PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19736945-1	2009	Extended-spectrum beta-lactamases (ESBLs) are derivatives of enzymes such as SHV-1 and TEM-1 that have undergone site-specific mutations that enable them to hydrolyze, and thus inactivate, oxyimino-cephalosporins, such as cefotaxime and ceftazidime.	Cefotaxime	222-232	CD248 molecule	Homo sapiens	87-92	
29527530-4	2018	Oxyimino-cephalosporins, such as cefotaxime and ceftazidime, however, are poor substrates for TEM-1 and were introduced, in part, to circumvent beta-lactamase-mediated resistance.	Cefotaxime	33-43	CD248 molecule	Homo sapiens	94-99	
12183265-1	2002	In an early example of DNA shuffling, Stemmer (W. P. C. Stemmer, Nature 370:389-390, 1994) demonstrated a dramatic improvement in the activity of the TEM-1 beta-lactamase toward cefotaxime as the consequence of six amino acid substitutions.	Cefotaxime	178-188	CD248 molecule	Homo sapiens	150-155	
9878443-4	1999	Here we report the results of an experiment in which we have hypermutated the bacterial enzyme TEM-1 beta-lactamase and selected small pools (<1.5x10(5)) of clones for enzymatic activity against the beta-lactam antibiotic cefotaxime.	Cefotaxime	225-235	CD248 molecule	Homo sapiens	95-100	
9878443-5	1999	The experiment resulted in the isolation of a number of TEM-1 mutants with greatly improved activity against cefotaxime.	Cefotaxime	109-119	CD248 molecule	Homo sapiens	56-61	
9878443-6	1999	Among these, clone 3D.5 (E104K:M182T:G238S) exhibited a minimum inhibitory concentration for cefotaxime 20,000-fold higher than wild-type TEM-1 and a catalytic efficiency (kcat/Km) 2383 times higher than the wild-type enzyme.	Cefotaxime	93-103	CD248 molecule	Homo sapiens	138-143	
7547898-0	1995	Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by beta-lactamase TEM-1 and the G238S mutant.	Cefotaxime	98-108	CD248 molecule	Homo sapiens	127-132	
7547898-1	1995	The G238S substitution found in extended-spectrum natural mutants of TEM-1 beta-lactamase induces a new capacity to hydrolyze cefotaxime and a large loss of activity against the good substrates of TEM-1.	Cefotaxime	126-136	CD248 molecule	Homo sapiens	69-74	
7547898-1	1995	The G238S substitution found in extended-spectrum natural mutants of TEM-1 beta-lactamase induces a new capacity to hydrolyze cefotaxime and a large loss of activity against the good substrates of TEM-1.	Cefotaxime	126-136	CD248 molecule	Homo sapiens	197-202	
7547898-3	1995	The hydrolysis of penicillins and cefotaxime by TEM-1 and the G238S mutant shows that the behavior of penicillins and cefotaxime is very different.	Cefotaxime	34-44	CD248 molecule	Homo sapiens	48-53	
7547898-3	1995	The hydrolysis of penicillins and cefotaxime by TEM-1 and the G238S mutant shows that the behavior of penicillins and cefotaxime is very different.	Cefotaxime	118-128	CD248 molecule	Homo sapiens	48-53	
7785992-5	1995	These three strains produced two beta-lactamases with pIs of 5.4 (TEM-1) and 7.6. beta-Lactamase assays revealed that the pI 7.6 enzyme hydrolyzed cefotaxime faster (at a relative hydrolysis rate of 30% compared with that of benzylpenicillin) than either ceftazidime or aztreonam (relative hydrolysis rates of 13 and 3.3%, respectively).	Cefotaxime	147-157	CD248 molecule	Homo sapiens	66-71	
2550326-2	1989	The TEM-4 enzyme, which confers high-level resistance to cefotaxime (Ctx) and ceftazidime (Caz), differed from the TEM-1 penicillinase by four amino acid substitutions.	Cefotaxime	57-67	CD248 molecule	Homo sapiens	115-120	
30501088-9	2018	A more exhaustive dynamic analysis, using a selection pressure for ampicillin and cefotaxime resistance on all possible types of substitutions in the amino acid sequence of TEM-1, further demonstrated the observed mechanism.	Cefotaxime	82-92	CD248 molecule	Homo sapiens	173-178	
27173379-4	2016	We measured the effect on ampicillin resistance of ~12,500 unique single amino acid mutants of the TEM-1, TEM-17, TEM-19, and TEM-15 beta-lactamase alleles, which constitute an adaptive path in the evolution of cefotaxime resistance.	Cefotaxime	211-221	CD248 molecule	Homo sapiens	99-104	
25489790-3	2015	Many of the active site residues are conserved between the CTX-M family and non-ESBL beta-lactamases such as TEM-1, but the residues Ser237 and Arg276 are specific to the CTX-M family, suggesting that they may help to define the increased specificity for cefotaxime hydrolysis.	Cefotaxime	255-265	CD248 molecule	Homo sapiens	109-114	
25489790-5	2015	Substitutions of Ser237 and Arg276 with their TEM-1 counterparts, Ala237 and Asn276, had a modest effect on cefotaxime hydrolysis, as did removal of the Arg276 side chain in an R276A mutant.	Cefotaxime	108-118	CD248 molecule	Homo sapiens	46-51