Modulation of protein structure and function by asparagine-linked glycosylation.
about
O-fucosylation is required for ADAMTS13 secretionHyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine designN-glycans in cell survival and death: cross-talk between glycosyltransferasesCharacterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiaeGlycosylation influences cross-species formation of protease-resistant prion protein.Glycoprotein expression in human milk during lactation.Recent findings on the structure and function of teleost IgT.Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contextsContext-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.Effects of glycosylation on peptide conformation: a synergistic experimental and computational study.An allelic series of mutations in the kit ligand gene of mice. I. Identification of point mutations in seven ethylnitrosourea-induced Kitl(Steel) alleles.'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocksThe interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment.Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin.Differential dependence on N-glycosylation of anthrax toxin receptors CMG2 and TEM8Structural stability of myoglobin and glycomyoglobin: a comparative molecular dynamics simulation studyN-glycosylation of enhanced aromatic sequons to increase glycoprotein stabilityPost-translational changes to PrP alter transmissible spongiform encephalopathy strain properties.N-glycans are direct determinants of CFTR folding and stability in secretory and endocytic membrane traffic.Recent Departures in the Synthesis of Peptides and Glycopeptides.Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.N-linked glycosylation in bacteria: an unexpected application.Membrane targeting of ATP-sensitive potassium channel. Effects of glycosylation on surface expression.Structural and functional characterization of a C-type lectin-like antifreeze protein from rainbow smelt (Osmerus mordax).Stability of Curcuma longa rhizome lectin: Role of N-linked glycosylation.Structure and function of the N-linked glycans of HBP/CAP37/azurocidin: crystal structure determination and biological characterization of nonglycosylated HBP.Metabolic glycoengineering bacteria for therapeutic, recombinant protein, and metabolite production applications.Drug-induced amino acid deprivation as strategy for cancer therapy.Enterocyte glycosylation is responsive to changes in extracellular conditions: implications for membrane functions.Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account.The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and functionTotal synthesis of the 2,6-sialylated immunoglobulin G glycopeptide fragment in homogeneous form.Structural requirements for additional N-linked carbohydrate on recombinant human erythropoietin.Glycoprotein Enrichment Analytical Techniques: Advantages and Disadvantages.Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco.Charge and Polarity Preferences for N-Glycosylation: A Genome-Wide In Silico Study and Its Implications Regarding Constitutive Proliferation and Adhesion of Carcinoma Cells.Misfolding and aggregation of vacuolar glycoproteins in plant cells
P2860
Q24301310-D973B9FD-0575-4DC5-93E5-B8A343CBFA0DQ24679395-59DBAF79-34F4-48A8-A0A3-67147BABA9DDQ27027708-936998E8-3205-4600-BF3F-2F5EC2F5E3D3Q27934636-708A46B4-5092-420C-A2DA-D54CE007E551Q28365495-722CF66D-EC76-4AF3-9ABB-D8422C8310A4Q30388479-86A08746-79AD-469D-AD36-EF090DFE9D8CQ30401550-EAEFA883-106A-4E61-AE87-D4B9E6C05A0DQ33875537-4A2FD823-9500-4D74-B2E6-C160D74BF654Q34028044-53D548C8-C9C4-47C4-B608-D8712DD19E8EQ34249680-20EE775A-D5FD-4B6B-896E-49B4CFF8D04AQ34418726-E3008000-BDE0-48E7-8C1D-8E5CDECC0BD1Q34615833-1667A1FE-93C7-4EB5-811D-A1A8F773DA03Q35017648-828EA8A9-E9E8-4123-9D23-41E709BDE98AQ35146215-0D195C56-0D21-4DD8-93D5-1BA7E500CCAAQ35220103-A16D6B90-7B00-4C03-A77D-BDC49F7BA021Q35579665-CC191267-EFFB-4238-850A-E4D43CDA9367Q35998655-A86005BE-DF07-4CD9-BE9F-0E95AF7E5203Q36515262-C975B8DD-1B7A-47A7-9129-925D34043C28Q36664699-A814E3CE-5199-4E41-BF3C-738BAD75F1D3Q37234365-B064EC17-8270-46C9-A000-293C3663D2CAQ37428099-FFF90555-DD39-4971-A3AF-21A7C845962AQ37448617-F266BAE8-88CF-4CEA-B1E4-70017F2FE364Q37470569-C4A35785-10F2-440D-AE21-A4640C82DD86Q38289527-2BC937BC-D818-4E80-9B04-1DFCCCD2F13EQ38291804-7FD803D3-E339-4455-9A0B-57B510AF445EQ38295115-DA168291-C0CF-4604-BE0B-CCEC74E2FA24Q38318788-D9B15D28-753D-4695-8AD8-25405727BECFQ38452524-0612C87E-DA40-42B7-9FEC-59E3D7CB67C9Q38657061-5155761A-8C33-4991-8A33-94660DABD895Q38795724-09425339-8F7E-4D04-AE1B-47C864A307C5Q40316404-3A5D700A-2AFE-4827-A023-987479A130ECQ42025674-59BDFD72-1927-4ADA-B861-F2C2E181E0CDQ42687289-35026308-6897-4AC6-AEE8-5B3689D3240FQ44752485-9D5EBE16-F2CC-4DC3-AD65-9067EC4DB156Q49812897-EA16BDB0-F63C-4CBE-8B3D-F8A98F8DA7CEQ52165355-FC055E59-6BD3-44E1-9DA5-CC2F5A02A90FQ54985550-3667EA9E-F56A-452C-83CC-7CE5308B6344Q59306483-2D8FD3DF-CDC6-4535-B201-5286DB5A381F
P2860
Modulation of protein structure and function by asparagine-linked glycosylation.
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
Modulation of protein structure and function by asparagine-linked glycosylation.
@ast
Modulation of protein structure and function by asparagine-linked glycosylation.
@en
type
label
Modulation of protein structure and function by asparagine-linked glycosylation.
@ast
Modulation of protein structure and function by asparagine-linked glycosylation.
@en
prefLabel
Modulation of protein structure and function by asparagine-linked glycosylation.
@ast
Modulation of protein structure and function by asparagine-linked glycosylation.
@en
P1476
Modulation of protein structure and function by asparagine-linked glycosylation.
@en
P2093
Imperiali B
O'Connor SE
P304
P356
10.1016/S1074-5521(96)90064-2
P577
1996-10-01T00:00:00Z