PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
1400336-5	1992	Covalent reaction of the active site Glu165 with the substrate analogue 3-chloroacetol phosphate (CAP) results in dimers with increased susceptibility to unfolding and inactivation by denaturants (i.e. the rates of inactivation and unfolding are (TPICAP)2 greater than (TPI-TPICAP) greater than (TPI)2).	3-chloroacetol phosphate	72-96	triosephosphate isomerase 1	Homo sapiens	247-250
1400336-5	1992	Covalent reaction of the active site Glu165 with the substrate analogue 3-chloroacetol phosphate (CAP) results in dimers with increased susceptibility to unfolding and inactivation by denaturants (i.e. the rates of inactivation and unfolding are (TPICAP)2 greater than (TPI-TPICAP) greater than (TPI)2).	3-chloroacetol phosphate	72-96	triosephosphate isomerase 1	Homo sapiens	270-273
1521533-6	1992	The rate of TPI reactivation also increased with increasing protein concentration in the system with denatured TPI covalently derivatized at the catalytic site with the substrate analogue 3-chloroacetol phosphate.	3-chloroacetol phosphate	188-212	triosephosphate isomerase 1	Homo sapiens	12-15
1521533-6	1992	The rate of TPI reactivation also increased with increasing protein concentration in the system with denatured TPI covalently derivatized at the catalytic site with the substrate analogue 3-chloroacetol phosphate.	3-chloroacetol phosphate	188-212	triosephosphate isomerase 1	Homo sapiens	111-114
1586170-5	1992	Covalent reaction of the active site Glu 165 with the substrate analogue 3-chloroacetol phosphate results in a conformational change (decrease in beta-sheet) which is similar in TPI from all three species.	3-chloroacetol phosphate	73-97	triosephosphate isomerase 1	Homo sapiens	178-181
1536574-1	1992	Covalent modification of the active site Glu165 of triosephosphate isomerase (TPI) (EC 5.3.1.1) with the substrate analogue 3-chloroacetol phosphate (CAP) induces conformational changes similar to those observed during catalysis.	3-chloroacetol phosphate	124-148	triosephosphate isomerase	Oryctolagus cuniculus	51-76
1536574-1	1992	Covalent modification of the active site Glu165 of triosephosphate isomerase (TPI) (EC 5.3.1.1) with the substrate analogue 3-chloroacetol phosphate (CAP) induces conformational changes similar to those observed during catalysis.	3-chloroacetol phosphate	124-148	triosephosphate isomerase	Oryctolagus cuniculus	78-81