PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3120710-3	1987	In the DNA binding domain of poly(ADP-ribose) polymerase, there are predicted alpha-helix-turn-alpha-helix structures and two sequences each of about 100 amino acids that are similar to each other containing potential cysteine-zinc DNA binding structures.	Cysteine	218-226	poly(ADP-ribose) polymerase 1	Homo sapiens	29-56	
33940558-3	2021	In response to DNA strand breaks, PARP1 covalently attaches ADP-ribose moieties to arginine, glutamate, aspartate, cysteine, lysine, and serine acceptor sites on both itself and other proteins.	Cysteine	115-123	poly(ADP-ribose) polymerase 1	Homo sapiens	34-39	
10652256-7	2000	The HNE-mediated activation of caspases, cleavage of PARP and DNA fragmentation were blocked by antioxidants cysteine, N-acety-L-cysteine and dithiothreitol, but not by two other HNE-reactive amino acids lysine and histidine, or by cystine, the oxidized form of cysteine.	Cysteine	109-117	poly(ADP-ribose) polymerase 1	Homo sapiens	53-57	
8896444-7	1996	Several cysteine and serine protease inhibitors prevented apoptotic DNA fragmentation by acting either upstream or downstream of the DEVD-sensitive protease(s) activation and PARP cleavage.	Cysteine	8-16	poly(ADP-ribose) polymerase 1	Homo sapiens	175-179	
32966781-5	2020	Under physiological conditions, AI-ETD identifies 450 ADPr sites on low-abundant proteins, including in vivo cysteine modifications on poly(ADP-ribosyl)polymerase (PARP) 8 and tyrosine modifications on PARP14, hinting at specialist enzymatic functions for these enzymes.	Cysteine	109-117	poly(ADP-ribose) polymerase 1	Homo sapiens	135-162	
32966781-5	2020	Under physiological conditions, AI-ETD identifies 450 ADPr sites on low-abundant proteins, including in vivo cysteine modifications on poly(ADP-ribosyl)polymerase (PARP) 8 and tyrosine modifications on PARP14, hinting at specialist enzymatic functions for these enzymes.	Cysteine	109-117	poly(ADP-ribose) polymerase 1	Homo sapiens	164-168	
25043379-6	2014	In addition, we identify cysteine as a novel amino-acid target for ADP-ribosylation on PARPs.	Cysteine	25-33	poly(ADP-ribose) polymerase 1	Homo sapiens	87-92	
31152818-6	2019	We identified peroxynitrite was responsible for S-nitrosation on cysteine residues resulting in PARP-1 zinc finger conformational changes.	Cysteine	65-73	poly(ADP-ribose) polymerase 1	Homo sapiens	96-102	
27741521-3	2016	AsIII-induced ROS lead to oxidation of cysteine residues within the PARP-1 zinc finger DNA binding domain.	Cysteine	39-47	poly(ADP-ribose) polymerase 1	Homo sapiens	68-74	
27741521-5	2016	In this work, we demonstrate that AsIII treatment of normal human keratinocyte (HEKn) cells induced S-nitrosation on cysteine residues of PARP-1 protein, in a similar manner to a nitric oxide donor.	Cysteine	117-125	poly(ADP-ribose) polymerase 1	Homo sapiens	138-144	
24778456-3	2014	Here, we show that H2S attenuates DNA damage in human endothelial cells and fibroblasts by S-sulfhydrating MEK1 at cysteine 341, which leads to PARP-1 activation.	Cysteine	115-123	poly(ADP-ribose) polymerase 1	Homo sapiens	144-150	
24778456-5	2014	Mutation of MEK1 cysteine 341 inhibits ERK phosphorylation and PARP-1 activation.	Cysteine	17-25	poly(ADP-ribose) polymerase 1	Homo sapiens	63-69	
21518760-5	2011	Mutation of the cysteines in the zinc finger domain of KLF8 abolished PARP-1 interaction.	Cysteine	16-25	poly(ADP-ribose) polymerase 1	Homo sapiens	70-76	
21550982-5	2011	MALDI-TOF-MS analysis of peptides harboring site-directed substitutions of cysteine with histidine residues within the PARP-1 zinc finger revealed that arsenite bound to peptides containing three or four cysteine residues, but not to peptides with two cysteines, demonstrating arsenite binding selectivity.	Cysteine	75-83	poly(ADP-ribose) polymerase 1	Homo sapiens	119-125	
21550982-5	2011	MALDI-TOF-MS analysis of peptides harboring site-directed substitutions of cysteine with histidine residues within the PARP-1 zinc finger revealed that arsenite bound to peptides containing three or four cysteine residues, but not to peptides with two cysteines, demonstrating arsenite binding selectivity.	Cysteine	204-212	poly(ADP-ribose) polymerase 1	Homo sapiens	119-125	
21550982-10	2011	These findings demonstrate that PARP-1 is a direct molecular target of arsenite and that arsenite interacts selectively with zinc finger motifs containing three or more cysteine residues.	Cysteine	169-177	poly(ADP-ribose) polymerase 1	Homo sapiens	32-38