PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7791208-4	1995	The revertant beta-lactamase had the same pI as TEM-1 (5.4) and had restored inhibition by clavulanic acid (ID50 reduced from 4.2 microM to 0.15 microM).	Clavulanic Acid	91-106	hypothetical protein	Escherichia coli	48-53	
14534312-2	2003	In TEM-1 and SHV-1, the common class A beta-lactamases, alterations at Ser-130 confer resistance to inactivation by the beta-lactamase inhibitors, clavulanic acid, and tazobactam.	Clavulanic Acid	147-162	hypothetical protein	Escherichia coli	3-8	
11050776-2	2000	These enzymes have arisen by mutation of the genes coding for clavulanate-sensitive, plasmid-mediated beta-lactamases such as TEM-1, TEM-2 and SHV-1.	Clavulanic Acid	62-73	hypothetical protein	Escherichia coli	126-131	
9527373-10	1997	The inhibitory efficacy of sulbactam, clavulanic acid and tazobactam over TEM-1 is inversely proportional to the amounts of enzyme produced.	Clavulanic Acid	38-53	hypothetical protein	Escherichia coli	74-79	
7640670-5	1995	The enzyme was as efficiently inhibited by clavulanic acid and tazobactam as the TEM-1 and TEM-2 beta-lactamases but more than the amoxycillin-clavulanic acid-resistant TRC-1 enzyme.	Clavulanic Acid	43-58	hypothetical protein	Escherichia coli	81-86	
7726509-2	1995	These beta-lactamases derived from TEM-1 enzyme focused at pI 5.2 (n = 68) or 5.4 (n = 39) and were very poorly inhibited by clavulanic acid compared with TEM-1 enzyme.	Clavulanic Acid	125-140	hypothetical protein	Escherichia coli	35-40	
7726509-9	1995	The implication of these novel mutated positions, 165 and 275, in resistance to inactivation by clavulanate was supported by crystallographic data on the TEM-1 enzyme and results of site-directed mutagenesis.	Clavulanic Acid	96-107	hypothetical protein	Escherichia coli	154-159	
8056282-5	1994	A Met-69-Leu variant of TEM-1, obtained by site-directed mutagenesis, has been described as resistant to clavulanate.	Clavulanic Acid	105-116	hypothetical protein	Escherichia coli	24-29	
8067751-5	1994	The doubly mutated derivative of the TEM-1 enzyme (Ser-164/Ser-244) retains the characteristics of the Ser-164 mutant enzyme, i.e., enhanced activity against ceftazidime and sensitivity to inactivation by clavulanate.	Clavulanic Acid	205-216	hypothetical protein	Escherichia coli	37-42	
8432315-3	1993	Forty-six percent of the TEM-1 producing strains were able to transfer this resistance to E. coli J62-2 at 37 degrees C. Analysis of the resulting transconjugants revealed that the degree of resistance to amoxycillin and amoxycillin in combination with clavulanic acid was related to the specific activity of the TEM-1 beta-lactamase.	Clavulanic Acid	253-268	hypothetical protein	Escherichia coli	25-30	
8257123-5	1993	The inhibitory effects of clavulanate, sulbactam, and tazobactam on the TEM-1 enzyme were substantially decreased in comparison with those on IRT-3, as indicated by the 50% inhibitory concentrations.	Clavulanic Acid	26-37	hypothetical protein	Escherichia coli	72-77	
2558615-13	1989	In particular, piperacillin with tazobactam or clavulanic acid, but not with sulbactam, inhibited TEM-1, TEM-2, and SHV-1 enzymes.	Clavulanic Acid	47-62	hypothetical protein	Escherichia coli	98-103	
2692515-4	1989	The beta-lactamase efficiently hydrolyzed cefotaxime and ceftriaxone but only moderately hydrolyzed ceftazidime and was inhibited by clavulanate and sulbactam (1 microM) and by anti-TEM-1 and anti-TEM-2 sera.	Clavulanic Acid	133-144	hypothetical protein	Escherichia coli	182-187	
1316862-6	1992	Its most significant difference is that it is inhibited by clavulanic acid 100-fold less efficiently than the TEM-1 enzyme.	Clavulanic Acid	59-74	hypothetical protein	Escherichia coli	110-115	
1769944-4	1991	However, the TEM-1 and TEM-2 producers were resistant in disc tests to ampicillin/sulbactam and amoxycillin/clavulanic acid, and showed intermediate susceptibility to ticarcillin/clavulanic acid.	Clavulanic Acid	108-123	hypothetical protein	Escherichia coli	13-18	
2661324-3	1989	The TEM-E1 beta-lactamase has a similar molecular weight of 22,000 to the TEM-1 and it is also inhibited by clavulanic acid.	Clavulanic Acid	108-123	hypothetical protein	Escherichia coli	74-79	
3263690-8	1988	Synergy between clavulanate or sulbactam (2 micrograms/mL) and amoxicillin was greater against derivatives producing EBS-Bla than against those producing TEM-1, TEM-2, or SHV-1; this synergy was greater with clavulanate than with sulbactam against derivatives producing SHV-2 and the SHV-2-type enzyme but was similar with clavulanate and sulbactam against those producing CTX-1.	Clavulanic Acid	16-27	hypothetical protein	Escherichia coli	154-159	
3061383-0	1988	In vitro activity of mecillinam and amoxicillin/clavulanic acid against strains of Escherichia coli producing TEM-1, Oxa-1 and chromosomal beta-lactamases.	Clavulanic Acid	48-63	hypothetical protein	Escherichia coli	110-115