Glucosidase II and MRH-domain containing proteins in the secretory pathway

Current Protein and Peptide Science

Volumn 16, Issue 1, 2015, Pages 31-48

  D’Alessio, Cecilia ^a   Dahms, Nancy M ^b  

^a UNIVERSIDAD DE BUENOS AIRES   (Argentina)

^b MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

Endoplasmic reticulum; Glucosidase II; Glycoprotein; Glycosylation; MRH domain; N glycan; Quality control; Secretory pathway

Indexed keywords

ACID HYDROLASE; ALPHA N ACETYLGLUCOSAMINIDASE; CALNEXIN; CALRETICULIN; CARBOHYDRATE BINDING PROTEIN; CATION DEPENDENT MANNOSE 6 PHOSPHATE RECEPTOR; CATION INDEPENDENT MANNOSE 6 PHOSPHATE RECEPTOR; DNA METHYLTRANSFERASE ASSOCIATED PROTEIN; GLUCOPYRANOSIDE; GLUCOSIDASE; GLUCOSIDASE II; GLUCOSIDASE II BETA SUBUNIT; GLYCAN DERIVATIVE; HYDROLASE; LECTIN; MAMMALIAN TARGET OF RAPAMYCIN; MANNOSE; MANNOSE 6 PHOSPHATE; MANNOSIDASE; OLIGOSACCHARIDE; OSTEOSARCOMA AMPLIFIED 9; PHOSPHOTRANSFERASE; SOMATOMEDIN B; SOMATOMEDIN B RECEPTOR; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; 4-NITROPHENYL-ALPHA-GLUCOSIDASE; ALPHA GLUCOSIDASE; GLYCOPROTEIN; PROTEIN BINDING; PROTEIN SUBUNIT;

ARTICLE; BINDING AFFINITY; ENDOPLASMIC RETICULUM; ENZYME PHOSPHORYLATION; HUMAN; MOLECULAR RECOGNITION; MUCOLIPIDOSIS TYPE 2; MUTAGENESIS; NONHUMAN; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SECRETORY PATHWAY; SIGNAL TRANSDUCTION; SURFACE PLASMON RESONANCE; TRANS GOLGI NETWORK; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GLYCOSYLATION; LYSOSOME; METABOLISM; PROTEIN SUBUNIT; PROTEIN TRANSPORT;

ALPHA-GLUCOSIDASES; BINDING SITES; ENDOPLASMIC RETICULUM; GLYCOPROTEINS; GLYCOSYLATION; LECTINS; LYSOSOMES; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN SUBUNITS; PROTEIN TRANSPORT; RECEPTOR, IGF TYPE 2; SECRETORY PATHWAY; TRANSFERASES (OTHER SUBSTITUTED PHOSPHATE GROUPS);

EID: 84930936566     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/1389203716666150213160438     Document Type: Article

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