The Dimerization Function of MinC Resides in a Structurally Autonomous C-Terminal Domain
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| Veröffentlicht in: | Journal of Bacteriology 2001-11, Vol.183 (22), p.6684-6687 |
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| container_title | Journal of Bacteriology |
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| creator | Szeto, T H Rowland, S L King, G F |
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| doi_str_mv | 10.1128/JB.183.22.6684-6687.2001 |
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</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1067-8832</identifier><identifier>EISSN: 1098-5530</identifier><identifier>DOI: 10.1128/JB.183.22.6684-6687.2001</identifier><identifier>PMID: 11673440</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacteriology ; Biochemistry ; Cell Division ; Dimerization ; Escherichia coli ; Escherichia coli - cytology ; Escherichia coli - metabolism ; Genetics and Molecular Biology ; Mass Spectrometry ; Membranes ; MinC protein ; MinD protein ; Molecular Sequence Data ; Peptide Fragments - analysis ; Peptide Fragments - chemistry ; Proline ; Proteins ; Sequence Analysis, Protein</subject><ispartof>Journal of Bacteriology, 2001-11, Vol.183 (22), p.6684-6687</ispartof><rights>Copyright American Society for Microbiology Nov 2001</rights><rights>Copyright © 2001, American Society for Microbiology 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c565t-d664f9cc6bd2b28ab08c157a3ff9bc6b28e1a9a755ffe0d4a6bb1bc0461a77773</citedby><cites>FETCH-LOGICAL-c565t-d664f9cc6bd2b28ab08c157a3ff9bc6b28e1a9a755ffe0d4a6bb1bc0461a77773</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/PMC95501/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC95501/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11673440$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Szeto, T H</creatorcontrib><creatorcontrib>Rowland, S L</creatorcontrib><creatorcontrib>King, G F</creatorcontrib><title>The Dimerization Function of MinC Resides in a Structurally Autonomous C-Terminal Domain</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>Article Usage Stats
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</description><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biochemistry</subject><subject>Cell Division</subject><subject>Dimerization</subject><subject>Escherichia coli</subject><subject>Escherichia coli - cytology</subject><subject>Escherichia coli - metabolism</subject><subject>Genetics and Molecular Biology</subject><subject>Mass Spectrometry</subject><subject>Membranes</subject><subject>MinC protein</subject><subject>MinD protein</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Fragments - chemistry</subject><subject>Proline</subject><subject>Proteins</subject><subject>Sequence Analysis, Protein</subject><issn>0021-9193</issn><issn>1067-8832</issn><issn>1098-5530</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUcFu1DAUtBCILoVfQBYHbkn97MR2JC7tllKqVkiwSNwsx3G6XiV2sRNQ-XocuqKlF3x4tvxmRvPeIISBlABUHl2clCBZSWnJuayKXERJCYEnaAWEi0JKRp-iFSEUigYadoBepLTLgKqq6XN0AMAFqyqyQt82W4tP3Wij-6UnFzw-m7358wg9vnJ-jT_b5DqbsPNY4y9TnM00Rz0Mt_h4noIPY5gTXhcbG0fn9YBPw6idf4me9XpI9tX-PkRfz95v1ufF5acPH9fHl4WpeT0VHedV3xjD2462VOqWSAO10Kzvmzb_UmlBN1rUdd9b0lWaty20hlQctMiHHaJ3d7o3czvazlg_ZXPqJrpRx1sVtFP_drzbquvwQzV1TSDT3-7pMXyfbZrU6JKxw6C9zXMpQSmFhv8fCBIoq7jMwDePgLswx7yYpCgVRAAji2t5BzIxpBRt_9cwELVErC5OsiTLFLVEvBShlogz9fXDge-J-0zvDWzd9fani1bpNKpd-1CP_QZ_P67P</recordid><startdate>20011101</startdate><enddate>20011101</enddate><creator>Szeto, T H</creator><creator>Rowland, S L</creator><creator>King, G F</creator><general>American Society for Microbiology</general><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>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20011101</creationdate><title>The Dimerization Function of MinC Resides in a Structurally Autonomous C-Terminal Domain</title><author>Szeto, T H ; 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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Amino Acid Sequence Bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacteriology Biochemistry Cell Division Dimerization Escherichia coli Escherichia coli - cytology Escherichia coli - metabolism Genetics and Molecular Biology Mass Spectrometry Membranes MinC protein MinD protein Molecular Sequence Data Peptide Fragments - analysis Peptide Fragments - chemistry Proline Proteins Sequence Analysis, Protein |
| title | The Dimerization Function of MinC Resides in a Structurally Autonomous C-Terminal Domain |
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