Advances in collagen cross-link analysis.

by: DR Eyre, MA Weis, JJ Wu

Methods (San Diego, Calif.), Vol. 45, No. 1. (May 2008), pp. 65-74.

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Abstract

The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement.

@article{citeulike:2784495, abstract = {The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement.}, address = {Orthopaedic Research Labs, Department of Orthopaedics \& Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA.}, author = {Eyre, D. R. and Weis, M. A. and Wu, J. J. }, citeulike-article-id = {2784495}, doi = {10.1016/j.ymeth.2008.01.002}, issn = {1046-2023}, journal = {Methods (San Diego, Calif.)}, month = {May}, number = {1}, pages = {65--74}, posted-at = {2008-05-11 15:41:20}, priority = {2}, title = {Advances in collagen cross-link analysis.}, url = {http://dx.doi.org/10.1016/j.ymeth.2008.01.002}, volume = {45}, year = {2008} }

RIS record

TY - JOUR ID - citeulike:2784495 TI - Advances in collagen cross-link analysis. JF - Methods (San Diego, Calif.) VL - 45 IS - 1 SP - 65 EP - 74 AD - Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA. SN - 1046-2023 N2 - The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement. AU - Eyre, DR AU - Weis, MA AU - Wu, JJ PY - 2008/05// UR - http://dx.doi.org/10.1016/j.ymeth.2008.01.002 ER -

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