Search Results - "Cohen‐Doyle, M. F."

The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules by Vassilakos, A., Cohen‐Doyle, M. F., Peterson, P. A., Jackson, M. R., Williams, D. B.

“…Calnexin, a membrane protein of the endoplasmic reticulum, is generally thought to function as a molecular chaperone, based on indirect or correlative…”
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Interaction of MHC Class I Molecules With the Transporter Associated with Antigen Processing by Suh, Woong-Kyung, Cohen-Doyle, Myrna F., Fruh, Klaus, Wang, Kena, Peterson, Per A., Williams, David B.

“…The transporter associated with antigen processing (TAP) delivers cytosolic peptides into the endoplasmic reticulum (ER) where they bind to nascent class I…”
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Calnexin Discriminates between Protein Conformational States and Functions as a Molecular Chaperone In Vitro by Ihara, Yoshito, Cohen-Doyle, Myrna F, Saito, Yoshiro, Williams, David B

“…Although calnexin is thought to function as a molecular chaperone for glycoproteins, a prevalent view is that it cannot distinguish between protein…”
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Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide by Degen, E, Cohen-Doyle, M F, Williams, D B

“…Previously, we showed that an 88-kD protein (p88) associates rapidly and quantitatively with newly synthesized murine major histocompatibility complex class I…”
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Functional Relationship between Calreticulin, Calnexin, and the Endoplasmic Reticulum Luminal Domain of Calnexin by Danilczyk, Ursula G., Cohen-Doyle, Myrna F., Williams, David B.

“…Calnexin is a membrane protein of the endoplasmic reticulum (ER) that functions as a molecular chaperone and as a component of the ER quality control…”
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Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90) by Jackson, Michael R., Cohen-Doyle, Myrna F., Peterson, Per A., Williams, David B.

“…Assembled class I histocompatibility molecules, consisting of heavy chain, $\beta_2$-microglobulin, and peptide ligand, are transported rapidly to the cell…”
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Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins by Saito, Yoshiro, Ihara, Yoshito, Leach, Michael R., Cohen-Doyle, Myrna F., Williams, David B.

“…Calreticulin (CRT) is thought to be a molecular chaperone that interacts with glycoproteins exclusively through a lectin site specific for monoglucosylated…”
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Localization of the Lectin, ERp57 Binding, and Polypeptide Binding Sites of Calnexin and Calreticulin by Leach, Michael R., Cohen-Doyle, Myrna F., Thomas, David Y., Williams, David B.

“…Calnexin and calreticulin are membrane-bound and soluble chaperones, respectively, of the endoplasmic reticulum (ER) which interact transiently with a broad…”
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Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both β2-microglobulin and peptide by DEGEN, E, COHEN-DOYLE, M. F, WILLIAMS, D. B

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Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alpha3 domain by Suh, W K, Derby, M A, Cohen-Doyle, M F, Schoenhals, G J, Früh, K, Berzofsky, J A, Williams, D B

“…In human cells the association of MHC class I molecules with TAP is thought to be mediated by a third protein termed tapasin. We now show that tapasin is…”
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Interaction of Murine MHC Class I Molecules with Tapasin and TAP Enhances Peptide Loading and Involves the Heavy Chain alpha sub(3) Domain by Suh, W-K, Derby, MA, Cohen-Doyle, M F, Schoenhals, G J, Frueh, K, Berzofsky, JA, Williams, D B

“…In human cells the association of MHC class I molecules with TAP is thought to be mediated by a third protein termed tapasin. We now show that tapasin is…”
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Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta sub(2)-microglobulin and peptide by Degen, E, Cohen-Doyle, M F, Williams, D B

“…Previously, we showed that an 88-kD protein (p88) associates rapidly and quantitatively with newly synthesized murine major histocompatibility complex class I…”
Get full text