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 ?
family of Cu bearing proteins, cuproenzymes, Cu transporters and Cu chaperone proteins have been manifested for enabling Cu to show its relevance in biological health.
Similar to our RAP molecule, Mesd is a natural human receptor chaperone protein that has the potential to act as both a receptor targeting therapeutic, as well as a targeted delivery platform that could be used to deliver other drugs.
The article reports on certain aspects of MANFtrafficking inside the cell and its secretion outside the cell, as well as MANF's interactions with other chaperone proteins of the endoplasmic reticulum (ER).
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.
Hsp90 is a chaperone protein required for the proper folding and activation of cellular proteins, particularly kinases.
Hsp90 is a chaperone protein for a variety of oncogene products (such as Her2 and Raf) and their downstream signaling molecules (such as Akt and Erk).
Hsp90 is a chaperone protein for a variety of oncogenes (such as Her2 and Raf) and their downstream signaling molecules (such as Akt and Erk).
As a chaperone protein, HSP90 plays an important role in regulating the function and activity of numerous clients, or signalling, proteins that have been shown to be critical to cancer cell growth, proliferation and survival.
Sections of brain tissue were then evaluated for each of the following: 1) chaperone protein HSP70; 2) the number of cells with the characteristic DNA cleavage caused by apoptosis; 3) the microglial cell marker IB4-receptor; or 4) a marker for newly developing brain cells called doublecortin.
This activity against cancers resistant to a kinase inhibitor is consistent with the underlying rationale of targeting the Hsp90 chaperone protein rather than the kinase itself.
XL888 is an orally available small molecule inhibitor of HSP90, which is a chaperone protein that promotes the activity and stability of a range of key regulatory proteins, including kinases.