reticulum, in conjunction with other chaperone proteins, PDIA3 assists in glycoprotein folding (Bedard et al.
Comparative 2DE analysis also defined decreased expression of ER chaperone proteins such as PDI and GRP58, which may lead to increased unfolded protein load in mesangial cells and induction of proteasomal degradation processes.
We classified proteins into chaperone proteins, cell death related and apoptotic proteins, ras-related proteins, and glutathione related proteins.
Molecular chaperone proteins of interest were added at various concentrations to measure their ability to suppress rhodanese aggregation.
They found that the chaperone proteins bind far more strongly to the mutated proteins in an effort to keep the lens clear.