PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12377772-4	2002	Highest affinity of the syndecan-4 cytoplasmic domain was seen with phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5P)(2)) and phosphatidylinositol 4-phosphate, and both promoted syndecan-4 oligomerization.	Phosphatidylinositol 4,5-Diphosphate	68-105	syndecan 4	Homo sapiens	24-34	
16310216-2	2006	We have shown that the syndecan-4 cytoplasmic domain (4L) forms oligomeric complexes that bind to and stimulate PKCalpha activity in the presence of PtdIns(4,5)P2, emphasizing the importance of multimerization in the regulation of PKCalpha activation.	Phosphatidylinositol 4,5-Diphosphate	149-162	syndecan 4	Homo sapiens	23-33	
16310216-3	2006	Oligomerization of the cytoplasmic domain of syndecan-4 is regulated either positively by PtdIns(4,5)P2 or negatively by phosphorylation of serine 183.	Phosphatidylinositol 4,5-Diphosphate	90-103	syndecan 4	Homo sapiens	45-55	
16310216-4	2006	Phosphorylation results in reduced PKCalpha activity by inhibiting PtdIns(4,5)P2-dependent oligomerization of the syndecan-4 cytoplasmic domain.	Phosphatidylinositol 4,5-Diphosphate	67-80	syndecan 4	Homo sapiens	114-124	
12241528-5	2002	Syndecan-4 also binds and activates protein kinase Calpha in the presence of phosphatidylinositol 4,5-bisphosphate, and regulates signalling by Rho-family GTPases and focal adhesion kinase.	Phosphatidylinositol 4,5-Diphosphate	77-114	syndecan 4	Homo sapiens	0-10	
12011116-2	2002	It appears now that the syndecan-4 core protein, a transmembrane proteoglycan shown previously to bind phosphatidylinositol 4,5-bisphosphate (PIP(2)) and activate PKC alpha, participates in mediating the effects of fibroblast growth factor (FGF)2 on cell function.	Phosphatidylinositol 4,5-Diphosphate	103-140	syndecan 4	Homo sapiens	24-34	
11916978-5	2002	Syndecan-4/PIP(2)-dependent PKCalpha activity was significantly increased in PKCdelta DN cells, while PKCdelta overexpression was accompanied by decreased PKCalpha activity.	Phosphatidylinositol 4,5-Diphosphate	11-17	syndecan 4	Homo sapiens	0-10	
11916978-1	2002	The phosphorylation state of Ser(183) in the cytoplasmic tail of syndecan-4 determines the binding affinity of the cytoplasmic tail to phosphatidylinositol 4,5-bisphosphate (PIP(2)), the capacity of the tail to multimerize, and its ability to activate protein kinase C (PKC) alpha.	Phosphatidylinositol 4,5-Diphosphate	135-172	syndecan 4	Homo sapiens	65-75	
11728825-5	2001	The cytoplasmic tail of the ubiquitously expressed syndecan-4 is distinct from the other syndecans in its capacity to bind phosphatidylinositol 4,5-bisphosphate (PIP2) and to activate protein kinase C (PKC) alpha.	Phosphatidylinositol 4,5-Diphosphate	123-160	syndecan 4	Homo sapiens	51-61	
11728825-5	2001	The cytoplasmic tail of the ubiquitously expressed syndecan-4 is distinct from the other syndecans in its capacity to bind phosphatidylinositol 4,5-bisphosphate (PIP2) and to activate protein kinase C (PKC) alpha.	Phosphatidylinositol 4,5-Diphosphate	162-166	syndecan 4	Homo sapiens	51-61	
10504290-4	1999	Overexpression of syndecan-4 increases focal adhesion formation, whereas a partially truncated core protein that lacks the binding site for protein kinase C(&agr;) and phosphatidylinositol 4, 5-bisphosphate acts as a dominant negative inhibitor of focal adhesion formation.	Phosphatidylinositol 4,5-Diphosphate	172-210	syndecan 4	Homo sapiens	18-28	
10625452-0	1999	Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C. Recent studies have demonstrated that the cytoplasmic tail of syndecan-4, a widely expressed transmembrane proteoglycan, can activate protein kinase Calpha in vitro, in combination with phosphatidylinositol-4,5-bisphosphate (PI-4,5-P(2)).	Phosphatidylinositol 4,5-Diphosphate	0-37	syndecan 4	Homo sapiens	66-76	
10625452-0	1999	Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C. Recent studies have demonstrated that the cytoplasmic tail of syndecan-4, a widely expressed transmembrane proteoglycan, can activate protein kinase Calpha in vitro, in combination with phosphatidylinositol-4,5-bisphosphate (PI-4,5-P(2)).	Phosphatidylinositol 4,5-Diphosphate	0-37	syndecan 4	Homo sapiens	162-172	
10625452-0	1999	Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C. Recent studies have demonstrated that the cytoplasmic tail of syndecan-4, a widely expressed transmembrane proteoglycan, can activate protein kinase Calpha in vitro, in combination with phosphatidylinositol-4,5-bisphosphate (PI-4,5-P(2)).	Phosphatidylinositol 4,5-Diphosphate	286-323	syndecan 4	Homo sapiens	66-76	
10625452-0	1999	Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C. Recent studies have demonstrated that the cytoplasmic tail of syndecan-4, a widely expressed transmembrane proteoglycan, can activate protein kinase Calpha in vitro, in combination with phosphatidylinositol-4,5-bisphosphate (PI-4,5-P(2)).	Phosphatidylinositol 4,5-Diphosphate	286-323	syndecan 4	Homo sapiens	162-172	
9748216-6	1998	The cytoplasmic tail of syndecan-4 is known to undergo multimerization and to activate protein kinase Calpha (PKCalpha), with both events depending on the presence of the commonly occurring phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2).	Phosphatidylinositol 4,5-Diphosphate	242-246	syndecan 4	Homo sapiens	24-34	
9748216-8	1998	Because Ser183 is adjacent to positively charged lysine groups that resemble PIP2-binding regions in several other proteins, phosphorylation of this serine may affect the binding affinity of the syndecan-4 cytoplasmic tail to PIP2.	Phosphatidylinositol 4,5-Diphosphate	77-81	syndecan 4	Homo sapiens	195-205	
9748216-8	1998	Because Ser183 is adjacent to positively charged lysine groups that resemble PIP2-binding regions in several other proteins, phosphorylation of this serine may affect the binding affinity of the syndecan-4 cytoplasmic tail to PIP2.	Phosphatidylinositol 4,5-Diphosphate	226-230	syndecan 4	Homo sapiens	195-205	
9748216-9	1998	We found that the Ser183-phosphorylated cytoplasmic tail of syndecan-4 has indeed a significantly lower affinity to PIP2 compared with the nonphosphorylated tail.	Phosphatidylinositol 4,5-Diphosphate	116-120	syndecan 4	Homo sapiens	60-70	
9748216-11	1998	We conclude that Ser183 phosphorylation regulates syndecan-4-dependent activation of PKCalpha by reducing the affinity to PIP2 and inhibiting the oligomerization of syndecan-4 cytoplasmic tails.	Phosphatidylinositol 4,5-Diphosphate	122-126	syndecan 4	Homo sapiens	50-60	
9582338-0	1998	Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate.	Phosphatidylinositol 4,5-Diphosphate	79-116	syndecan 4	Homo sapiens	24-34	
9582338-10	1998	These findings reveal that PIP2 promotes oligomerization of syndecan-4 cytoplasmic domain for transmembrane signaling and cell-matrix adhesion.	Phosphatidylinositol 4,5-Diphosphate	27-31	syndecan 4	Homo sapiens	60-70	
9553124-7	1998	Addition of the cytoplasmic syndecan-4 peptide, but not equivalent syndecan-1 or syndecan-2 peptides, potentiated the partial activation of PKCalpha beta gamma by PIP2, resulting in activity greater than that observed with phosphatidylserine, diolein, and calcium.	Phosphatidylinositol 4,5-Diphosphate	163-167	syndecan 4	Homo sapiens	28-38	
9115237-5	1997	A synthetic peptide encompassing the whole cytoplasmic domain of syndecan-4 (4L) containing a membrane-proximal basic sequence did not form higher order oligomers and could not regulate the activity of PKCalphabetagamma unless induced to aggregate by phosphatidylinositol 4,5-bisphosphate.	Phosphatidylinositol 4,5-Diphosphate	251-288	syndecan 4	Homo sapiens	65-75