Diverse roles of conserved asparagine-linked glycan sites on tyrosinase family glycoproteins

Experimental Cell Research

Volumn 267, Issue 1, 2001, Pages 115-125

  Xu, Yiqing ^a   Bartido, Shirley ^a   Setaluri, Vijayasaradhi ^b   Qin, Jie ^a   Yang, George ^a   Houghton, Alan N ^a  

^a Department of Obstetrics Gynecology   (United States)

^b WAKE FOREST SCHOOL OF MEDICINE   (United States)

Author keywords

Asparagine; Evolution; Glycosylation; N glycan; Protein sorting; Tyrosinase; Tyrosinase related protein

Indexed keywords

ASPARAGINE DERIVATIVE; GLYCAN DERIVATIVE; GLYCOPROTEIN; MONOPHENOL MONOOXYGENASE; POLYPEPTIDE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENDOCYTOSIS; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; GENETIC CONSERVATION; MOUSE; MULTIGENE FAMILY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN TARGETING; SITE DIRECTED MUTAGENESIS;

VERTEBRATA;

EID: 0035398555     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2001.5232     Document Type: Article

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