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- Roberto Vanacore
- Division of Nephrology, Department of Medicine and Center for Matrix Biology, Vanderbilt University, Nashville, TN 37232, USA.
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- Amy-Joan L. Ham
- Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, USA.
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- Markus Voehler
- Department of Chemistry, Vanderbilt University, Nashville, TN 37232, USA.
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- Charles R. Sanders
- Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, USA.
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- Thomas P. Conrads
- Laboratory of Proteomics and Analytical Technologies, Advanced Technology Program, SAIC-Frederick, Incorporated, National Cancer Institute, Frederick, MD 21702, USA.
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- Timothy D. Veenstra
- Laboratory of Proteomics and Analytical Technologies, Advanced Technology Program, SAIC-Frederick, Incorporated, National Cancer Institute, Frederick, MD 21702, USA.
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- K. Barry Sharpless
- Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
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- Philip E. Dawson
- Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
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- Billy G. Hudson
- Division of Nephrology, Department of Medicine and Center for Matrix Biology, Vanderbilt University, Nashville, TN 37232, USA.
説明
<jats:title>Toughing It Out in Membranes</jats:title> <jats:p> The formation of crosslinks in the triple-helical structure of collagen is crucial to its function. In the case of collagen IV, which provides structural integrity to the basement membrane of animal tissues, the chemical nature of the crosslinks has been difficult to pin down. <jats:bold> Vanacore <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="5945" page="1230" related-article-type="in-this-issue" vol="325" xlink:href="10.1126/science.1176811">1230</jats:related-article> ) report a combination of high-resolution mass spectrometric and nuclear magnetic resonance studies that establish the crosslink between hydroxylysine-211 and methionine-93 is a sulfimine group (-S=N-). This type of bond appears to have evolved to withstand mechanical stress as animals evolved into more structurally complex organisms. </jats:p>
収録刊行物
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- Science
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Science 325 (5945), 1230-1234, 2009-09-04
American Association for the Advancement of Science (AAAS)
