PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8881287-4	1996	Use of deletion mutants showed that both activation functions (AF1 and AF2) of PR as well as the coiled coil and His-Cys rich domains of PML were required for transcriptional enhancement.	Cysteine	117-120	PML nuclear body scaffold	Homo sapiens	137-140	
9671411-6	1998	The PML aminoterminal portion retained within the PML/RARalpha protein contains the RING finger, two newly defined cystein/histidine-rich motifs called B-boxes (B1 and B2) and a coiled-coil region.	Cysteine	115-122	PML nuclear body scaffold	Homo sapiens	4-7	
9671498-6	1998	Mutant PML proteins containing either a Cys point mutation within the N-terminal RING finger domain or a small deletion (of positions 281 to 304) within the coiled-coil region did not localize to the PODs but instead gave a nuclear diffuse distribution, similar to that produced by intact PML in the presence of IE1.	Cysteine	40-43	PML nuclear body scaffold	Homo sapiens	7-10	
9016654-3	1996	TIF1 beta, TIF1 alpha, PML and efp belong to a characteristic subgroup of RING finger proteins that contain one or two other Cys/His-rich clusters (B boxes) and a putative coiled-coil in addition to the classical C3HC4 RING finger motif (RBCC configuration).	Cysteine	125-128	PML nuclear body scaffold	Homo sapiens	23-26	
7675545-7	1995	PML, whose function is unknown, belongs to a novel family of nuclear proteins characterized by the presence of a Cys/His-rich motif, named a RING finger, that include RNA-binding proteins, transcription factors and oncoproteins.	Cysteine	113-116	PML nuclear body scaffold	Homo sapiens	0-3	
8614415-4	1995	The use of deletion mutants showed that both activation functions (AF1 and AF2) of PR as well as the coiled coil and His-Cys-rich domains of PML were required for transcriptional enhancement.	Cysteine	121-124	PML nuclear body scaffold	Homo sapiens	141-144	
32243901-6	2020	Mechanistically, SFN modifies several cysteine residues, including C204, located in the RBCC domain of PML.	Cysteine	38-46	PML nuclear body scaffold	Homo sapiens	103-106	
35594310-2	2022	Trivalent arsenic (As3+) is known to cure APL by binding to cysteine residues of PML and enhance the degradation of PML-retinoic acid receptor alpha (RARalpha), a t(15;17) gene translocation product in APL cells, and restore PML-nuclear bodies (NBs).	Cysteine	60-68	PML nuclear body scaffold	Homo sapiens	81-84	
1652368-2	1991	PML contains a cysteine-rich region present in a new family of apparent DNA-binding proteins that includes a regulator of the interleukin-2 receptor gene (Rpt-1) and the recombination-activating gene product (RAG-1).	Cysteine	15-23	PML nuclear body scaffold	Homo sapiens	0-3	
30021158-5	2018	Importantly, mutation of the putative catalytic cysteine is sufficient to reverse LUNA-mediated PML dispersal and markedly reduces the efficiency of viral reactivation.	Cysteine	48-56	PML nuclear body scaffold	Homo sapiens	96-99	
30763586-4	2019	ATO acts through a direct arsenic binding to cysteine residues in zinc fingers located in promyelocytic leukemia protein (PML), thus killing the leukemia stem cells (LSCs).	Cysteine	45-53	PML nuclear body scaffold	Homo sapiens	90-120	
30763586-4	2019	ATO acts through a direct arsenic binding to cysteine residues in zinc fingers located in promyelocytic leukemia protein (PML), thus killing the leukemia stem cells (LSCs).	Cysteine	45-53	PML nuclear body scaffold	Homo sapiens	122-125	
21454520-3	2011	Arsenic trioxide, a drug for patients with acute promyelocytic leukemia, is found to target and degrade a class of proteins with high levels of cysteine residues and vicinal thiol groups, such as promyelocytic leukemia protein (PML) and PML-retinoic acid receptor alpha fusion protein.	Cysteine	144-152	PML nuclear body scaffold	Homo sapiens	196-226	
24135626-3	2013	PML, a nuclear transcription factor, has a RING finger domain with densely positioned cysteine residues.	Cysteine	86-94	PML nuclear body scaffold	Homo sapiens	0-3	
21148299-7	2011	Mutation of the catalytic cysteine of SENP6 results in its accumulation in PML NBs, and biochemical analysis indicates that SUMO-modified PML is a substrate of SENP6.	Cysteine	26-34	PML nuclear body scaffold	Homo sapiens	75-78	
21148299-7	2011	Mutation of the catalytic cysteine of SENP6 results in its accumulation in PML NBs, and biochemical analysis indicates that SUMO-modified PML is a substrate of SENP6.	Cysteine	26-34	PML nuclear body scaffold	Homo sapiens	138-141	
20378816-4	2010	Here we show that arsenic binds directly to cysteine residues in zinc fingers located within the RBCC domain of PML-RARalpha and PML.	Cysteine	44-52	PML nuclear body scaffold	Homo sapiens	112-115	
20378816-4	2010	Here we show that arsenic binds directly to cysteine residues in zinc fingers located within the RBCC domain of PML-RARalpha and PML.	Cysteine	44-52	PML nuclear body scaffold	Homo sapiens	129-132