PRC1/YMR297W Literature Guide Help

Other names published for PRC1: LBC1, CPY, carboxypeptidase C PRC1, YMR297W

PRC1 - Protein Physical Properties (23)

ReferenceOther Genes Addressed
Izawa T, et al.  (2012) Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation. Mol Biol Cell 23(7):1283-93
Nagayama M, et al.  (2012) Mutated intramolecular chaperones generate high-activity isomers of mature enzymes. Biochemistry 51(17):3547-53
Wang S, et al.  (2012) Development of a method for the efficient release of N-glycans from glycoproteins generating native deglycosylated proteins. Enzyme Microb Technol 51(3):139-42
Chawla A, et al.  (2011) Attenuation of yeast UPR is essential for survival and is mediated by IRE1 kinase. J Cell Biol 193(1):41-50
Yoshida T, et al.  (2006) Comparative analysis of binding energy of chymostatin with human cathepsin a and its homologous proteins by molecular orbital calculation. J Chem Inf Model 46(5):2093-103
Baxter SM, et al.  (2004) Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast. Mol Cell Proteomics 3(3):209-25
Kato M, et al.  (2003) The propeptide in the precursor form of carboxypeptidase Y ensures cooperative unfolding and the carbohydrate moiety exerts a protective effect against heat and pressure. Eur J Biochem 270(22):4587-93
Mima J, et al.  (2003) The multiple site binding of carboxypeptidase Y inhibitor (IC) to the cognate proteinase. Implications for the biological roles of the phosphatidylethanolamine-binding protein. J Biol Chem 278(32):29792-8
Stennicke HR, et al.  (1996) Studies on the hydrolytic properties of (serine) carboxypeptidase Y. Biochemistry 35(22):7131-41
Simons JF, et al.  (1995) BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J Cell Biol 130(1):41-9
Mortensen UH and Breddam K  (1994) A conserved glutamic acid bridge in serine carboxypeptidases, belonging to the alpha/beta hydrolase fold, acts as a pH-dependent protein-stabilizing element. Protein Sci 3(5):838-42
Sorensen SO and Winther JR  (1994) Active-site residues of procarboxypeptidase Y are accessible to chemical modification. Biochim Biophys Acta 1205(2):289-93
Sorensen SO, et al.  (1994) pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro. Eur J Biochem 220(1):19-27
te Heesen S and Aebi M  (1994) The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae. Eur J Biochem 222(2):631-7
Ballou L, et al.  (1990) Revision of the oligosaccharide structures of yeast carboxypeptidase Y. Proc Natl Acad Sci U S A 87(9):3368-72
Distel B, et al.  (1983) Synthesis and maturation of the yeast vacuolar enzymes carboxypeptidase Y and aminopeptidase I. Biochim Biophys Acta 741(1):128-35
Nakagawa Y, et al.  (1982) Carboxypeptidase Y from Saccharomyces cerevisiae. Conformational differences reflected in kinetic behaviour in water and deuterium oxide. Biochim Biophys Acta 706(1):141-3
Hashimoto C, et al.  (1981) Carbohydrate chains on yeast carboxypeptidase Y are phosphorylated. Proc Natl Acad Sci U S A 78(4):2244-8
Chang WT and Douglas KT  (1980) Mechanistic studies of carboxypeptidase Y from Saccharomyces cerevisiae. pH and pD profiles and inactivation at low pH (pD) values. Biochem J 187(3):843-9
Margolis HC, et al.  (1978) Multiple forms of carboxypeptidase Y from Saccharomyces cerevisiae. Kinetic demonstration of effects of carbohydrate residues on the catalytic mechanism of a glycoenzyme. J Biol Chem 253(21):7891-7
Hayashi R, et al.  (1975) Evidence for an essential histidine in carboxypeptidase Y. Reaction with the chloromethyl ketone derivative of benzyloxycarbonyl-L-phenylalanine. J Biol Chem 250(13):5221-6
Hayashi R, et al.  (1973) Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. J Biol Chem 248(7):2296-302
Hayashi R, et al.  (1973) Serine at the active center of yeast carboxypeptidase. J Biol Chem 248(24):8366-9