PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8681440-8	1996	PKC alpha, epsilon and delta, but not PKC eta and zeta, were down-regulated by treating both cell types with bryostatin; pre-treatment of cells with bryostatin inhibited stsp-induced protein cross-linking and marker expression, suggesting a necessity for the alpha, delta and/or epsilon isoforms in stsp-induced differentiation.	Bryostatins	109-119	protein kinase C, alpha	Mus musculus	0-28	
7987836-5	1994	Pretreatment of v-rasHa keratinocytes with bryostatin to block PKC function restored Ca(2+)-mediated expression of K1 and K10 and blocked abnormal expression of K8, suggesting that these responses are mediated by the PKC pathway.	Bryostatins	43-53	protein kinase C, alpha	Mus musculus	63-66	
7870033-5	1995	After translocation, PKC-alpha, -delta, -eta, and -epsilon were down-regulated; the down-regulation of PKC-epsilon contrasts with its retention after phorbol-12-myristate-13-acetate or bryostatin treatment.	Bryostatins	185-195	protein kinase C, alpha	Mus musculus	21-58	
7987836-5	1994	Pretreatment of v-rasHa keratinocytes with bryostatin to block PKC function restored Ca(2+)-mediated expression of K1 and K10 and blocked abnormal expression of K8, suggesting that these responses are mediated by the PKC pathway.	Bryostatins	43-53	protein kinase C, alpha	Mus musculus	217-220	
7987836-6	1994	Furthermore, expression of K1 is restored at bryostatin doses which specifically down-modulate PKC-alpha, the only Ca(2+)-dependent PKC isozyme detected in cultured keratinocytes.	Bryostatins	45-55	protein kinase C, alpha	Mus musculus	95-104	
7987836-6	1994	Furthermore, expression of K1 is restored at bryostatin doses which specifically down-modulate PKC-alpha, the only Ca(2+)-dependent PKC isozyme detected in cultured keratinocytes.	Bryostatins	45-55	protein kinase C, alpha	Mus musculus	95-98	
7987836-8	1994	Pretreatment of v-rasHa keratinocytes with bryostatin blocked expression of late markers in these cells, and this response was correlated with down-regulation of PKC-alpha.	Bryostatins	43-53	protein kinase C, alpha	Mus musculus	162-171	
32209043-4	2020	The structure-activity relationship of bryostatins has been well established, with the identification of key pharmacopjoric features important for PKC modulation.	Bryostatins	39-50	protein kinase C, alpha	Mus musculus	147-150