The MHC class i heavy chain structurally conserved cysteines 101 and 164 participate in HLA-B27 dimer formation

Antioxidants and Redox Signaling

Volumn 16, Issue 1, 2012, Pages 33-43

  Lenart, Izabela ^a   Guiliano, David B ^a   Burn, Garth ^a   Campbell, Elaine C ^b   Morley, Kenneth D ^c   Fussell, Helen ^d   Powis, Simon J ^b   Antoniou, Antony N ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF ST ANDREWS   (United Kingdom)

^c NINEWELLS HOSPITAL   (United Kingdom)

^d NHS BLOOD AND TRANSPLANT   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYSTEINE 101; CYSTEINE 164; HLA B27 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; UNCLASSIFIED DRUG;

ARTHRITIS; ARTICLE; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; ENDOPLASMIC RETICULUM STRESS; HEAVY CHAIN; HUMAN; HUMAN CELL; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN CONFORMATION;

ACTIVATING TRANSCRIPTION FACTOR 6; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CONSERVED SEQUENCE; CYSTEINE; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; HLA-B27 ANTIGEN; HUMANS; MOLECULAR WEIGHT; OXIDATION-REDUCTION; PROTEIN MULTIMERIZATION; RATS;

EID: 81155127506     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2010.3693     Document Type: Article

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