chaperone

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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 ?
Significant work remains to be done in the preclinical domain to optimize methods to target chaperone proteins but the potential for the development of a novel therapeutic approach that slows neurodegeneration in PD remains high.
Eventually, we used the STRING (vision 9.1, http://stringdb.org/) database to establish the interactions between chaperone proteins and related proteins to demonstrate the relationships between [Fe.sub.3][O.sub.4] NPs and the associated proteins [20].
We hypothesized an antagonistic effect in NRK-52E cell lines which is presented as cell death, apoptosis, and cancerization via programmed cell death protein and ras-related proteins; however there are protective mechanism proteins in NRK-52E such as chaperone proteins and glutathione related proteins.
Also, up-regulation of cyotskeletal proteins like actin, actin-capping protein, vimentin along with chaperone proteins like HSPB 1 and TCP-1could explain the structural changes and cell survival strategies adapted by the bovine satellite cells during in vitro myogenic differentiation.
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.
Cu transporters, chaperone proteins and carrier proteins make Cu available to the intricate network of biochemical systems.
"By better defining the mechanisms linking chaperone proteins to both the tau aggregation and degradation pathways, we can move toward more individualized, effective therapies targeting Alzheimer's and other distinct neurological disorders," said Dickey.
Washington, Dec 4 (ANI): In a new study, scientists found that dynamic regulation of the chaperone protein Hsp27 is required to get rid of abnormally accumulating tau in the brains of mice genetically modified to develop the memory-choking tau tangles associated with Alzheimer's disease.
When the stress-related protein FKBP51 partners with another protein known as Hsp90, this formidable chaperone protein complex prevents the clearance from the brain of the toxic tau protein associated with Alzheimer's disease.
Hsp90 is a chaperone protein, which supervises the activity of tau inside nerve cells.