PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
29555700-6	2018	Increased expression of crp and pla correlated with a reduction in lung glucose levels.	Glucose	72-79	plasminogen activator protease precursor	Yersinia pestis	32-35
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	catabolite	607-617	plasminogen activator protease precursor	Yersinia pestis	204-207
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	Glucose	16-23	plasminogen activator protease precursor	Yersinia pestis	170-173
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	Glucose	16-23	plasminogen activator protease precursor	Yersinia pestis	204-207
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	Glucose	93-100	plasminogen activator protease precursor	Yersinia pestis	204-207
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	Cyclic AMP	284-288	plasminogen activator protease precursor	Yersinia pestis	204-207
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	Glucose	93-100	plasminogen activator protease precursor	Yersinia pestis	204-207
29555700-7	2018	Deletion of the glucose-specific phosphotransferase system EIIBC (PtsG) of Y. pestis rescued glucose levels in the lungs, resulting in reduced expression of both crp and pla We propose that activation of pla expression during pneumonic plague is driven by an increase of both Crp and cAMP levels following consumption of available glucose in the lungs by Y. pestis Thus, Crp operates as a sensor linking the nutritional environment of the host to regulation of virulence gene expression.IMPORTANCE Using Yersinia pestis as a model for pneumonia, we discovered that glucose is rapidly consumed, leading to a catabolite-repressive environment in the lungs.	Glucose	93-100	plasminogen activator protease precursor	Yersinia pestis	204-207
20637417-0	2010	An active site water network in the plasminogen activator pla from Yersinia pestis.	Water	15-20	plasminogen activator protease precursor	Yersinia pestis	36-39
21604388-5	2011	RESULTS: Sialic acids were found in LPS, Pla-protease, allergen pestin PP, and all cholera O-AG; their absence was demonstrated in MSA and F1.	Sialic Acids	9-21	plasminogen activator protease precursor	Yersinia pestis	41-44
20368351-6	2010	Reactivation of His(6)-Pla was higher with Y. pestis LPSs isolated from bacteria grown at 37 degrees C than with LPSs from cells grown at 25 degrees C. Lack of O antigens and the presence of the outer core region as well as a lowered level of acylation in LPS were found to enhance the Pla-LPS interaction.	lpss	53-57	plasminogen activator protease precursor	Yersinia pestis	23-26
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Arginine	24-32	plasminogen activator protease precursor	Yersinia pestis	172-175
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Arginine	24-32	plasminogen activator protease precursor	Yersinia pestis	194-197
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Arginine	24-32	plasminogen activator protease precursor	Yersinia pestis	194-197
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Lipid A	104-111	plasminogen activator protease precursor	Yersinia pestis	172-175
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Phosphates	112-122	plasminogen activator protease precursor	Yersinia pestis	172-175
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Phosphates	112-122	plasminogen activator protease precursor	Yersinia pestis	194-197
20368351-7	2010	Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction.	Phosphates	112-122	plasminogen activator protease precursor	Yersinia pestis	194-197
15194160-5	2004	Pre-treatment with staurosporin, a potent inhibitor of protein kinases (PKs) and with genistein, a specific tyrosine kinase inhibitor decreased the number of internalised bacteria about seven-fold and two-fold, respectively, indicating the involvement of PKs including tyrosine kinases in Pla-mediated internalisation.	Staurosporine	19-31	plasminogen activator protease precursor	Yersinia pestis	289-292
19465664-9	2009	The substitution (259)IIDKT/TIDKN in PgtE, constructed to mimic the L5 region in Pla, altered proteolysis in favor of plasmin formation, whereas the reverse substitution (259)TIDKN/IIDKT in Pla altered proteolysis in favor of alpha(2)-antiplasmin inactivation.	pgte	37-41	plasminogen activator protease precursor	Yersinia pestis	81-84
17966423-10	2007	The sequence of Pla contains a three-dimensional motif for protein binding to lipid A of the lipopolysaccharide.	Lipid A	78-85	plasminogen activator protease precursor	Yersinia pestis	16-19
15969469-2	2005	In this study we characterised the laminin-binding site(s) of Pla via phage display and alanine-scanning mutagenesis.	Alanine	88-95	plasminogen activator protease precursor	Yersinia pestis	62-65
15194160-5	2004	Pre-treatment with staurosporin, a potent inhibitor of protein kinases (PKs) and with genistein, a specific tyrosine kinase inhibitor decreased the number of internalised bacteria about seven-fold and two-fold, respectively, indicating the involvement of PKs including tyrosine kinases in Pla-mediated internalisation.	Genistein	86-95	plasminogen activator protease precursor	Yersinia pestis	289-292
9826351-6	1998	The Pla-expressing strains showed a low-affinity adherence to another basement membrane component, heparan sulfate proteoglycan, but not to chondroitin sulfate proteoglycan.	Heparitin Sulfate	99-114	plasminogen activator protease precursor	Yersinia pestis	4-7