Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1 - Wikidata - wikimedia - TriplyDB

Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1

Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1

http://www.wikidata.org/entity/Q33812834

about

Glycoproteomic and glycomic databases The Origin and Activities of IgA1-Containing Immune Complexes in IgA Nephropathy The pathophysiology of IgA nephropathy Clinical Glycomics Employing Graphitized Carbon Liquid Chromatography-Mass Spectrometry High-Throughput Analysis and Automation for Glycomics Studies Glycan analysis of therapeutic glycoproteins Glycobioinformatics: current strategies and tools for data mining in MS-based glycoproteomics.Label-free analysis of o-glycosylation site-occupancy based on the signal intensity of glycopeptide/peptide ions Development and Application of Multidimensional HPLC Mapping Method for O-linked Oligosaccharides.Recent advances in cellular glycomic analyses.O-linked glycosylation determines the nephritogenic potential of IgA rheumatoid factor.Determination of carbohydrate structure recognized by prostate-specific F77 monoclonal antibody through expression analysis of glycosyltransferase genes.The genetics and immunobiology of IgA nephropathy.Glycomic and glycoproteomic analysis of glycoproteins-a tutorial.Site-specific glycosylation of secretory immunoglobulin A from human colostrum.Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient.Detection of the heterogeneous O-glycosylation profile of MT1-MMP expressed in cancer cells by a simple MALDI-MS method.Polylactosaminoglycan glycomics: enhancing the detection of high-molecular-weight N-glycans in matrix-assisted laser desorption ionization time-of-flight profiles by matched filtering.Elucidating heterogeneity of IgA1 hinge-region O-glycosylation by use of MALDI-TOF/TOF mass spectrometry: role of cysteine alkylation during sample processing.N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy.Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2009-2010.Bacterial glycosidases in pathogenesis and glycoengineering.MALDI-TOF MS applied to apoC-III glycoforms of patients with congenital disorders affecting O-glycosylation. Comparison with two-dimensional electrophoresis.Benchmark study of automatic annotation of MALDI-TOF N-glycan profiles.O-glycosylated IgA rheumatoid factor induces IgA deposits and glomerulonephritis.The Art of Destruction: Optimizing Collision Energies in Quadrupole-Time of Flight (Q-TOF) Instruments for Glycopeptide-Based Glycoproteomics.Mass spectrometry of transferrin and apolipoprotein C-III for diagnosis and screening of congenital disorder of glycosylation.Longitudinal monitoring of immunoglobulin A glycosylation during pregnancy by simultaneous MALDI-FTICR-MS analysis of N- and O-glycopeptides Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles--part 1: separation-based methods The level of galactose-deficient IgA1 in the sera of patients with IgA nephropathy is associated with disease progression New Insights into the Pathogenesis of IgA Nephropathy.Targeting the glycoproteome Glycoproteomic analysis of antibodies.Comparison of analytical methods for profiling N- and O-linked glycans from cultured cell lines : HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study Glycomics and glycoproteomics of membrane proteins and cell-surface receptors: Present trends and future opportunities.Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma.Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: the ABRF glycoprotein research multi-institutional study 2012 Naturally occurring structural isomers in serum IgA1 o-glycosylation.Analytical tools for the study of cellular glycosylation in the immune system.Cytokines alter IgA1 O-glycosylation by dysregulating C1GalT1 and ST6GalNAc-II enzymes.

P2860

Q21245406-AC14F800-8C48-454A-BCCA-10FCA6E82088 Q26752555-EA7FD386-B8F9-4D80-93E9-62ACD258B889 Q27023866-795140C2-9C18-4441-B011-19EA3DC55F34 Q27024150-FA793C2B-6F98-48C3-BFE5-577958500BE0 Q28080479-BD147489-E3DB-4C3A-A39A-FE57A3E3BF43 Q28082842-C874AD92-DC7B-4E54-A07A-C87D8FF7DDAF Q30578276-F7F1235E-3ED8-421F-BB91-19B264F22374 Q31146356-1474F0BE-F9CE-4E12-8C06-2D1BE25491E6 Q33649454-1DDB2A2B-AF35-4922-9C04-0D782D4ACFEF Q33649651-FE49597E-D5FD-40BA-AE7D-13249E2049FF Q33660620-CFFEBCEA-2364-4BDA-8F72-DFCA90252730 Q33718567-0FB0A78B-430F-4B9E-B33D-798910D28200 Q33872517-F50B6C33-D7EB-4052-A8D0-E10C2846E66E Q33875839-4303AD04-9589-48CF-814D-F9F6DB672F6A Q33920673-5F53BD79-49CC-4EC6-B558-F92087EC9CB7 Q34275670-4B252CD4-79D4-4226-A5A3-43CF0A9483E7 Q34395979-4A50330C-12B5-43A1-A418-B39555D29F6B Q34550562-AD27D946-42C4-42E1-AC0F-6E1C211EDC97 Q34869928-28DB24DB-6B35-4762-8F53-601FEA2AC73C Q35022256-5DEE0899-475F-4A27-A291-2A64ED20AEA2 Q35174495-84DF84C0-0FCB-468F-9CE5-2091C523EFBE Q35362348-86BFFB61-E12E-4A2C-B904-4BA36578C6DA Q35553180-CFCBF2F6-C9BF-421E-A8FD-88523328E6C2 Q35654789-88138387-D54D-47C2-BDE5-88D1183D9121 Q35804190-024DFE19-1D0F-4930-9557-6E6A38796668 Q35884818-97B80006-F1F6-44D6-A128-A99BFC39614D Q35923095-B3D2549B-9FA7-4165-9836-31543E28367F Q36052433-943EF71F-5146-4D38-9391-50ED98824B5C Q36216323-C4A5BC7E-F4B9-462F-83CC-B6A1C675C667 Q36237466-D75DFEE5-C04D-46FD-8FDC-13092CD12747 Q36267833-21DC2100-2CAD-43E7-86A2-29CE2727E8F0 Q36554714-8997DF3F-29E4-4A60-A7B0-B54A8D8EECF5 Q36742404-E2AB2457-BB4E-4AE3-80AE-A4C54E04A645 Q36844855-FE877331-DA9C-41E7-9CD8-C129B957DA2F Q36957711-1E7247A3-748D-49DA-AB10-0F1D96DF48E0 Q37100578-3D32C0A1-3CF5-490A-88FB-D4834C46A143 Q37214705-00233A78-B045-4EF5-ABB0-0F015770F691 Q37352215-05974E7A-BC54-4DB2-82C7-AA14BA775A02 Q37381965-9B0A1E32-B7C2-4F3D-AAF2-D2E47E9F0B92 Q37596411-EE019133-CF40-435A-B9F6-9E253E5C5E9E

P2860

Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1

http://www.wikidata.org/entity/Q33812834

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Comparison of methods for prof ...... ti-institutional study of IgA1

@ast

Comparison of methods for prof ...... ti-institutional study of IgA1

@en

type

label

Comparison of methods for prof ...... ti-institutional study of IgA1

@ast

Comparison of methods for prof ...... ti-institutional study of IgA1

@en

prefLabel

Comparison of methods for prof ...... ti-institutional study of IgA1

@ast

Comparison of methods for prof ...... ti-institutional study of IgA1

@en

P1433

Q33812834-F43E3777-6012-4F50-AE72-6DFBC0710613

P1476

Q33812834-F35B358F-167B-461F-B779-D2DC22A07FFB

P2093

Q33812834-0F1FF0D2-3929-42B5-88D7-2F4DBF7575E2

Q33812834-15F64217-D2DB-4DC9-BF27-E394DF36737C

Q33812834-16CF2E19-0E14-4AE3-96DA-6DE85BD5B6FF

Q33812834-17322649-AD4B-4850-9E1A-C5B57AD62FB3

Q33812834-1752C019-4B75-4B5F-B44E-4BDC80187010

Q33812834-1EE1C864-E75A-439C-A9AF-D2421B3EF1BF

Q33812834-30323F77-07F3-431E-8274-0FDD25FC41C9

Q33812834-36BA5175-78C8-457B-9F9C-AF69226BB785

Q33812834-38ED557B-BE8F-4EEA-94F3-9ABD6464B5E9

Q33812834-3F0D339B-303B-4D6D-9DB0-85060FEB8925

P2860

Q33812834-04BC5FD8-4650-484B-A28A-8E27BD92B48A

Q33812834-2F05D8FC-A852-4114-8B2E-78951DC43ABB

Q33812834-3CBA6D32-26F0-4579-B46B-446E4F9E2360

Q33812834-40AFC754-B38D-4F20-814A-2C65D5369FE9

Q33812834-40D5C39D-CEDC-4DB9-BDF9-BA78579141DF

Q33812834-4A7E0ECF-C969-4E68-A56E-C488E9658647

Q33812834-4DBF026E-B290-4C79-9E02-234B5FC21A7A

Q33812834-4F3C6BAA-D7DD-4F2B-B13C-21A15F9DE0DB

Q33812834-56AE3A5A-2533-434F-BDDB-D2215D26EE3F

Q33812834-57D0E066-37F9-47A1-9D16-DE6AF3C4174C

P304

Q33812834-BC1D451A-E72C-4E8B-AE1A-6D62E99FC20F

P31

Q33812834-8D87847E-8132-40F1-BC4C-32E49E311B09

P356

Q33812834-279C2174-9AA0-4217-8F1C-66E879B6FE64

P433

Q33812834-E58390AD-4519-4800-AE7E-4AF66F4F753C

P478

Q33812834-784022E6-4B56-4F7A-A421-A3586D480918

P50

Q33812834-05897C96-D1BE-40C6-A69C-94206458F107

Q33812834-05B5634F-1758-49C1-B46B-CB38E0E5FD7B

Q33812834-1F1FAF83-7024-48B0-85F8-278BB2B98B39

Q33812834-3EC75480-1698-4AB2-83B4-78418422465C

Q33812834-7262A603-4D39-46B3-81D0-2763C8A6057C

Q33812834-79F176C3-A86C-4B82-AAD4-0F1038C79746

Q33812834-7E4F4A26-612E-41D5-AD06-A70C922D80BA

Q33812834-A89DC7E1-BB61-4744-8E8B-F5EC3C66A2C1

Q33812834-C6705AB2-4B3E-4930-AAFB-292B00445D10

P577

Q33812834-E66DB96D-FD1A-4174-B94B-EB1329EFC2B0

P698

Q33812834-481BBE08-DB0E-4305-BD5E-3C80A9D42BFE

P921

Q33812834-CD80A403-BA74-45D5-8D01-C86D88064A25

P932

Q33812834-C7C19160-002E-44EE-B9E5-6977DF463F72

P356

MCP.M900450-MCP200

P1433

Molecular & Cellular Proteomics

P1476

Comparison of methods for prof ...... ti-institutional study of IgA1

@en

P2093

Akihiro Kondo

http://www.w3.org/2001/XMLSchema#string

Anne Dell

http://www.w3.org/2001/XMLSchema#string

Bérangère Tissot

http://www.w3.org/2001/XMLSchema#string

Carlito Lebrilla

http://www.w3.org/2001/XMLSchema#string

Catherine E Hayes

http://www.w3.org/2001/XMLSchema#string

Elizabeth Palaima

http://www.w3.org/2001/XMLSchema#string

Erina Ohno

http://www.w3.org/2001/XMLSchema#string

Hiromi Ito

http://www.w3.org/2001/XMLSchema#string

Jan Novak

http://www.w3.org/2001/XMLSchema#string

Kazuaki Kakehi

http://www.w3.org/2001/XMLSchema#string

P2860

Heterogeneity of O-glycosylation in the hinge region of human IgA1.

Altered O-glycosylation and sulfation of airway mucins associated with cystic fibrosis.

Human serum IgA1 is substituted with up to six O-glycans as shown by matrix assisted laser desorption ionisation time-of-flight mass spectrometry.

Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics.

Comparison of the methods for profiling glycoprotein glycans--HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.

The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.

Aberrantly glycosylated IgA1 in IgA nephropathy patients is recognized by IgG antibodies with restricted heterogeneity

IgA1-secreting cell lines from patients with IgA nephropathy produce aberrantly glycosylated IgA1

Critical functions of N-glycans in L-selectin-mediated lymphocyte homing and recruitment.

Immunobiology of IgA.

P304

719-727

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/MCP.M900450-MCP200

http://www.w3.org/2001/XMLSchema#string

P433

4

http://www.w3.org/2001/XMLSchema#string

P478

9

http://www.w3.org/2001/XMLSchema#string

P50

Gunnar C Hansson

Catherine Costello

Daniel Kolarich

Niclas G Karlsson

Matthew B. Renfrow

Hisashi Narimatsu

Nicolle H Packer

P577

2009-12-28T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

20038609

http://www.w3.org/2001/XMLSchema#string

P921

P932

2860227

http://www.w3.org/2001/XMLSchema#string