PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18822298-1	2008	TEM-1 beta-lactamase confers bacterial resistance to penicillin antibiotics and has acquired mutations that permit the enzyme to hydrolyze extended-spectrum cephalosporins or to avoid inactivation by beta-lactamase inhibitors.	Cephalosporins	157-171	CD248 molecule	Homo sapiens	0-5	
27267601-16	2016	Among 12 cephalosporin-resistant Salmonella isolates, TEM-1 and CTX-M-14 determinants were present in two (16.7 %) isolates.	Cephalosporins	9-22	CD248 molecule	Homo sapiens	54-59	
27267601-23	2016	TEM-1 and CTX-M-14 genetic determinants, and gyrA mutations, were the major mechanisms associated with high levels of cephalosporin and quinolone resistance, respectively, in Salmonella isolates.	Cephalosporins	118-131	CD248 molecule	Homo sapiens	0-5	
25713062-2	2015	TEM-1 is a prevalent plasmid-encoded beta-lactamase in Gram-negative bacteria that efficiently catalyzes the hydrolysis of penicillins and early cephalosporins but not oxyimino-cephalosporins.	Cephalosporins	145-159	CD248 molecule	Homo sapiens	0-5	
21867672-0	2011	Fluorogenic cephalosporin substrates for beta-lactamase TEM-1.	Cephalosporins	12-25	CD248 molecule	Homo sapiens	56-61	
21867672-1	2011	Cephalosporin was used to synthesize soluble and precipitating fluorogenic beta-lactam substrates that demonstrated differential catalytic hydrolysis by three different subtypes of beta-lactamase: TEM-1 (class A), p99 (class C), and a Bacillus cereus enzyme sold by Genzyme (class B).	Cephalosporins	0-13	CD248 molecule	Homo sapiens	197-202	
26055690-7	2017	Among 44 cephalosporin-resistant isolates, TEM-1, CMY-2, CMY-14, CTX-M-3-like and CTX-M-15-like determinants were present in 31 (70.5%), 32 (72.7%), 1 (2.3%), 1 (2.3%), and 1 (2.3%) of isolates, respectively.	Cephalosporins	9-22	CD248 molecule	Homo sapiens	43-48	
18687656-4	2008	The frequency of genes conferring a new function (degradation of a cephalosporin antibiotic) was measured at various stages of the drift, and a model that accounts for the differences in the observed adaptation dynamics of the drifting TEM-1 populations was derived.	Cephalosporins	67-80	CD248 molecule	Homo sapiens	236-241	
1644749-3	1992	To identify other amino acid substitutions that alter the activity of TEM-1 towards extended-spectrum cephalosporins, we probed regions around the active-site pocket by random-replacement mutagenesis.	Cephalosporins	102-116	CD248 molecule	Homo sapiens	70-75	
17600829-10	2007	Our results add to the body of evidence suggesting that Tyr105 displays a dynamical behavior resulting in alternate ligand binding modes and are consistent with the lower affinity of TEM-1 for cephalosporins relative to penicillins.	Cephalosporins	193-207	CD248 molecule	Homo sapiens	183-188	
8089110-2	1994	To identify other amino acid substitutions that alter the activity of TEM-1 toward extended-spectrum cephalosporins, a random library was constructed that contained all possible amino acid substitutions over the 3-residue window of 238-241 (ABL numbering).	Cephalosporins	101-115	CD248 molecule	Homo sapiens	70-75	
1644749-6	1992	Substitutions at positions 104, 168, and 238 in the TEM-1 beta-lactamase that resulted in increased enzyme activity towards extended-spectrum cephalosporins were found.	Cephalosporins	142-156	CD248 molecule	Homo sapiens	52-57	
1516458-2	1992	The most common enzymes responsible for resistance to aminopenicillins and older (1st generation) cephalosporins are the TEM-1, TEM-2, OXA-1 and SHV-1 enzymes, all of which are plasmid-mediated.	Cephalosporins	98-112	CD248 molecule	Homo sapiens	121-126	
2550326-5	1989	Analysis of the location of the mutations in the primary and tertiary structures of class A beta-lactamases suggests that interactions between the substituted residues and beta-lactam antibiotics non-hydrolysable by TEM-1 and TEM-2 allow TEM-4 and TEM-5 to hydrolyse efficiently novel broad-spectrum cephalosporins such as Ctx and Caz.	Cephalosporins	300-314	CD248 molecule	Homo sapiens	216-221