PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
17132105-6	2006	Functional analysis showed that Fes1p accelerates the release of the nucleotide analog MABA-ADP from Ssb1p by a factor of 35.	N(8)-(4-((N'-methylanthraniloyl)amino)butyl)-8-aminoadenosine 5'-diphosphate	87-95	Fes1p	Saccharomyces cerevisiae S288C	32-37
16374585-3	2005	Here we report the identification and characterization of additional genes involved in regulating polyamine tolerance: YGL007W, FES1 and AGP2.	Polyamines	98-107	Fes1p	Saccharomyces cerevisiae S288C	128-132
16374585-5	2005	Deletion of FES1 or AGP2 resulted in reduced polyamine uptake.	Polyamines	45-54	Fes1p	Saccharomyces cerevisiae S288C	12-16
33361368-4	2021	The induction of this stress resistance required the new synthesis of proteins; the expression of proteins comprising the bi-chaperone system (Hsp104, Ssa3, and Fes1), Sis1, and Hsp42 was up-regulated during the pretreatment and maintained under subsequent severe ethanol stress.	Ethanol	264-271	Fes1p	Saccharomyces cerevisiae S288C	161-165
12052876-5	2002	We found that Fes1p associates preferentially to the ADP-bound form of the cytosolic Hsp70 molecular chaperone Ssa1p and promotes nucleotide release.	Adenosine Diphosphate	53-56	Fes1p	Saccharomyces cerevisiae S288C	14-19
12052876-10	2002	However, the Delta fes1 mutant showed increased cycloheximide sensitivity and a general translational defect, suggesting that Fes1p acts during protein translation, a process in which Ssa1p and Ydj1p are known to be involved.	Cycloheximide	48-61	Fes1p	Saccharomyces cerevisiae S288C	19-23
12052876-10	2002	However, the Delta fes1 mutant showed increased cycloheximide sensitivity and a general translational defect, suggesting that Fes1p acts during protein translation, a process in which Ssa1p and Ydj1p are known to be involved.	Cycloheximide	48-61	Fes1p	Saccharomyces cerevisiae S288C	126-131
31806703-0	2020	Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.	Methionine	99-109	Fes1p	Saccharomyces cerevisiae S288C	67-71
31806703-3	2020	Here, we describe a methionine-based oxidation event involving the yeast cytoplasmic Hsp70 co-chaperone Fes1.	Methionine	20-30	Fes1p	Saccharomyces cerevisiae S288C	104-108
31806703-4	2020	We show that Fes1 undergoes reversible methionine oxidation during excessively-oxidizing cellular conditions, and we map the site of this oxidation to a cluster of three methionine residues in the Fes1 core domain.	Methionine	39-49	Fes1p	Saccharomyces cerevisiae S288C	13-17
31806703-4	2020	We show that Fes1 undergoes reversible methionine oxidation during excessively-oxidizing cellular conditions, and we map the site of this oxidation to a cluster of three methionine residues in the Fes1 core domain.	Methionine	170-180	Fes1p	Saccharomyces cerevisiae S288C	13-17
31806703-4	2020	We show that Fes1 undergoes reversible methionine oxidation during excessively-oxidizing cellular conditions, and we map the site of this oxidation to a cluster of three methionine residues in the Fes1 core domain.	Methionine	170-180	Fes1p	Saccharomyces cerevisiae S288C	197-201
31806703-8	2020	The characterization of Fes1 oxidation during cellular stress provides a new perspective as to how the activities of the cytoplasmic Hsp70 chaperones may be attuned by fluctuations in cellular ROS levels and provides further insight into how cells use methionine-based redox switches to sense and respond to oxidative stress.	Reactive Oxygen Species	193-196	Fes1p	Saccharomyces cerevisiae S288C	24-28
31806703-8	2020	The characterization of Fes1 oxidation during cellular stress provides a new perspective as to how the activities of the cytoplasmic Hsp70 chaperones may be attuned by fluctuations in cellular ROS levels and provides further insight into how cells use methionine-based redox switches to sense and respond to oxidative stress.	Methionine	252-262	Fes1p	Saccharomyces cerevisiae S288C	24-28