PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29992271-6	2018	By solution-state nuclear magnetic resonance, one of these CHAMP peptides was shown to bind primarily the integrin beta1 TM domain, which itself has a Gly-X3-Gly motif.	Glycine	151-154	integrin subunit beta 1	Homo sapiens	106-120	
29356040-8	2018	This signal transduction was initiated by competitive binding of CD147 with integrin beta1 that interrupted the interaction between the Arg-Gly-Asp motif of fibronectin and integrin beta1.	Glycine	140-143	integrin subunit beta 1	Homo sapiens	76-90	
29356040-8	2018	This signal transduction was initiated by competitive binding of CD147 with integrin beta1 that interrupted the interaction between the Arg-Gly-Asp motif of fibronectin and integrin beta1.	Glycine	140-143	integrin subunit beta 1	Homo sapiens	173-187	
29992271-6	2018	By solution-state nuclear magnetic resonance, one of these CHAMP peptides was shown to bind primarily the integrin beta1 TM domain, which itself has a Gly-X3-Gly motif.	Glycine	158-161	integrin subunit beta 1	Homo sapiens	106-120	
28877491-10	2017	These results demonstrate that only the amphiphile that thinned Ld lipid domains increased beta1-integrin-Arg-Gly-Asp-peptide affinity and valency, thus implicating Ld domains in modulation of integrin adhesion, nascent adhesion formation, and cell migration.	Glycine	110-113	integrin subunit beta 1	Homo sapiens	91-105	
35579101-5	2022	After instillation, the presence of integrin-beta1 endows coated nanoparticles with steady adhesion via specific binding to Arg-Gly-Asp sequence on the fibronectin of ocular epithelium, achieving durable retention on ocular surface.	Glycine	128-131	integrin subunit beta 1	Homo sapiens	36-50	
17877151-5	2007	Cell adhesion was partially inhibited by Arg-Gly-Asp (RGD) peptide, anti-beta1 integrin suggesting that integrin beta1 receptors have roles to play in the process.	Glycine	45-48	integrin subunit beta 1	Homo sapiens	104-118	
9548475-7	1997	Thus, the carboxyl-terminal five amino acids, Lys-Tyr-Glu-Gly-Lys (KYEGK), of the beta1 integrin cytoplasmic domain are critical for the coordinate tyrosine phosphorylation of three non-FAK substrates in human T cells.	Glycine	58-61	integrin subunit beta 1	Homo sapiens	82-96	
11603727-9	2001	Blocking of the beta1-integrin with cyclic-peptides containing the Arg-Gly-Asp sequences and antibodies reduced chondrocyte attachment to Type II collagen by 93%.	Glycine	71-74	integrin subunit beta 1	Homo sapiens	16-30