PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16962064-0	2006	Ysp2 mediates death of yeast induced by amiodarone or intracellular acidification.	Amiodarone	40-50	Ysp2p	Saccharomyces cerevisiae S288C	0-4
16962064-3	2006	We have described a novel mitochondrial protein, Ysp2, acting in the amiodarone-induced death cascade.	Amiodarone	69-79	Ysp2p	Saccharomyces cerevisiae S288C	49-53
16962064-4	2006	After amiodarone addition both the control and amiodarone-resistant ysp2-deleted cells formed ROS, but the mutant (unlike the control) did not undergo the mitochondrial thread-to-grain transition.	Amiodarone	6-16	Ysp2p	Saccharomyces cerevisiae S288C	68-72
16962064-4	2006	After amiodarone addition both the control and amiodarone-resistant ysp2-deleted cells formed ROS, but the mutant (unlike the control) did not undergo the mitochondrial thread-to-grain transition.	Amiodarone	47-57	Ysp2p	Saccharomyces cerevisiae S288C	68-72
16962064-4	2006	After amiodarone addition both the control and amiodarone-resistant ysp2-deleted cells formed ROS, but the mutant (unlike the control) did not undergo the mitochondrial thread-to-grain transition.	Reactive Oxygen Species	94-97	Ysp2p	Saccharomyces cerevisiae S288C	68-72
16962064-5	2006	To test whether the action of Ysp2 is amiodarone-specific we tried to induce PCD by other agents.	Amiodarone	38-48	Ysp2p	Saccharomyces cerevisiae S288C	30-34
16962064-6	2006	We have found that acetic acid-induced PCD also depends on Ysp2.	Acetic Acid	19-30	Ysp2p	Saccharomyces cerevisiae S288C	59-63
16962064-8	2006	We suggest that intracellular acidification results in the protonation of superoxide anion (O2-*) to form HO2, one of the most aggressive ROS, which in turn induces Ysp2-mediated PCD.	Superoxides	74-90	Ysp2p	Saccharomyces cerevisiae S288C	165-169
16962064-8	2006	We suggest that intracellular acidification results in the protonation of superoxide anion (O2-*) to form HO2, one of the most aggressive ROS, which in turn induces Ysp2-mediated PCD.	Superoxides	92-94	Ysp2p	Saccharomyces cerevisiae S288C	165-169
16962064-8	2006	We suggest that intracellular acidification results in the protonation of superoxide anion (O2-*) to form HO2, one of the most aggressive ROS, which in turn induces Ysp2-mediated PCD.	perhydroxyl radical	106-109	Ysp2p	Saccharomyces cerevisiae S288C	165-169
16962064-8	2006	We suggest that intracellular acidification results in the protonation of superoxide anion (O2-*) to form HO2, one of the most aggressive ROS, which in turn induces Ysp2-mediated PCD.	Reactive Oxygen Species	138-141	Ysp2p	Saccharomyces cerevisiae S288C	165-169
33255682-4	2020	At ER-PM CSs, Lam2 and Lam4 associate with Laf1/Ymr102c and Dgr2/Ykl121w (paralogous WD40 repeat-containing proteins) that reportedly bind sterol.	Sterols	139-145	Ysp2p	Saccharomyces cerevisiae S288C	14-18
33255682-2	2020	Two of the six family members-Lam2/Ltc4 (initially Ysp2) and paralog Lam4/Ltc3-localize to ER-plasma membrane (PM) contact sites (CSs) and mediate retrograde ergosterol transport from the PM to the ER.	Ergosterol	158-168	Ysp2p	Saccharomyces cerevisiae S288C	30-34
33255682-2	2020	Two of the six family members-Lam2/Ltc4 (initially Ysp2) and paralog Lam4/Ltc3-localize to ER-plasma membrane (PM) contact sites (CSs) and mediate retrograde ergosterol transport from the PM to the ER.	Ergosterol	158-168	Ysp2p	Saccharomyces cerevisiae S288C	35-39
33255682-2	2020	Two of the six family members-Lam2/Ltc4 (initially Ysp2) and paralog Lam4/Ltc3-localize to ER-plasma membrane (PM) contact sites (CSs) and mediate retrograde ergosterol transport from the PM to the ER.	Ergosterol	158-168	Ysp2p	Saccharomyces cerevisiae S288C	51-55
33255682-3	2020	Our prior work demonstrated that Lam2 and Lam4 are substrates of TORC2-regulated protein kinase Ypk1, that Ypk1-mediated phosphorylation inhibits their function in retrograde sterol transport, and that PM sterol retention bolsters cell survival under stressful conditions.	Sterols	175-181	Ysp2p	Saccharomyces cerevisiae S288C	33-37
33255682-8	2020	Lam2 phosphorylated by Ypk1, and Lam2 with phosphomimetic (Glu) replacements at its Ypk1 sites, exhibited a marked reduction in Laf1 binding.	Glutamic Acid	59-62	Ysp2p	Saccharomyces cerevisiae S288C	33-37
33255682-9	2020	Thus, phosphorylation prevents Lam2 interaction with Laf1 at ER-PM CSs, providing a mechanism by which Ypk1 action inhibits retrograde sterol transport.	Sterols	135-141	Ysp2p	Saccharomyces cerevisiae S288C	31-35
32047490-6	2020	Surprisingly, the quadruple deletant and LAM2/LAM4 double deletion strain showed increased tolerance to the azole antifungals clotrimazole and miconazole.	Azoles	108-113	Ysp2p	Saccharomyces cerevisiae S288C	41-45
32047490-6	2020	Surprisingly, the quadruple deletant and LAM2/LAM4 double deletion strain showed increased tolerance to the azole antifungals clotrimazole and miconazole.	Clotrimazole	126-138	Ysp2p	Saccharomyces cerevisiae S288C	41-45
32047490-6	2020	Surprisingly, the quadruple deletant and LAM2/LAM4 double deletion strain showed increased tolerance to the azole antifungals clotrimazole and miconazole.	Miconazole	143-153	Ysp2p	Saccharomyces cerevisiae S288C	41-45
26001273-3	2015	StART-like domains from Ysp2p and its paralog Lam4p specifically bind sterols, and Ysp2p, Lam4p and their homologs Ysp1p and Sip3p target punctate ER-PM contact sites distinct from those occupied by known ER-PM tethers.	Sterols	70-77	Ysp2p	Saccharomyces cerevisiae S288C	24-29
26001273-4	2015	The activity of Ysp2p, reflected in amphotericin-sensitivity assays, requires its second StART-like domain to be positioned so that it can reach across ER-PM contacts.	Amphotericin B	36-48	Ysp2p	Saccharomyces cerevisiae S288C	16-21
26001273-5	2015	Absence of Ysp2p, Ysp1p or Sip3p reduces the rate at which exogenously supplied sterols traffic from the PM to the ER.	Sterols	80-87	Ysp2p	Saccharomyces cerevisiae S288C	11-16
32564734-8	2020	The UPC2-1 mutation in the transcription factor UPC2 gene, which leads to the excessive accumulation of sterols in the cell, promotes cell survival in the presence of the pheromone and shows additivity with the LAM2 deletion.	Sterols	104-111	Ysp2p	Saccharomyces cerevisiae S288C	211-215
32564734-10	2020	We have found that the deletion of ergosterol biosynthesis genes ERG2 and ERG6 reduces the effect of LAM2 deletion.	Ergosterol	35-45	Ysp2p	Saccharomyces cerevisiae S288C	101-105
32564734-11	2020	Deletion of LAM2 in the Deltaerg4 strain lacking the gene of the last step of ergosterol biosynthesis, significantly increased the proportion of dead cells and decreased the growth rate of the yeast suspension culture even in the absence of the pheromone.	Ergosterol	78-88	Ysp2p	Saccharomyces cerevisiae S288C	12-16
32564734-12	2020	We suggest that the absence of the effect of LAM2 deletion in the Deltaerg6 and Deltaerg2 strains indicates the inability of Lam2p to transport some ergosterol biosynthesis intermediates, such as lanosterol.	Ergosterol	149-159	Ysp2p	Saccharomyces cerevisiae S288C	125-130
29927351-3	2018	Here we document that Ysp2 and its paralogue Lam4/Ltc3 are authentic Ypk1 substrates in vivo and show using genetic and biochemical criteria that Ypk1-mediated phosphorylation inhibits the ability of these proteins to promote retrograde transport of sterols from the PM to the ER.	Sterols	250-257	Ysp2p	Saccharomyces cerevisiae S288C	22-26
29339490-4	2018	Here, we determined the crystal structures of the yeast Lam6 pleckstrin homology (PH)-like domain and the SDs of Lam2 and Lam4 in the apo form and in complex with ergosterol.	Sodium Dodecyl Sulfate	106-109	Ysp2p	Saccharomyces cerevisiae S288C	113-117
29339490-4	2018	Here, we determined the crystal structures of the yeast Lam6 pleckstrin homology (PH)-like domain and the SDs of Lam2 and Lam4 in the apo form and in complex with ergosterol.	Ergosterol	163-173	Ysp2p	Saccharomyces cerevisiae S288C	113-117
27227887-5	2016	These phenotypes were rescued by TORC1 inhibition using pharmacological or genetic means, and the loss of Lam2, Gtr1, Gtr2, Npr2 or Npr3 disinhibited TORC1 activity under nitrogen depletion, as measured by Rps6 phosphorylation.	Nitrogen	171-179	Ysp2p	Saccharomyces cerevisiae S288C	106-110
27227887-6	2016	Consistently, overexpression of GDP-locked Gtr1S20L or GTP-locked Gtr2Q60L, which suppress TORC1 activity in budding yeast, rescued the growth defect of Deltagtr1 cells or Deltagtr2 cells, respectively, and the loss of Lam2, Npr2 or Npr3 similarly diminished the vacuolar localization and the protein levels of Gtr1 and Gtr2.	Guanosine Diphosphate	32-35	Ysp2p	Saccharomyces cerevisiae S288C	219-223
27227887-8	2016	These findings suggest that Lam2 and Npr2-Npr3 function together as a tether for GDP-bound Gtr1 to the vacuolar membrane, thereby suppressing TORC1 activity for multiple cellular functions.	Guanosine Diphosphate	81-84	Ysp2p	Saccharomyces cerevisiae S288C	28-32