Results 11 to 20 of about 26,398 (197)

Lysyl Oxidase [PDF]

open access: yesArteriosclerosis, Thrombosis, and Vascular Biology, 2002
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.
Robert Rucker   +3 more
openaire   +3 more sources

The Interactome of Cancer-Related Lysyl Oxidase and Lysyl Oxidase-Like Proteins [PDF]

open access: yesCancers, 2020
The members of the lysyl oxidase (LOX) family are amine oxidases, which initiate the covalent cross-linking of the extracellular matrix (ECM), regulate ECM stiffness, and contribute to cancer progression. The aim of this study was to build the first draft of the interactome of the five members of the LOX family in order to determine its molecular ...
Sylvain D. Vallet   +4 more
openaire   +2 more sources

Emergence of highly profibrotic and proinflammatory Lrat+Fbln2+ HSC subpopulation in alcoholic hepatitis

open access: yesHepatology, EarlyView., 2022
Lrat+ quiescent hepatic stellate cells (qHSC) give rise to Lrat+Fbln2+ activated HSC (aHSC) in alcohol‐associated hepatitis and this subpopulation is highly profibrotic, inflammatory, and immunoregulatory based on their single cell transcriptomic profile. Abstract Background and Aims Relative roles of HSCs and portal fibroblasts in alcoholic hepatitis (
Steven Balog   +12 more
wiley   +1 more source

Multifunctional Lysyl Oxidases

open access: yesInternational Journal of Molecular Sciences, 2023
This Special Issue on lysyl oxidases, which are proteins derived from five related genes known as Lox, and Loxl1–Loxl4, brings together articles that reflect some of the diverse approaches and perspectives needed to better understand the biology of these multifunctional proteins [...]
openaire   +2 more sources

LOX (lysyl oxidase) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on LOX (lysyl oxidase), with data on DNA, on the protein encoded, and where the gene is implicated.
Fong, SFT, Fong, KSK, Csiszar, K
openaire   +2 more sources

Focus on Molecules: Lysyl oxidase [PDF]

open access: yesExperimental Eye Research, 2012
1. StructureLysyl Oxidase (LOX, also called protein-lysine 6-oxidase)(Genbank accession numbers: Nucleotide NM_002317.5, ProteinNP_002308.2, EC 1.4.3.13) is one of the five LOX family members(LOX and LOX Like1-4). The human LOX gene is located onchromosome 5q23.2.
Anirudh, Sethi   +2 more
openaire   +2 more sources

Human lysyl oxidase-like 2 [PDF]

open access: yesBioorganic Chemistry, 2014
Lysyl oxidase like-2 (LOXL2) belongs to the lysyl oxidase (LOX) family, which comprises Cu(2+)- and lysine tyrosylquinone (LTQ)-dependent amine oxidases. LOXL2 is proposed to function similarly to LOX in the extracellular matrix (ECM) by promoting crosslinking of collagen and elastin.
Moon, Hee-Jung   +3 more
openaire   +3 more sources

Lysyl Oxidases in the Trabecular Meshwork [PDF]

open access: yesJournal of Glaucoma, 2014
The mechanical properties of the extracellular matrix (ECM) play an important role in maintaining cellular function and overall tissue homeostasis. Emerging evidence suggests that biomechanical modifications of the ECM may be initiators and/or drivers of disease, exemplified by increased tissue stiffness.
Robert J, Wordinger, Abbot F, Clark
openaire   +2 more sources

Targeting lysyl oxidase reduces peritoneal fibrosis [PDF]

open access: yesPLOS ONE, 2017
Abdominal surgery and disease cause persistent abdominal adhesions, pelvic pain, infertility and occasionally, bowel obstruction. Current treatments are ineffective and the aetiology is unclear, although excessive collagen deposition is a consistent feature.
Christopher R. Harlow   +12 more
openaire   +5 more sources

Fibulin-4 is essential for maintaining arterial wall integrity in conduit but not muscular arteries [PDF]

open access: yes, 2017
Homozygous or compound heterozygous mutations in fibulin-4 (FBLN4) lead to autosomal recessive cutis laxa type 1B (ARCL1B), a multisystem disorder characterized by significant cardiovascular abnormalities, including abnormal elastin assembly, arterial ...
Broekelmann, Thomas J   +5 more
core   +3 more sources

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