PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15707964-2	2005	In baker"s yeast external high osmolarity activates high osmolarity glycerol (HOG) MAPK pathway which consists of two upstream branches (SHO1 and SLN1) and common downstream elements Pbs2p MAPKK and Hog1p MAPK.	Glycerol	68-76	osmosensor SHO1	Saccharomyces cerevisiae S288C	137-141	
16778768-1	2006	The yeast high osmolarity glycerol (HOG) signaling pathway can be activated by either of the two upstream pathways, termed the SHO1 and SLN1 branches.	Glycerol	26-34	osmosensor SHO1	Saccharomyces cerevisiae S288C	127-131	
21483474-2	2011	Here, the goal is to generate, fit and discriminate several candidate models that represent different hypotheses for feedback mechanisms responsible for downregulating the response of the Sho1 branch of the yeast high osmolarity glycerol (HOG) signaling pathway after initial stimulation.	Glycerol	229-237	osmosensor SHO1	Saccharomyces cerevisiae S288C	188-192	
20958245-6	2010	For stress caused by the degradation of cell wall glucans by Zymolyase, mid2Delta and wsc1Delta deletions show little effect, but the transcriptional response rather depends on the transmembrane protein Sho1, a component of the high-osmolarity glycerol (HOG) pathway.	Glycerol	244-252	osmosensor SHO1	Saccharomyces cerevisiae S288C	203-207	
19657148-1	2009	Adaptation to osmotic shock in Saccharomyces cerevisiae is brought about by the activation of two independent signaling pathways, Sho1 and Sln1, which in turn trigger the high osmolarity glycerol (HOG) pathway.	Glycerol	187-195	osmosensor SHO1	Saccharomyces cerevisiae S288C	130-134	
19061190-1	2008	In yeast, external signals such as high osmolarity or oxidant conditions activate the high osmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) cascade pathway, which consists of two upstream branches, i.e. Sho1p and Sln1p and common downstream elements, including the Pbs2p MAPK kinase and the Hog1p MAPK.	Glycerol	102-110	osmosensor SHO1	Saccharomyces cerevisiae S288C	220-225	
16543225-5	2006	We have identified Opy2p, an integral membrane protein that can interact with Ste50p, as a new component in the Sho1p-Ste11p/Ste50p signaling branch of the high-osmolarity glycerol (HOG) pathway.	Glycerol	172-180	osmosensor SHO1	Saccharomyces cerevisiae S288C	112-117	
15256499-5	2004	Msb2 is localized to polarized sites on the cell surface and interacts with Cdc42 and with the osmosensor for the high osmolarity glycerol response (HOG) pathway, Sho1.	Glycerol	130-138	osmosensor SHO1	Saccharomyces cerevisiae S288C	163-167	
22586268-1	2012	The yeast high-osmolarity glycerol response (HOG) mitogen-activated protein (MAP) kinase pathway is activated in response to hyperosmotic stress via two independent osmosensing branches, the Sln1 branch and the Sho1 branch.	Glycerol	26-34	osmosensor SHO1	Saccharomyces cerevisiae S288C	211-215	
30682143-2	2019	Hog1 is activated through the high-osmolarity glycerol (HOG) pathway, which consists of a core MAPK cascade and two independent upstream branches (SHO1 and SLN1 branches) containing distinct osmosensing machineries.	Glycerol	46-54	osmosensor SHO1	Saccharomyces cerevisiae S288C	147-151	
26598606-2	2016	Hog1 is activated through the high-osmolarity glycerol (HOG) pathway, which consists of independent upstream signaling routes termed the SLN1 branch and the SHO1 branch.	Glycerol	46-54	osmosensor SHO1	Saccharomyces cerevisiae S288C	157-161	
25213170-4	2014	By examining the genetic interactions of known spindle disassembly genes, we identified three genes in the environmental stress-sensing HOG (high-osmolarity glycerol response) pathway, SHO1, PBS2, and HOG1, and found they are necessary for proper localization of She1 to the anaphase spindle and for proper spindle disassembly.	Glycerol	157-165	osmosensor SHO1	Saccharomyces cerevisiae S288C	185-189	
12853477-3	2003	In yeast, external high osmolarity activates the HOG (high osmolarity glycerol) MAPK pathway, which consists of two upstream branches (SHO1 and SLN1) and common downstream elements including the Pbs2 MAPKK and the Hog1 MAPK.	Glycerol	70-78	osmosensor SHO1	Saccharomyces cerevisiae S288C	135-139	
29341399-1	2018	Yeast cells respond to hyperosmotic stress by activating the high-osmolarity glycerol (HOG) pathway, which consists of two branches, Hkr1/Msb2-Sho1 and Sln1, which trigger phosphorylation and nuclear internalization of the Hog1 mitogen-activated protein kinase.	Glycerol	77-85	osmosensor SHO1	Saccharomyces cerevisiae S288C	143-147	
25644660-1	2015	Sho1p, an integral membrane protein, plays a vital role in the high-osmolarity glycerol (HOG) mitogen-activated protein kinase pathway in the yeast Saccharomyces cerevisiae.	Glycerol	79-87	osmosensor SHO1	Saccharomyces cerevisiae S288C	0-5	
25331360-4	2014	Both Sln1 and Sho1 upstream branches are involved in the cadmium-induced activation of high osmolarity glycerol (HOG) pathway.	Glycerol	103-111	osmosensor SHO1	Saccharomyces cerevisiae S288C	14-18