胚胎肌腱细胞在原胶原蛋白生物合成过程中链间二硫键的形成及螺旋结构的形成。 - Suppr

Suppr

超能文献

Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells.

作者信息

Schofield J D, Uitto J, Prockop D J

出版信息

Biochemistry. 1974 Apr 23;13(9):1801-6. doi: 10.1021/bi00706a004.

DOI:10.1021/bi00706a004

PMID:4366267

Abstract

摘要

相似文献

Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells.胚胎肌腱细胞在原胶原蛋白生物合成过程中链间二硫键的形成及螺旋结构的形成。

Biochemistry. 1974 Apr 23;13(9):1801-6. doi: 10.1021/bi00706a004.

Intracellular collagen and protocollagen from embryonic tendon cells.来自胚胎肌腱细胞的细胞内胶原蛋白和前胶原蛋白。

J Biol Chem. 1973 Jan 25;248(2):720-9.

The sub-cellular location of inter-chain disulfide bond formation during procollagen biosynthesis by embryonic chick tendon cells.胚胎鸡肌腱细胞在原胶原蛋白生物合成过程中链间二硫键形成的亚细胞定位。

Biochem Biophys Res Commun. 1973 Dec 19;55(4):1188-96. doi: 10.1016/s0006-291x(73)80020-8.

Effects of temperature on conformation, hydroxylation, and secretion of chick tendon procollagen.温度对鸡肌腱原胶原的构象、羟基化及分泌的影响

J Biol Chem. 1974 Jul 25;249(14):4480-6.

Intracellular hydroxylation of non-helical protocollagen to form triple-helical procollagen and subsequent secretion of the molecule.非螺旋原胶原蛋白的细胞内羟基化以形成三螺旋前胶原蛋白，随后该分子被分泌。

Eur J Biochem. 1974 Apr 1;43(2):221-30. doi: 10.1111/j.1432-1033.1974.tb03403.x.

Incorporation of cis-hydroxyproline into collagen by tendon cells. Failure of the intracellular collagen to assume a triple-helical conformation.肌腱细胞将顺式羟脯氨酸掺入胶原蛋白中。细胞内胶原蛋白无法呈现三螺旋构象。

Biochim Biophys Acta. 1972 Oct 31;278(3):601-5. doi: 10.1016/0005-2795(72)90023-2.

Synthesis and secretion of under-hydroxylated procollagen at various temperatures by cells subject to temporary anoxia.在经历短暂缺氧的细胞中，不同温度下羟基化不足的前胶原的合成与分泌

Biochem Biophys Res Commun. 1974 Sep 9;60(1):414-23. doi: 10.1016/0006-291x(74)90220-4.

The biosynthesis of basement membrane collagen in embryonic chick lens. 3. Intracellular formation of the triple helix and the formation of aggregates through disulfide bonds.胚胎鸡晶状体中基底膜胶原蛋白的生物合成。3. 三螺旋的细胞内形成以及通过二硫键形成聚集体。

J Biol Chem. 1973 Nov 10;248(21):7432-7.

Secretion of procollagen: evidence for the transfer of nascent polypeptides across microsomal membranes of tendon cells.前胶原的分泌：新生多肽穿过肌腱细胞微粒体膜的证据。

Biochem Biophys Res Commun. 1974 Aug 5;59(3):947-54. doi: 10.1016/s0006-291x(74)80071-9.

Hydroxylation of peptide-bound proline and lysine before and after chain completion of the polypeptide chains of procollagen.前胶原蛋白多肽链完成前后，肽结合的脯氨酸和赖氨酸的羟基化。

Arch Biochem Biophys. 1974 Sep;164(1):210-7. doi: 10.1016/0003-9861(74)90024-1.

引用本文的文献

Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.设计胶原蛋白以揭示基质疾病的多尺度结构-功能映射关系。

Matrix Biol Plus. 2023 Dec 14;21:100139. doi: 10.1016/j.mbplus.2023.100139. eCollection 2024 Feb.

Efficacy of Collagen Particles in Chronic Non Healing Ulcers.胶原蛋白颗粒在慢性难愈合溃疡中的疗效

J Clin Diagn Res. 2015 Jun;9(6):PC01-3. doi: 10.7860/JCDR/2015/11782.6001. Epub 2015 Jun 1.

Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans.过氧化物酶MLT-7和双氧化酶BLI-3的联合细胞外基质交联活性对于秀丽隐杆线虫胚胎后期的生存能力至关重要。

J Biol Chem. 2009 Jun 26;284(26):17549-63. doi: 10.1074/jbc.M900831200. Epub 2009 Apr 30.

The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis.原胶原蛋白的C-前肽结构域可以被一个跨膜结构域取代，而不会影响生物合成过程中的三聚体形成或胶原三螺旋折叠。

EMBO J. 1997 Nov 17;16(22):6694-701. doi: 10.1093/emboj/16.22.6694.

Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen.确定决定原胶原类型特异性组装的分子识别序列。

EMBO J. 1997 Mar 3;16(5):908-16. doi: 10.1093/emboj/16.5.908.

Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation.III型前胶原在半完整细胞中的组装：链缔合、成核和三螺旋折叠不需要链间二硫键的形成，但三螺旋成核确实需要羟基化。

Biochem J. 1996 Jul 1;317 ( Pt 1)(Pt 1):195-202. doi: 10.1042/bj3170195.

Effect of prevention of procollagen triple-helix formation on proline 3-hydroxylation in freshly isolated chick-embryo tendon cells.预防原胶原三螺旋形成对新鲜分离的鸡胚肌腱细胞中脯氨酸3-羟化作用的影响。

Biochem J. 1981 Apr 15;196(1):203-6. doi: 10.1042/bj1960203.

Isolation of a major cell surface glycoprotein from fibroblasts.从成纤维细胞中分离出一种主要的细胞表面糖蛋白。

Proc Natl Acad Sci U S A. 1974 Sep;71(9):3492-6. doi: 10.1073/pnas.71.9.3492.

Chondrocalcin is identical with the C-propeptide of type II procollagen.软骨钙素与II型前胶原的C-前肽相同。

Biochem J. 1986 Aug 1;237(3):923-5. doi: 10.1042/bj2370923.

The calcification of cartilage matrix in chondrocyte culture: studies of the C-propeptide of type II collagen (chondrocalcin).软骨细胞培养中软骨基质的钙化：II型胶原C-前肽（软骨钙素）的研究

J Cell Biol. 1987 May;104(5):1435-41. doi: 10.1083/jcb.104.5.1435.

文献AI研究员

20分钟写一篇综述，助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型，支持多种主流文档格式。

立即体验