LOX (lysyl oxidase)

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Lysyl oxidase: new looks on LOX.

The extracellular matrix proteins collagen and elastin determine, to a large extent, the biomechanical properties of the vessel wall. Both molecules are secreted as monomers, but are posttranslationally modified in the extracellular space in order to generate stable polymers. A critical feature of collagen and elastin fibers is the degree of cross-linking. The first step in cross-linking is the...

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Effect of lysyl oxidase (LOX) on corpus cavernous fibrosis caused by ischaemic priapism

Penile fibrosis caused by ischemic priapism (IP) adversely affects patients' erectile function. We explored the role of lysyl oxidase (LOX) in rat and human penes after ischemic priapism (IP) to verify the effects of anti-LOX in relieving penile fibrosis and preventing erectile dysfunction caused by IP in rats. Seventy-two rats were randomly divided into six groups: control group, control + β-a...

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Expression of lysyl oxidase (LOX) in human placental amnion in preterm labor

Purpose: The proper function of amnion is necessary for a normal pregnancy and delivery to occur. Understanding the change of amnion between term and preterm labor leads to a better method of diagnosis and prevention for preterm labor. Lysyl oxidase (LOX) catalyzes a series of reactions about the formation of cross-linking of collagen fibrils. Human amniotic tissue, containing a large amount of...

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LOXL2 (lysyl oxidase-like 2)

The LOXL2 gene is located on chromosome 8p21.2p21.3 (Jourdan-Le Saux et al., 1998). It is composed of fourteen exons and thirteen introns, distributed through approximately 107 kb of genomic DNA (Fong et al., 2007). Two transcripts of sizes 3.6 kb and 4.9 kb have been reported, with the smaller transcript much more abundant and resulting from three possible termination sites located 690 bp, 740...

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LOXL3 (lysyl oxidase-like 3)

Note LOXL3 is part of the lysyl oxidase (LOX) family, the members of which are secreted extracellular matrix enzymes. LOXL3 contains a C-terminal region that is conserved in all five isoforms of this copper-dependent amine oxidase family. The domains included within this region are a copper-binding site, lysyl and tyrosine residues that form the lysyltyrosine-quinone cofactor (LTQ) and a cytoki...

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ژورنال

عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology

سال: 2011

ISSN: 1768-3262

DOI: 10.4267/2042/44656