Results 181 to 190 of about 155,219 (227)

Lysyl Oxidase Family Enzymes and Their Role in Tumor Progression

open access: yesInternational Journal of Molecular Sciences, 2022
The five genes of the lysyl oxidase family encode enzymes that covalently cross-link components of the extracellular matrix, such as various types of collagen and elastin, and, thus, promote the stabilization of extracellular matrixes.
Shira Toledano   +2 more
exaly   +2 more sources
Some of the next articles are maybe not open access.

Related searches:

A micromethod for the purification of lysyl oxidase

Analytical Biochemistry, 1982
Abstract A simple, efficient, and rapid procedure for the purification of lysyl oxidase is described. This method utilizes an affinity scheme involving powdered elastin-hydroxyethylmethacrylate hydrogels and high-performance liquid chromatography and permits the study of enzyme from sources which contain limited amounts of enzyme, such as aortic ...
R, Ferrera   +4 more
openaire   +2 more sources

The origin of lysyl oxidase

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1994
Lysyl oxidase initiates crosslink formation of the collagen and elastin extracellular matrix, thereby delimiting its expansive properties. Recently lysyl oxidase has been cloned from several species enabling the computation of the relative order of appearance of the various components of this enzyme system.
openaire   +2 more sources

Lysyl Oxidases: Functions and Disorders

Journal of Glaucoma, 2018
Lysyl oxidases (LOX) are copper-dependent enzymes that oxidize lysyl and hydroxylysyl residues in collagen and elastin, as a first step in the stabilization of these extracellular matrix proteins through the formation of covalent cross-linkages, an essential process for connective tissue maturation.
Fernando, Rodriguez-Pascual   +1 more
openaire   +2 more sources

Lysyl Oxidase and Lysyl Oxidase-Like Enzymes

2010
Lysyl oxidase (LOX) and its four congeners, lysyl oxidase-like 1 (LOXL1), -2, -3, and -4, have received much investigative attention in recent years. LOX itself, is the prototypic form of these amine oxidase enzymes. LOX has long been considered to function exclusively as the enzyme that oxidizes peptidyl lysine in its collagen and elastin substrates ...
Herbert M. Kagan, Faina Ryvkin
openaire   +1 more source

An ultrafiltration assay for lysyl oxidase

Analytical Biochemistry, 1990
A modification of the original microdistillation assay for lysyl oxidase is described in which Amicon C-10 microconcentrators are used to separate, by ultrafiltration, the 3H-labeled products released from a [4,5-3H]-lysine-labeled elastin substrate.
D R, Shackleton, D J, Hulmes
openaire   +2 more sources

Stability and purification of lysyl oxidase

Archives of Biochemistry and Biophysics, 1974
Abstract Previous attempts to purify lysyl oxidase have been frustrated by the failure to recover activity during ion exchange or affinity chromatography. We have found that lysyl oxidase from chick cartilage shows marked stability in buffers containing urea and in these solutions can be recovered in high yield from DKAE-cellulose and collagen ...
A S, Narayanan, R C, Siegel, G R, Martin
openaire   +2 more sources

Properties and Function of Lysyl Oxidase

American Journal of Respiratory Cell and Molecular Biology, 1991
Abstract Lysyl oxidase catalyzes the oxidation of peptidyl lysine to α-aminoadipic-δ-semialdehyde, the precursor to the covalent crosslinkages that stabilize fibers of elastin and collagen. This enzyme contains both copper and a carbonyl cofactor consistent with an o-quinone.
H M, Kagan, P C, Trackman
openaire   +2 more sources

On the inhibition of lysyl oxidase by β-aminopropionitrile

Biochemical and Biophysical Research Communications, 1972
Summary β-Aminopropionitrile binds to and inactivates lysyl oxidase, the enzyme carrying out the first step in the cross-linking of collagen and elastin.
A S, Narayanan, R C, Siegel, G R, Martin
openaire   +2 more sources

Lysyl Oxidases

Respirology, 2015
Aim: The development of fibrosis in Idiopathic Pulmonary Fibrosis (IPF) is a key feature and challenge in the treatment of the disease. The mechanisms of collagen I (COL1) reorganisation in the development of fibrosis, which may alter the stiffness of the tissue, are not well understood.
Tjin, G.   +4 more
openaire   +1 more source

Home - About - Disclaimer - Privacy