about
Complete sequence of the human mucin MUC4: a putative cell membrane-associated mucinNKp44, a triggering receptor involved in tumor cell lysis by activated human natural killer cells, is a novel member of the immunoglobulin superfamilyCloning and characterization of gp36, a human mucin-type glycoprotein preferentially expressed in vascular endotheliumMolecular and functional characterization of IRp60, a member of the immunoglobulin superfamily that functions as an inhibitory receptor in human NK cellsEpisialin (MUC1) overexpression inhibits integrin-mediated cell adhesion to extracellular matrix componentsMolecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cellsThe Cys-rich region of hepatitis A virus cellular receptor 1 is required for binding of hepatitis A virus and protective monoclonal antibody 190/4The human homolog of HAVcr-1 codes for a hepatitis A virus cellular receptorThe structure and function of proline-rich regions in proteinsHuman meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretionSurface glycans of Candida albicans and other pathogenic fungi: physiological roles, clinical uses, and experimental challenges.MUC1: a multifunctional cell surface component of reproductive tissue epitheliaStructure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamilyIdentification of three mannoproteins in the cell wall of Saccharomyces cerevisiaeIntegrity of Narrow Epithelial Tubes in the C. elegans Excretory System Requires a Transient Luminal MatrixInitiation of T cell signaling by CD45 segregation at 'close contacts'Complement regulation at the molecular level: The structure of decay-accelerating factorCrystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor unit presented in transStructural basis of flocculin-mediated social behavior in yeastCrystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyxNeurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neuritesSaccharomyces cerevisiae a- and alpha-agglutinin: characterization of their molecular interactionMembers of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves.Functional characterization of the YUR1, KTR1, and KTR2 genes as members of the yeast KRE2/MNT1 mannosyltransferase gene family.Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity.Bud8p and Bud9p, proteins that may mark the sites for bipolar budding in yeast.Mid2 is a putative sensor for cell integrity signaling in Saccharomyces cerevisiae.Saccharomyces cerevisiae mid2p is a potential cell wall stress sensor and upstream activator of the PKC1-MPK1 cell integrity pathwayIdentification of a mannoprotein present in the inner layer of the cell wall of Saccharomyces cerevisiae.Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferaseShedding of kidney injury molecule-1, a putative adhesion protein involved in renal regenerationGlycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) mucin is expressed by lactating mammary gland epithelial cells and is present in milkBiosynthesis and shedding of epiglycanin: a mucin-type glycoprotein of the mouse TA3Ha mammary carcinoma cellDatabase analysis of O-glycosylation sites in proteins.Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segmentsPrediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sitesMolecular characterization of a family of metalloendopeptidases from the intestinal brush border of Haemonchus contortus.Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study.Identification and Functional Characterization of Glycosylation of Recombinant Human Platelet-Derived Growth Factor-BB in Pichia pastorisAdaptive evolution by mutations in the FLO11 gene.
P2860
Q22008776-D1523032-3A2B-4C65-870D-8ACB46263E0DQ22008826-F278A165-0C56-41D8-B5DE-74C29452E01FQ22010210-825EA7B8-C4AB-4208-917E-38B36466630EQ22010724-3D88D117-459F-4CC6-87CD-19ADCF342258Q24312497-0BF8F8CA-98DE-44C3-9D33-AF04857FD044Q24314822-4979CFE4-3C6A-4EE3-A889-BBD58E9188DFQ24523091-C1068689-B6F3-4464-B201-34B753DD9747Q24523454-39D15BDE-B0DA-4D67-9279-87585C4606A8Q24528663-A3ABCDFB-A77F-48FC-8572-89F0CC9FA2A6Q24535259-C87BC58B-DD37-4FCA-89AA-52EAA7D0AC5CQ24625384-068988EF-701E-48EB-A6EE-B6555D977806Q24633038-76625F0C-03B0-4521-B87A-647B435076C7Q24643048-62FFB2ED-FF42-413E-9D45-3D7B189EC5C0Q27187092-FD45A6DD-9ED1-4698-8D62-45D60905CAC9Q27308141-3BC82084-AE47-4FEC-AA5D-CDAA478CC85CQ27315848-A09AE596-2B14-4967-B185-340687255BF9Q27643002-20284D86-AB82-423D-BB99-353D62D97B10Q27646838-D5466FB6-B72B-4C71-8FBA-B20EC3ECDCC2Q27666352-C626AA9A-7728-41BC-976E-DCF64AA30CC0Q27670793-5186CA62-F546-4D84-BE00-1BDAEFFFFC0DQ27867694-8ED58C35-1BA9-4A52-AE75-1C6F92B8A79AQ27932289-73C77395-5950-4DED-832F-A0F657BD1613Q27932724-D4849A54-C742-454D-8561-C3FB0FDF657EQ27933475-E429DE4D-17E0-4D18-A632-C53682C854ABQ27934261-16AA8EDF-8EDE-4019-8C6D-191CD3A6DC3EQ27935824-B6120963-80D4-4B09-985A-8345CC6142F5Q27936923-8611DED3-015B-4E71-AB20-BE5EA1AB8C37Q27939724-250EB66B-3E60-41D1-95A5-D4FEFF616ADDQ27940218-B1C42049-F203-4523-9BE9-2DE3FB3037F7Q28114903-1EA05386-04FE-4CE5-B612-6681012C5177Q28215816-F4314BE7-FF6A-4895-BE1E-F952A0B6FB21Q28261440-4097DB66-F4CC-45CB-B6BB-338C27141127Q28345062-F1A2F67B-74DF-4577-880F-ECCF539044B4Q28346313-158062CF-8C0B-494C-BC0F-A119176FF561Q28566036-9FFA3592-27D7-43B0-84DB-A18C6E659F27Q29615170-F8469FE6-5ABC-4B1F-9ECE-F31B4C654E38Q30354699-58BBF8EB-9744-4CF5-B71A-A1FD5056285DQ30372497-985CF39D-1DB4-422A-B1D0-E4565387C00BQ30382850-20962496-8C71-419C-B4BE-A94B70B5BAD7Q30477809-87E324A9-6BA8-4015-B45B-C47E20DC8A5C
P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Why are proteins O-glycosylated?
@en
Why are proteins O-glycosylated?
@nl
type
label
Why are proteins O-glycosylated?
@en
Why are proteins O-glycosylated?
@nl
prefLabel
Why are proteins O-glycosylated?
@en
Why are proteins O-glycosylated?
@nl
P1476
Why are proteins O-glycosylated?
@en
P2093
P304
P356
10.1016/0968-0004(90)90014-3
P577
1990-08-01T00:00:00Z