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Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteinsMolecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegansPurification, characterization, and molecular cloning of a novel rat liver Dopa/tyrosine sulfotransferaseStabilization of a tyrosine O-sulfate residue by a cationic functional group: formation of a conjugate acid-base pair.Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix.Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry.Sulfation, the up-and-coming post-translational modification: its role and mechanism in protein-protein interactionTyrosine modification enhances metal-ion binding.A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins.Nutritional essentiality of sulfur in health and disease.The multi-protein family of sulfotransferases in plants: composition, occurrence, substrate specificity, and functions.Updated perspectives on the cytosolic sulfotransferases (SULTs) and SULT-mediated sulfation.Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells.Tyrosine O-sulfation promotes proteolytic processing of progastrinExistence of a plant tyrosylprotein sulfotransferase: novel plant enzyme catalyzing tyrosine O-sulfation of preprophytosulfokine variants in vitro.Expression of tyrosine-sulfated secretory proteins in Xenopus laevis oocytes. Differential export of constitutive and regulated proteins.Tyrosine O-sulfation.Sulfonation, an underexploited area: from skeletal development to infectious diseases and cancer.Urinary excretion of the uraemic toxin p-cresol in the rat: contribution of glucuronidation to its metabolization.Suppression of DHEA sulfotransferase (Sult2A1) during the acute-phase response.Requirement of tyrosylprotein sulfotransferase-A for proper cuticle formation in the nematode C. elegans.Choice of cellular protein expression system.The essentiality of sulfur is closely related to nitrogen metabolism: a clue to hyperhomocysteinaemia.Cell type-specific transgene expression of the prion protein in Xenopus intermediate pituitary cells.Tissue distribution and ontogeny of sulfotransferase enzymes in mice.Sulfakinin neuropeptides in a crustacean. Isolation, identification andtissue localization in the tiger prawn Penaeus monodon.An innovative strategy for sulfopeptides analysis using MALDI-TOF MS reflectron positive ion modeInhibition of the vacuolar H+-ATPase perturbs the transport, sorting, processing and release of regulated secretory proteins
P2860
Q24313018-EC021113-D7A2-4D21-A76D-6B73253B5F79Q24317447-90B8AEF9-313C-4409-ABB4-984EBA4DADAEQ28115054-42113DB7-938A-465B-982B-ADB5AF9EF522Q28567773-017AF541-5F2D-4EA0-9CDE-0F87A680768EQ30964674-83BE9682-F881-45BF-8BF7-0B45D738AFFDQ32059783-D430FACA-C765-4D28-9393-7DF965E9B5F6Q33193850-4423C2F0-6D58-4D03-B999-14806D2F71A4Q33270497-8C8D6FB3-B980-4AC1-A260-9B15533A8124Q36953175-0387D441-1422-4F5E-A747-EAFC330A5F88Q37226512-46FA4D01-D004-4742-B81E-083498AC3BA4Q38118338-BCBEB479-02EE-4FD3-BBC9-C7027EB6D7ADQ38264122-52ED3DE0-CBC3-48EB-9933-C5213F105972Q38959814-4E08A0C1-721F-418E-A580-B813BDB02CA1Q40367090-68B09114-BEDC-4D45-BDEB-5D1B4574A6D2Q40788653-FC46897E-1C5D-4CBA-A3A3-1DAE74EDD8C5Q40891266-D450E9B6-7E1A-46ED-B2FD-C643B2260D92Q41189127-8BC4C89B-294A-4080-B7E6-858224D83FB5Q42169857-F2446F0D-AC78-4D5F-BC2C-CB7B172D206BQ42317502-D652044C-77B8-468C-AD94-202C33E88FC1Q44478954-775A9B2F-FFC4-4217-93FA-49DED8D0F14FQ44938038-35E04F08-3C64-4713-ACEF-A167C6E6AD5AQ45202856-580600E5-1943-4C71-A231-B1262A42E580Q45966460-93BFEB41-909E-43DB-8A8E-97841516EBE6Q46199961-AF153F28-81B6-4D31-9678-6AEF72898C3CQ46383132-AE9B7465-D493-46AD-83AE-D2B5DFB8A99CQ48484144-A4ADDE64-4538-415F-8586-7DE37CCA20B7Q52576396-7C41DD72-2F0D-4E31-9D46-65ACD292909FQ56789118-8EC49C55-9668-4227-888E-D496AB834662Q57269820-0887B70B-30CC-4D11-AB46-E86A0BF6BDA8
P2860
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Protein tyrosine sulfation, 1993--an update
@ast
Protein tyrosine sulfation, 1993--an update
@en
Protein tyrosine sulfation, 1993--an update
@nl
type
label
Protein tyrosine sulfation, 1993--an update
@ast
Protein tyrosine sulfation, 1993--an update
@en
Protein tyrosine sulfation, 1993--an update
@nl
prefLabel
Protein tyrosine sulfation, 1993--an update
@ast
Protein tyrosine sulfation, 1993--an update
@en
Protein tyrosine sulfation, 1993--an update
@nl
P2093
P1476
Protein tyrosine sulfation, 1993--an update
@en
P2093
R Beisswanger
W B Huttner
P304
P356
10.1016/0009-2797(94)90068-X
P407
P577
1994-06-01T00:00:00Z