戊二醛连接的蛋白聚糖硫酸皮肤素中的肽序列：来自大鼠尾腱的胶原片段定位蛋白聚糖结合位点。 - Suppr

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超能文献

Peptide sequences in glutaraldehyde-linked proteodermatan sulphate: collagen fragments from rat tail tendon locate the proteoglycan binding sites.

作者信息

Scott J E, Ritchie M, Glanville R W, Cronshaw A D

机构信息

Manchester University, U.K.

出版信息

Biochem Soc Trans. 1997 Nov;25(4):S663. doi: 10.1042/bst025s663.

DOI:10.1042/bst025s663

PMID:9450091

Abstract

摘要

相似文献

Peptide sequences in glutaraldehyde-linked proteodermatan sulphate: collagen fragments from rat tail tendon locate the proteoglycan binding sites.戊二醛连接的蛋白聚糖硫酸皮肤素中的肽序列：来自大鼠尾腱的胶原片段定位蛋白聚糖结合位点。

Biochem Soc Trans. 1997 Nov;25(4):S663. doi: 10.1042/bst025s663.

A role for disulphide bridges in the protein core in the interaction of proteodermatan sulphate and collagen.

Biochem Biophys Res Commun. 1986 Aug 14;138(3):1348-54. doi: 10.1016/s0006-291x(86)80431-4.

Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region.富含硫酸皮肤素的蛋白聚糖在间隙区域的d带与大鼠尾腱胶原蛋白结合。

Biochem J. 1981 Jul 1;197(1):213-6. doi: 10.1042/bj1970213.

Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate. Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycans.硫酸皮肤素位于牛皮肤蛋白聚糖硫酸皮肤素的丝氨酸 - 4上。证明大多数分子仅拥有一条糖胺聚糖链，并比较不同蛋白聚糖糖基化位点周围的氨基酸序列。

Biochem J. 1985 Nov 15;232(1):277-9. doi: 10.1042/bj2320277.

Self-aggregation of bovine skin proteodermatan sulphate promoted by removal of the three N-linked oligosaccharides.

Connect Tissue Res. 1990;24(3-4):225-35. doi: 10.3109/03008209009152151.

Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen.硫酸皮肤素和硫酸蛋白角质素（核心蛋白聚糖、光蛋白聚糖/纤调蛋白聚糖）呈马蹄形。这对它们与胶原蛋白的相互作用具有启示意义。

Biochemistry. 1996 Jul 9;35(27):8795-9. doi: 10.1021/bi960773t.

A study of the interaction in vitro between type I collagen and a small dermatan sulphate proteoglycan.I型胶原蛋白与一种小分子硫酸皮肤素蛋白聚糖的体外相互作用研究。

Biochem J. 1988 May 1;251(3):643-8. doi: 10.1042/bj2510643.

[Conformation analysis of D-xylose-containing O-glycopeptide sequences].[含D-木糖的O-糖肽序列的构象分析]

Carbohydr Res. 1991 Jul 30;214(2):227-34. doi: 10.1016/0008-6215(91)80030-q.

The proteins of proteodermatan and proteokeratan sulphates (decoron and fibromodulon/lumicon) are horseshoe shaped, resembling ribonuclease inhibitor.硫酸蛋白聚糖和硫酸蛋白角质素（decoron和纤维调节素/发光调节素）的蛋白质呈马蹄形，类似于核糖核酸酶抑制剂。

Biochem Soc Trans. 1995 Nov;23(4):515S. doi: 10.1042/bst023515s.

Proteoglycan-collagen arrangements in developing rat tail tendon. An electron microscopical and biochemical investigation.发育中大鼠尾腱中蛋白聚糖-胶原蛋白的排列。一项电子显微镜和生物化学研究。

Biochem J. 1981 Jun 1;195(3):573-81. doi: 10.1042/bj1950573.

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Correlation between growth differentiation factor-15 and collagen metabolism indicators in patients with myocardial infarction and heart failure.心肌梗死和心力衰竭患者生长分化因子-15 与胶原代谢指标的相关性。

J Geriatr Cardiol. 2016 Jan;13(1):88-93. doi: 10.11909/j.issn.1671-5411.2016.01.002.

Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion.I型胶原蛋白的非酶糖基化会减少胶原蛋白与蛋白聚糖的结合，并削弱细胞黏附。

J Cell Biochem. 2008 Aug 1;104(5):1684-98. doi: 10.1002/jcb.21735.

Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.成骨不全症I型胶原蛋白螺旋结构域突变联盟：富含致死性突变的区域与整合素和蛋白聚糖的胶原蛋白结合位点对齐。

Hum Mutat. 2007 Mar;28(3):209-21. doi: 10.1002/humu.20429.

Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model.肌腱、软骨等细胞外基质“形状模块”中的弹性。一种滑动蛋白聚糖-细丝模型。

J Physiol. 2003 Dec 1;553(Pt 2):335-43. doi: 10.1113/jphysiol.2003.050179. Epub 2003 Aug 15.

The structure of interfibrillar proteoglycan bridges (shape modules') in extracellular matrix of fibrous connective tissues and their stability in various chemical environments.纤维结缔组织细胞外基质中纤维间蛋白聚糖桥（“形状模块”）的结构及其在各种化学环境中的稳定性。

J Anat. 1998 Apr;192 ( Pt 3)(Pt 3):391-405. doi: 10.1046/j.1469-7580.1998.19230391.x.

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