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

/chap·er·one/ (shap´er-ōn) someone or something that accompanies and oversees another.
molecular chaperone  any of a diverse group of proteins that oversee the correct intracellular folding and assembly of polypeptides without being components of the final structure.

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.

chaperone

a family of proteins that aid in the folding of target proteins.
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.
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.
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.
They found that the chaperone proteins bind far more strongly to the mutated proteins in an effort to keep the lens clear.
Editors Kornberg, Rothman, Stubbe, and Thorner have chosen a wide range of topics for this work such as DNA replication, epigenetic readout mechanisms, protein structure, the role of chaperone proteins in the folding of newly translated proteins, voltage gated membrane channels, peroxisomes, and mRNA translation.
Thus, iron is almost always bound to transporter and chaperone proteins.
Increased synthesis of glutathione, humanin, and mitochondrial chaperone proteins are other additional consequences of increased mitogenesis and which would help ensure proteostasis.
The final straw could be the loss of chaperone proteins, which oversee protein-folding, or a strike by the cellular machinery that transports or breaks down proteins, causing crowding in the cell that foments aggregation.
The unfolded protein response maintains a balance between unfolded proteins and chaperones by regulating the rate of transcription and translation of chaperone proteins (David Ron, University of Cambridge, Cambridge, UK).
Hunt's postdoctoral research focused on X-ray crystallographic studies of molecular chaperone proteins.