About: A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum

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About: A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum Goto Sponge NotDistinct Permalink

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scientific article published on 01 June 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 2000 (uk) im Juni 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunu de 2000 (ast) scientific article published on 01 June 2000 (en)
publication date	wds:Q73626652-9D92EED8-D688-438B-AA8D-DA47E71DC297
publication date	2000-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73626652-C5616CAF-DD40-4409-B804-3BD678245E37
language of work or name	English
cites work	wds:Q73626652-1639AE4F-D912-4822-BDC9-9190102388C8 wds:Q73626652-1D3D569D-E2EF-4BF5-BF6F-81C080D446DD wds:Q73626652-1D6FAA92-06B7-4EE5-9007-80253C9B3A47 wds:Q73626652-1DF6A71C-F698-4384-A911-86E9D337265E wds:Q73626652-2096BD94-134C-429E-A20E-5F7E8F4EA6AB wds:Q73626652-23651E72-ED7D-486A-B438-9DC579291B14 wds:Q73626652-3C3A15E1-6105-4453-A9BA-1B8D55C2E076 wds:Q73626652-3C4493BA-ED38-4D62-B9B9-DAD9C1DA3F43 wds:Q73626652-5BFED6A4-6410-4503-B2AB-77562E407C58 wds:Q73626652-5EE6B249-C102-459B-9B63-8612A8A41002 wds:Q73626652-5F0913AA-1B94-426C-8E68-289155D6FD44 wds:Q73626652-6AD86079-75EC-47E5-89C9-761C79FADBAF wds:Q73626652-6FBDE16B-A2D4-445A-BFEC-B8EA4935EA62 wds:Q73626652-7159EAFC-3B2A-4BC4-8106-46AD86C2681E wds:Q73626652-74FD9C11-8BCF-4F66-952A-FFFAA4403443 wds:Q73626652-90234EA0-6B3E-4B89-AFBE-E2F32E559936 wds:Q73626652-9B35D742-3491-46DA-AA29-C5B063A9A57C wds:Q73626652-ABA042B2-AA6E-428A-9F8A-591C9C4492D5 wds:Q73626652-B21A1E99-3C44-4C4D-99B4-794CDAFDA361 wds:Q73626652-B3751561-12F5-4492-89B0-A5583368A029 wds:Q73626652-C2449146-6E53-4710-AA81-7E6F905B3C6D wds:Q73626652-C3591349-A81B-4D74-93FC-89D8D6CC7178 wds:Q73626652-CFE0C3CE-839C-4FD0-A60B-C50557AF7FA8 wds:Q73626652-DC8CF313-9AE5-4D39-A927-1B55D3A93942 wds:Q73626652-F4DB4FA9-83EB-4E2E-98C9-BC21195B68D8 wds:Q73626652-F6D47FBF-6B7A-47C8-B9FE-B49DD746FCBB
cites work	Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product Retrieval of transmembrane proteins to the endoplasmic reticulum Collagens: molecular biology, diseases, and potentials for therapy Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus 10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum A C-terminal signal prevents secretion of luminal ER proteins Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2 Recycling of proteins between the endoplasmic reticulum and Golgi complex Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells A human homologue of the yeast HDEL receptor Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients. Exposed Thiols Confer Localization in the Endoplasmic Reticulum by Retention Rather than Retrieval Membrane association, localization and topology of rat inositol 1,4,5-trisphosphate 3-kinase B: implications for membrane traffic and Ca2+ homoeostasis. The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence The pleckstrin homology domain: an intriguing multifunctional protein module Cloning and characterization of a third human lysyl hydroxylase isoform Monoclonal antibodies to human prolyl 4-hydroxylase A 115-kD polypeptide immunologically related to erythrocyte band 3 is present in Golgi membranes Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse.
author name string	wds:Q73626652-4177BD39-C295-481F-BD4F-76267ED70A96 wds:Q73626652-71D93193-F1DE-40D0-8C09-FB06C978B3C4 wds:Q73626652-DB97E488-0B7C-4616-B6E0-799B794CD0C7
author name string	Kellokumpu S Myllyla R Suokas M
rdfs:label	A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (en) A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (nl)
skos:prefLabel	A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (en) A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (nl)
name	A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (en) A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (nl)
title	wds:Q73626652-9E2CB6E3-028E-40EE-82FB-BD3D74C7A7DB
title	A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum (en)
page(s)	wds:Q73626652-CE2AFA51-86A4-4037-9247-3498DF407304
page(s)	17863-17868
instance of	wds:Q73626652-70245621-B879-4C28-878E-F1BE2F9021DA
instance of	scholarly article
main subject	wds:Q73626652-04CD4528-D0B6-4376-A93D-CA70AAC0BA64
main subject	endoplasmic reticulum
PubMed ID	wds:Q73626652-388C79CD-10CB-40D5-8168-759FB309C33A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10748089
PubMed ID	10748089
published in	wds:Q73626652-CCFB4450-1F01-4244-85F7-946F9E740693
published in	Journal of Biological Chemistry
issue	wds:Q73626652-6E8F8B8A-604E-4210-8545-C4BD8BE0AF3C
volume	wds:Q73626652-870B19E1-4C89-4B87-A6DA-5709BDC5E8F7
issue	23
volume	275
DOI	wds:Q73626652-15A28EB3-C7D4-4DA2-B1E9-32704EBACD9C
DOI	http://dx.doi.org/10.1074/JBC.M908025199
DOI	10.1074/JBC.M908025199
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73626652
is cites work of	TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis Functional diversity of lysyl hydroxylase 2 in collagen synthesis of human dermal fibroblasts Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space. Retrieval-independent localization of lysyl hydroxylase in the endoplasmic reticulum via a peptide fold in its iron-binding domain Collagen beta (1-O) galactosyltransferase 1 (GLT25D1) is required for the secretion of high molecular weight adiponectin and affects lipid accumulation

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