PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28978675-4	2017	Rer2-Nus1 and Srt1-Nus1 can both generate dolichol in vegetative cells, but srt1  cells grow normally while rer2  grows very slowly, indicating that Rer2-Nus1 is the primary enzyme used in mitotically dividing cells.	Dolichols	42-50	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	0-4	
31336877-6	2019	The finding of suppressors Rer2 and Srt1, which participate in the dolichol biosynthesis pathway revealed that the hog1Delta strain has a defective polyprenol metabolism.	Dolichols	67-75	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	27-31	
23134568-7	2013	Although no in vitro activity was demonstrated for SlCPT3, its expression in the Saccharomyces cerevisiae dolichol biosynthesis mutant (rer2) complemented the temperature-sensitive growth defect.	Dolichols	106-114	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	136-140	
16527501-0	2006	Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation.	Dolichols	87-95	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	47-51	
11442630-3	2001	We have identified a key enzyme of the dolichol synthesis, cis-prenyltransferase, as Rer2p from Saccharomyces cerevisiae.	Dolichols	39-47	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	85-90	
10217761-0	1999	The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis.	Dolichols	62-70	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	40-44	
10217761-10	1999	Our work on the yeast rer2 mutants shows that they are defective in the activity of cis-prenyltransferase, namely, dehydrodolichyl diphosphate synthase, a key enzyme of dolichol synthesis.	Dolichols	169-177	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	22-26	
10217761-11	1999	Taking these data together, we conclude that the RER2 gene family encodes cis-prenyltransferase, which plays an essential role in cell wall biosynthesis in bacteria and in dolichol synthesis in eukaryotic cells and has been well conserved during evolution.	Dolichols	172-180	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	49-53	
9858571-0	1999	The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis.	Dolichols	136-144	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	10-14	
9858571-10	1999	Taking a hint from the phenotype of newly established mutants of the Rer2p homologue of Escherichia coli, we discovered that the rer2 mutant is deficient in the activity of cis-prenyltransferase, a key enzyme of dolichol synthesis.	Dolichols	212-220	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	129-133	
9858571-12	1999	The difference in phenotypes between the rer2 mutant and previously obtained glycosylation mutants suggests a novel, as-yet-unknown role of dolichol.	Dolichols	140-148	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	41-45	
20602334-5	2010	The sensitivity of both mutants could be brought back to the wild-type level by a multicopy suppressor of the thermosensitive phenotype, the RER2 gene, encoding cis-prenyltransferase involved in dolichol biosynthesis.	Dolichols	195-203	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	141-145	
16213651-2	2006	Our results suggest that the activities of two yeast cis-prenyltransferases Rer2p and Srt1p and polyprenol reductase are not co-regulated and that reductase may be the rate-limiting enzyme in dolichol synthesis if the amount of polyisoprenoids synthesized exceeds a certain level.	Dolichols	192-200	ditrans,polycis-polyprenyl diphosphate synthase	Saccharomyces cerevisiae S288C	76-81