PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31209055-8	2019	Outside the membrane this symmetry is broken by the disulfide-bridged dimerization of the extracellular Ig domains of Igalpha and Igbeta.	Disulfides	52-61	CD79b molecule	Homo sapiens	130-136	
20696394-2	2010	Here we show that the extracellular domains of murine and human Igbeta form an I-set immunoglobulin-like structure with an interchain disulfide between cysteines on their G strands.	Disulfides	134-143	CD79b molecule	Homo sapiens	64-70	
20696394-4	2010	An Igalphabeta heterodimer model was generated based on the unique disulfide-bonded Igbeta dimer.	Disulfides	67-76	CD79b molecule	Homo sapiens	84-90	
17675462-2	2007	We recently identified a patient with a homozygous amino acid substitution in Igbeta, a glycine to serine at codon 137, adjacent to the cysteine required for the disulfide bond between Igalpha and Igbeta.	Disulfides	162-171	CD79b molecule	Homo sapiens	78-84	
17675462-2	2007	We recently identified a patient with a homozygous amino acid substitution in Igbeta, a glycine to serine at codon 137, adjacent to the cysteine required for the disulfide bond between Igalpha and Igbeta.	Disulfides	162-171	CD79b molecule	Homo sapiens	197-203	
17675462-4	2007	Using expression vectors in 293T cells or Jurkat T cells, we show that the mutant Igbeta can form disulfide-linked complexes and bring the mu H chain to the cell surface as part of the BCR but is inefficient at both tasks.	Disulfides	98-107	CD79b molecule	Homo sapiens	82-88	
10880522-1	2000	The B cell antigen receptor (BCR) is a large complex that consists of a disulfide-linked tetramer of two transmembrane heavy (mu) chains and two light (lambda or kappa) chains in association with a heterodimer of Igalpha and Igbeta.	Disulfides	72-81	CD79b molecule	Homo sapiens	225-231	
8639560-2	1996	Key to this process appears to be the interaction of the tyrosine kinase SH2 domains with the tyrosine-phosphorylated cytoplasmic domain of Ig-alpha, a disulfide-bonded heterodimeric (with Ig-beta or Ig-gamma) transmembrane protein that noncovalently associates with the antigen receptor immunoglobin chains.	Disulfides	152-161	CD79b molecule	Homo sapiens	189-196	
8011288-4	1994	Components of this disulfide linked heterodimeric complex, Ig-alpha and Ig-beta, contain an approximately 26 residue sequence motif termed ARH1, also known as TAM, which binds to cytoplasmic effectors, including src-family tyrosine kinases, and contains all structural information needed for signal transduction.	Disulfides	19-28	CD79b molecule	Homo sapiens	72-79	
1401917-8	1992	Thus, a product of the B29 gene is a component of the AgR complex in human and murine B cells, occurring as a disulfide linked dimer with product(s) of the mb-1 gene.	Disulfides	110-119	CD79b molecule	Homo sapiens	23-26	
1401917-0	1992	Human pre-B and B cell membrane mu-chains are noncovalently associated with a disulfide-linked complex containing a product of the B29 gene.	Disulfides	78-87	CD79b molecule	Homo sapiens	131-134	
1401917-2	1992	Studies of murine B cells conducted in several laboratories, including our own, suggest that products of the mb-1 (IgM-alpha or IgD-alpha) and B29 (Ig-beta, Ig-gamma) genes occur as disulfide-linked alpha/beta and alpha/gamma heterodimers that are noncovalently associated with mIgM and mIgD.	Disulfides	182-191	CD79b molecule	Homo sapiens	143-146	
1707541-4	1991	mIgM is associated with the MB-1 protein, which is disulfide-linked to a protein designated Ig-beta.	Disulfides	51-60	CD79b molecule	Homo sapiens	92-99	
1707541-5	1991	mIgD is not associated with MB-1 but is with IgD-alpha, which is also disulfide-linked to Ig-beta.	Disulfides	70-79	CD79b molecule	Homo sapiens	90-97