Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
about
Lysyl Hydroxylase 3 Localizes to Epidermal Basement Membrane and Is Reduced in Patients with Recessive Dystrophic Epidermolysis BullosaRegulation of post-Golgi LH3 trafficking is essential for collagen homeostasisLoss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null micePreserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient CollagenGene expression and functional studies of the optic nerve head astrocyte transcriptome from normal African Americans and Caucasian Americans donors.Glycosylation modulates melanoma cell α2β1 and α3β1 integrin interactions with type IV collagenGlycosylation and cross-linking in bone type I collagen.2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process.The activities of lysyl hydroxylase 3 (LH3) regulate the amount and oligomerization status of adiponectin.Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin.Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture.Extracellular matrix genes as hypoxia-inducible targets.A novel functional role of collagen glycosylation: interaction with the endocytic collagen receptor uparap/ENDO180Genomic structure and embryonic expression of zebrafish lysyl hydroxylase 1 and lysyl hydroxylase 2.Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance.Lysine post-translational modifications of collagenLessons on the pathogenesis of aneurysm from heritable conditionsA role for collagen IV cross-links in conferring immune privilege to the Goodpasture autoantigen: structural basis for the crypticity of B cell epitopes.Expanding the lysyl hydroxylase toolbox: new insights into the localization and activities of lysyl hydroxylase 3 (LH3).A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene.Disentangling mechanisms involved in collagen pyridinoline cross-linking: The immunophilin FKBP65 is critical for dimerization of lysyl hydroxylase 2Deregulation of the lysyl hydroxylase matrix cross-linking system in experimental and clinical bronchopulmonary dysplasia.Autosomal Recessive Keratoderma-Ichthyosis-Deafness (ARKID) Syndrome Is Caused by VPS33B Mutations Affecting Rab Protein Interaction and Collagen Modification.Inflammation and arthritis: perspectives of the glycobiologist.COL4A1 and COL4A2 mutations and disease: insights into pathogenic mechanisms and potential therapeutic targets.Development and pathologies of the arterial wall.The role of ascorbate in protein folding.Collagen Accumulation in Osteosarcoma Cells lacking GLT25D1 Collagen Galactosyltransferase.Lysyl hydroxylase 3 is secreted from cells by two pathways.Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2Reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix.The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells.The lh3 Glycosyltransferase Directs Target-Selective Peripheral Nerve Regeneration.Hemocyte-secreted type IV collagen enhances BMP signaling to guide renal tubule morphogenesis in Drosophila.Characterisation of the Drosophila procollagen lysyl hydroxylase, dPlod.Overhydroxylation of Lysine of Collagen Increases Uterine Fibroids Proliferation: Roles of Lysyl Hydroxylases, Lysyl Oxidases, and Matrix Metalloproteinases.Optimizing Genomic Methods for Mapping and Identification of Candidate Variants in ENU Mutagenesis Screens Using Inbred Mice.VPS33B and VIPAR are essential for epidermal lamellar body biogenesis and function.Overexpression of PLOD3 promotes tumor progression and poor prognosis in gliomas.
P2860
Q27318540-1D90C22D-A602-4825-A4B3-E7818CF939ADQ28314912-8CA4FE26-EEE8-48AD-BB0F-EC2773549E40Q28510970-92C413E9-E8F1-4328-9AFA-A8B59746C605Q28607123-7317776D-4608-42CA-900D-D3441EEC6FADQ33361962-0DC96DFD-10C4-4B4D-BF7C-13824D5F588DQ33985350-1D0AEC62-C8B5-49A2-A91E-783713C369F4Q34044568-0018C182-FC38-42BF-9EA7-0D76E2390F9CQ34482634-1812D013-A976-4376-87C5-978AC219BFBBQ34499898-97BC2D41-9A56-4DAC-A5A4-3AE3239570A4Q34566125-8872B178-432D-457C-B6C9-41F1C19531D6Q34684864-AFA09EEB-2800-44EA-A5A1-88F0889CA6DAQ34781591-01E2A4B5-F980-41D8-AADE-41CCF171C593Q35213422-73006FA0-769C-49BE-8D2E-80CD4520899DQ35688590-9E9054C4-8057-4580-8E27-BCE567C82EBCQ36080275-3BCC824E-7034-4584-A64B-97E347AF7BDEQ36404717-5B326B11-978D-44EE-A00D-853F7C64AB6DQ36756427-EBBCFE5B-C9A1-42E8-B0F9-40E75121F7D5Q36825505-1680DA0D-0BD6-4BF6-9E1B-6DDE782FA2DCQ36828014-5B919367-1237-47FC-91D9-8CE5AF148174Q36923816-88895B9C-52B8-4D74-BACE-D3863FBC56B0Q37065130-72190C60-BF91-4D86-83E0-D4C5BAE44E65Q37576073-ED15B7AD-5C00-47D1-BD24-0868E2C5F0DEQ37711878-87E43B3C-4C20-48A0-BF6E-FAFB9E572D32Q37754703-279C70E8-B570-4137-8365-0A74819D9A40Q38036904-494269B2-B7E2-4848-9B43-B4E9041CFD61Q38144750-63EF17F5-3D8F-453C-882D-4208DBB3363EQ38154807-11046842-9FA9-495F-A3CE-0A4713BF4C47Q38758686-0498EAD5-AA2A-4305-8998-F9E4188EF74BQ39564424-B175BE55-0553-498A-91DA-E50008960428Q39798194-8E022AC7-5C53-44EF-B7EB-1174BD33063CQ39810232-A578D465-4527-4E9F-8F7E-F9CF2551FAFDQ40009117-72CC1D4D-8664-4C3D-8217-8CC80CF5ABE4Q40167208-35E3228B-F071-4662-BF83-C4772ED5F266Q42114003-31F7319A-50DE-4753-B944-7CB22A9AF0C3Q42425699-1CBE848B-383B-41E2-83A6-E8BE03889C53Q42632135-0BBEEFFC-1269-4304-A4F5-837D642C5A85Q42730647-C6B08B10-F6F1-49B8-883D-5DAE586ECD0EQ50058933-E0EF6E9D-B139-4728-A4FA-2012389260B7Q50154405-9BF5AA50-C638-46EB-AC7D-E373B194C7DFQ55365652-47077F66-E0BF-4A33-81E9-0687A2E16968
P2860
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
description
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im Februar 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/02/15)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/02/15)
@nl
наукова стаття, опублікована в лютому 2006
@uk
مقالة علمية (نشرت في 15-2-2006)
@ar
name
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@ast
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@en
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@nl
type
label
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@ast
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@en
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@nl
prefLabel
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@ast
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@en
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@nl
P2093
P921
P3181
P356
P1476
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
@en
P2093
Antti M. Salo
Derry K. Mercer
Heli Ruotsalainen
Lahja Uitto
Laura Sipilä
Maija Risteli
Miia Vapola
Raija Sormunen
Raili Myllylä
Simon P. Robins
P304
P3181
P356
10.1242/JCS.02780
P407
P577
2006-02-15T00:00:00Z