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1)  college-Ⅳ
胶原-Ⅳ
2)  Type Ⅳ collagen
Ⅳ型胶原
1.
Effect of compound Rhizoma Coptidis capsule on expression of transforming growth factor-β_1 and type Ⅳ collagen proteins in renal tissue of diabetic rats with nephropathy;
复方黄连胶囊对糖尿病肾病大鼠肾组织TGF-β_1与Ⅳ型胶原蛋白表达的影响
2.
Effects of fluvastatin on the expression of connective tissue growth factor and type Ⅳ collagen in mesangial cells induced by transforming growth factor-β1;
氟伐他汀对转化生长因子β_1诱导的系膜细胞结缔组织生长因子和Ⅳ型胶原表达的影响
3.
Correlation between urinary transforming growth factor beta1&type Ⅳ collagen and the lesion of early diabetic nephropathy along with the intervene effect of Cozaar;
尿TGF-β1、Ⅳ型胶原与早期糖尿病肾损害及科素亚的干预作用
3)  Collagen Ⅳ
Ⅳ型胶原
1.
The Effect of TGF-β_1 in Mediating Collagen Ⅰ and Collagen Ⅳ Synthesis in Neonate Rat Cultured Cardiac Fibroblasts;
TGF-β_1对新生大鼠心肌成纤维细胞Ⅰ型和Ⅳ型胶原合成的影响
2.
TGF-β1 Mediates Collagen Ⅰ and Collagen Ⅳ Synthesis in Neonate Rat Cultured Cardiac Fibroblasts;
TGF-β1介导新生大鼠心肌成纤维细胞Ⅰ型和Ⅳ型胶原合成的研究(英文)
3.
Expressions of transforming growth factor-β_1 and collagen Ⅳ in renal tissues of patients with chronic allograft nephropathy;
TGF-β_1和Ⅳ型胶原在慢性移植肾病患者肾组织中的表达及意义
4)  Collagen TypeⅣ
胶原Ⅳ型
5)  collagen type Ⅳ
胶原Ⅳ型
6)  typeⅣcollagen
Ⅳ型胶原
1.
Objectives:To investigate the effects of advanced glycation end products (AGEs) on the expression of matrix metalloproteinase-2 (MMP-2),the content of typeⅣcollagen and laminin in supernatants of cultured human renal mesangial cells (HRMC).
目的:观察糖基化终产物(advanced glycation end products,AGEs)对人肾系膜细胞(human renal mesangial cell,HRMC)合成和分泌Ⅳ型胶原及层粘连蛋白(laminin,LN)的影响以及药物盐酸氨基胍(aminoguanidine,AG)的干预作用;观察AGEs对HRMC基质金属蛋白酶-2(matrix metallo proteinase-2,MMP-2)表达的影响以及AG的干预效应。
2.
To explore matrix metalloproteinase -2 (MMP-2) and typeⅣcollagen in colon of constipated rabbits,and research on the relationship between them with intractable constipation;3.
目的:1、建立家兔顽固性便秘的动物模型;2、探讨基质金属蛋白酶-2(MMP-2)及其底物Ⅳ型胶原与顽固性便秘疾病的关系;3、行结肠置管,皮下埋泵,并进行顺行冲洗治疗,观察总结疗效,为以后运用到临床提供基础理论依据。
补充资料:胶原三重螺旋体
分子式:
CAS号:

性质: 又称原胶原(tropocollagen)。是胶原分子的组成单元。原胶原呈细长的棒状结构,长约3000nm,直径约1.5nm,分子量为30万左右,由三条等长的α-多肽链(α链)组成。每条α链先自身左旋(螺距约0.95nm),然后相互缠绕(似电缆)形成右旋超螺旋体。螺旋体的主体部分为规整结构,其两端为伸展部分,即氨基端(5.0hm)和羧基端(7.5nm),它们又被称为肽尾(telopeptides),(图暂缺)。胶原三重螺旋体应是确指原胶原规整结构的主体部分,它们对化学试剂、酶等生物制品有很高的稳定性。

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