Substitutions at Position 105 in SHV Family β-Lactamases Decrease Catalytic Efficiency and Cause Inhibitor Resistance
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| Veröffentlicht in: | Antimicrobial Agents and Chemotherapy 2012-11, Vol.56 (11), p.5678-5686 |
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| container_title | Antimicrobial Agents and Chemotherapy |
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| creator | MEI LI CONKLIN, Benjamin C TARACILA, Magdalena A HUTTON, Rebecca A SKALWEIT, Marion J |
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| doi_str_mv | 10.1128/AAC.00711-12 |
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1752 N Street N.W. • Washington DC 20036
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Print ISSN:
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</description><identifier>ISSN: 0066-4804</identifier><identifier>EISSN: 1098-6596</identifier><identifier>DOI: 10.1128/AAC.00711-12</identifier><identifier>PMID: 22908166</identifier><identifier>CODEN: AACHAX</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Amino Acid Substitution ; Ampicillin - pharmacology ; Anti-Bacterial Agents ; Anti-Bacterial Agents - pharmacology ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; beta-Lactam Resistance ; beta-Lactam Resistance - drug effects ; beta-Lactam Resistance - genetics ; beta-Lactamases ; beta-Lactamases - genetics ; beta-Lactamases - metabolism ; Biocatalysis ; Biological and medical sciences ; Cephalosporins - pharmacology ; Clavulanic Acid - pharmacology ; Enzyme Inhibitors ; Enzyme Inhibitors - pharmacology ; Escherichia coli ; Escherichia coli - drug effects ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Kinetics ; Mechanisms of Resistance ; Medical sciences ; Microbial Sensitivity Tests ; Molecular Docking Simulation ; Mutagenesis, Site-Directed ; Pharmacology. Drug treatments ; Structure-Activity Relationship ; Substrate Specificity ; Sulbactam - pharmacology ; Thienamycins - pharmacology</subject><ispartof>Antimicrobial Agents and Chemotherapy, 2012-11, Vol.56 (11), p.5678-5686</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright © 2012, American Society for Microbiology. All Rights Reserved.</rights><rights>Copyright © 2012, American Society for Microbiology. All Rights Reserved. 2012 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a475t-5a8ab393300fece7dee3866572b38ed75488ad14fbc298a31b4ba9a313535ae43</citedby><cites>FETCH-LOGICAL-a475t-5a8ab393300fece7dee3866572b38ed75488ad14fbc298a31b4ba9a313535ae43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3486564/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3486564/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26545492$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22908166$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MEI LI</creatorcontrib><creatorcontrib>CONKLIN, Benjamin C</creatorcontrib><creatorcontrib>TARACILA, Magdalena A</creatorcontrib><creatorcontrib>HUTTON, Rebecca A</creatorcontrib><creatorcontrib>SKALWEIT, Marion J</creatorcontrib><title>Substitutions at Position 105 in SHV Family β-Lactamases Decrease Catalytic Efficiency and Cause Inhibitor Resistance</title><title>Antimicrobial Agents and Chemotherapy</title><addtitle>Antimicrob Agents Chemother</addtitle><addtitle>Antimicrob Agents Chemother</addtitle><description>Classifications
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</description><subject>Amino Acid Substitution</subject><subject>Ampicillin - pharmacology</subject><subject>Anti-Bacterial Agents</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>beta-Lactam Resistance</subject><subject>beta-Lactam Resistance - drug effects</subject><subject>beta-Lactam Resistance - genetics</subject><subject>beta-Lactamases</subject><subject>beta-Lactamases - genetics</subject><subject>beta-Lactamases - metabolism</subject><subject>Biocatalysis</subject><subject>Biological and medical sciences</subject><subject>Cephalosporins - pharmacology</subject><subject>Clavulanic Acid - pharmacology</subject><subject>Enzyme Inhibitors</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Kinetics</subject><subject>Mechanisms of Resistance</subject><subject>Medical sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Docking Simulation</subject><subject>Mutagenesis, Site-Directed</subject><subject>Pharmacology. Drug treatments</subject><subject>Structure-Activity Relationship</subject><subject>Substrate Specificity</subject><subject>Sulbactam - pharmacology</subject><subject>Thienamycins - pharmacology</subject><issn>0066-4804</issn><issn>1098-6596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc1O3DAUhS3UCgbKruvKqsSiUkPt-CfOBmk0hYI0ElVp2Vo3jsMYJQ6yHdC8Fg_SZ6qnQylddOPrq_P5XPsYobeUHFNaqk_z-eKYkIrSgpY7aEZJrQopavkKzQiRsuCK8D20H-Mtyb2oyS7aK8uaKCrlDN1fTU1MLk3JjT5iSPjrGN2mwZQI7Dy-Or_GZzC4fo1_PhZLMAkGiDbiz9YEm3d4AQn6dXIGn3adM856s8bg2yxMWb7wK9e4NAb8zUYXE3hj36DXHfTRHj7VA_Tj7PT74rxYXn65WMyXBfBKpEKAgobVjBHSWWOr1lqmpBRV2TBl20pwpaClvGtMWStgtOEN1LkywQRYzg7Qydb3bmoG2xrrU4Be3wU3QFjrEZz-V_FupW_Ge824kkJuDD5uDUwYYwy2ez5Lid7kr3P--nf-mpYZ_7DFIQ6lvh2n4PPz_se-e3m3Z-M_n5OBoycAooG-Czk5F_9yUnDB643R-y23cjerBxesztM1gNFC5rl5rRT7BW_6p5I</recordid><startdate>20121101</startdate><enddate>20121101</enddate><creator>MEI LI</creator><creator>CONKLIN, Benjamin C</creator><creator>TARACILA, Magdalena A</creator><creator>HUTTON, Rebecca A</creator><creator>SKALWEIT, Marion J</creator><general>American Society for Microbiology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>20121101</creationdate><title>Substitutions at Position 105 in SHV Family β-Lactamases Decrease Catalytic Efficiency and Cause Inhibitor Resistance</title><author>MEI LI ; CONKLIN, Benjamin C ; TARACILA, Magdalena A ; HUTTON, Rebecca A ; SKALWEIT, Marion J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a475t-5a8ab393300fece7dee3866572b38ed75488ad14fbc298a31b4ba9a313535ae43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Substitution</topic><topic>Ampicillin - pharmacology</topic><topic>Anti-Bacterial Agents</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>beta-Lactam Resistance</topic><topic>beta-Lactam Resistance - drug effects</topic><topic>beta-Lactam Resistance - genetics</topic><topic>beta-Lactamases</topic><topic>beta-Lactamases - genetics</topic><topic>beta-Lactamases - metabolism</topic><topic>Biocatalysis</topic><topic>Biological and medical sciences</topic><topic>Cephalosporins - pharmacology</topic><topic>Clavulanic Acid - pharmacology</topic><topic>Enzyme Inhibitors</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Kinetics</topic><topic>Mechanisms of Resistance</topic><topic>Medical sciences</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Docking Simulation</topic><topic>Mutagenesis, Site-Directed</topic><topic>Pharmacology. 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</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>22908166</pmid><doi>10.1128/AAC.00711-12</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0066-4804 |
| ispartof | Antimicrobial Agents and Chemotherapy, 2012-11, Vol.56 (11), p.5678-5686 |
| issn | 0066-4804 1098-6596 |
| language | eng |
| recordid | cdi_highwire_asm_aac_56_11_5678 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Substitution Ampicillin - pharmacology Anti-Bacterial Agents Anti-Bacterial Agents - pharmacology Antibiotics. Antiinfectious agents. Antiparasitic agents beta-Lactam Resistance beta-Lactam Resistance - drug effects beta-Lactam Resistance - genetics beta-Lactamases beta-Lactamases - genetics beta-Lactamases - metabolism Biocatalysis Biological and medical sciences Cephalosporins - pharmacology Clavulanic Acid - pharmacology Enzyme Inhibitors Enzyme Inhibitors - pharmacology Escherichia coli Escherichia coli - drug effects Escherichia coli - enzymology Escherichia coli - genetics Kinetics Mechanisms of Resistance Medical sciences Microbial Sensitivity Tests Molecular Docking Simulation Mutagenesis, Site-Directed Pharmacology. Drug treatments Structure-Activity Relationship Substrate Specificity Sulbactam - pharmacology Thienamycins - pharmacology |
| title | Substitutions at Position 105 in SHV Family β-Lactamases Decrease Catalytic Efficiency and Cause Inhibitor Resistance |
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