PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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