The NC1 Domain of Collagen IV Encodes a Novel Network Composed of the α1, α2, α5, and α6 Chains in Smooth Muscle Basement Membranes

Journal of Biological Chemistry

Volumn 276, Issue 30, 2001, Pages 28532-28540

  Borza, Dorin Bogdan ^a   Bondar, Olga ^a   Ninomiya, Yoshifumi ^b   Sado, Yoshikazu ^c   Naito, Ichiro ^c   Todd, Parvin ^a   Hudson, Billy G ^a  

^a UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

^b OKAYAMA UNIVERSITY MEDICAL SCHOOL   (Japan)

^c Shigei Medical Research Institute   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; ANTIBODIES; BIOLOGICAL MEMBRANES; DISEASES; ELECTROPHORESIS; MUSCLE;

TISSUE-SPECIFIC DISTRIBUTION;

COLLAGEN;

COLLAGEN TYPE 4; COLLAGENASE; ISOPROTEIN; MONOCLONAL ANTIBODY; COLLAGEN;

AFFINITY CHROMATOGRAPHY; ALPHA CHAIN; ALPORT SYNDROME; ANIMAL TISSUE; AORTA; ARTICLE; BASEMENT MEMBRANE; BLADDER; CONTROLLED STUDY; MOLECULAR RECOGNITION; NC1 DOMAIN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; SEQUENCE HOMOLOGY; SMOOTH MUSCLE; SOLUBILIZATION; TISSUE SPECIFICITY; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING; X CHROMOSOME LINKED DISORDER; ANIMAL; BIOLOGICAL MODEL; CATTLE; CHEMISTRY; CYTOLOGY; ELECTRON MICROSCOPY; FLUORESCENT ANTIBODY TECHNIQUE; GENETIC LINKAGE; GENETICS; HUMAN; IMMUNOHISTOCHEMISTRY; METABOLISM; MUTATION; NEPHRITIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; X CHROMOSOME;

ANIMALIA;

ANIMALS; AORTA; BLOTTING, WESTERN; CATTLE; COLLAGEN; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; HUMANS; IMMUNOHISTOCHEMISTRY; LINKAGE (GENETICS); MICROSCOPY, ELECTRON; MODELS, BIOLOGICAL; MUSCLE, SMOOTH; MUTATION; NEPHRITIS, HEREDITARY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; URINARY BLADDER; X CHROMOSOME;

EID: 0035958849     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M103690200     Document Type: Article

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