The effect of Fc glycan forms on human IgG2 antibody clearance in humans. - Wikidata - wikimedia - TriplyDB

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

http://www.wikidata.org/entity/Q46272691

about

Fc glycans of therapeutic antibodies as critical quality attributes In vitro and in vivo modifications of recombinant and human IgG antibodies High-throughput biophysical analysis and data visualization of conformational stability of an IgG1 monoclonal antibody after deglycosylation.High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans.Quantification of intracellular nucleotide sugars and formulation of a mathematical model for prediction of their metabolism.Glycosylation profiling of therapeutic antibodies in serum samples using a microfluidic CD platform and MALDI-MS.Analytical characterization of ch14.18: a mouse-human chimeric disialoganglioside-specific therapeutic antibody.N-glycan PK Profiling Using a High Sensitivity nanoLCMS Work-Flow with Heavy Stable Isotope Labeled Internal Standard and Application to a Preclinical Study of an IgG1 Biopharmaceutical.Time-Dependent Structural Alteration of Rituximab Analyzed by LC/TOF-MS after a Systemic Administration to Rats.Production, characterization, and pharmacokinetic properties of antibodies with N-linked mannose-5 glycans.Increased serum clearance of oligomannose species present on a human IgG1 molecule.Positron emission tomography imaging of fibrillar parenchymal and vascular amyloid-β in TgCRND8 mice.Stability of IgG isotypes in serum.Assessing monoclonal antibody product quality attribute criticality through clinical studies.Critical comparison of MS and immunoassays for the bioanalysis of therapeutic antibodies.Quality attributes of recombinant therapeutic proteins: an assessment of impact on safety and efficacy as part of a quality by design development approach.Proposed mechanism of off-target toxicity for antibody-drug conjugates driven by mannose receptor uptake.A systems biology approach to optimising hosts for industrial protein production.Assessment of the metabolism of therapeutic proteins and antibodies.Recent advances in the understanding of biological implications and modulation methodologies of monoclonal antibody N-linked high mannose glycans.Post-translational structural modifications of immunoglobulin G and their effect on biological activity.Impact of IgG Fc-Oligosaccharides on Recombinant Monoclonal Antibody Structure, Stability, Safety, and Efficacy.Glycosylation of monoclonal antibody products: Current status and future prospects.Pharmacokinetics of monoclonal antibodies and Fc-fusion proteins.Impact of cell culture on recombinant monoclonal antibody product heterogeneity.Effects of cell culture conditions on antibody N-linked glycosylation--what affects high mannose 5 glycoform.Quantitation and pharmacokinetic modeling of therapeutic antibody quality attributes in human studies.Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc.Effects of altered FcγR binding on antibody pharmacokinetics in cynomolgus monkeys Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion.Assessing in vivo dynamics of multiple quality attributes from a therapeutic IgG4 monoclonal antibody circulating in cynomolgus monkey 5th European Antibody Congress 2009: November 30–December 2, 2009, Geneva, Switzerland.4th European Antibody Congress 2008: December 1-3, 2008, Geneva, Switzerland.Production of sialylated O-linked glycans in Pichia pastoris.Separation of nonfucosylated antibodies with immobilized FcγRIII receptors.Cell culture media supplementation of uncommonly used sugars sucrose and tagatose for the targeted shifting of protein glycosylation profiles of recombinant protein therapeutics.Microheterogeneity of Recombinant Antibodies: Analytics and Functional Impact.Analytical comparability study of recombinant monoclonal antibody therapeutics.Regulatory considerations for development of bioanalytical assays for biotechnology products.A novel glycosylated anti-CD20 monoclonal antibody from transgenic cattle

P2860

Q26799266-CF51D897-483B-4931-9C59-1ED0BDA77DDF Q26859713-C711474F-CAAE-49FE-8802-8E13118BE85C Q30675226-E4DFCF85-9EA2-468F-8559-A2A6B88B76F8 Q31004131-98342700-40B3-4DE3-B377-899688673447 Q34177450-33EC3184-1679-44A7-AD00-01E19694F89E Q34697409-D2EC8044-57AB-4827-A3CA-4660826D1935 Q35918866-39B933CE-0736-444B-BAD4-2CE2EA4BEFC4 Q36133312-01912B44-4294-4267-B591-46FA189B37B7 Q36239584-36F4FAF9-01B2-49D3-82FB-87C7741CC1F7 Q36402805-FB42E1C1-0886-46C5-9469-954A4149802C Q36402812-339E14A2-3B73-4D89-8AA4-929C88F4F72C Q36776410-7422EAA4-5686-4316-A5C9-E4C3A9A5BDCD Q37734089-6FA43211-7C5F-4FC4-9733-F11627B36A6E Q37776618-C68C1AAB-9349-4DEA-842E-E976FAC5275A Q37810155-6BD6AAE0-26F9-40CF-A219-655E0F2B19F4 Q37999739-15305A9D-9D53-42D4-B5D3-DC586D2BB477 Q38065955-E3B28264-9507-4514-AC38-6394F17C2F23 Q38124736-522768A5-DF1E-4989-8337-1B28DB848597 Q38217623-8DCE0FE1-50E4-4140-93DD-2D0B4B297C37 Q38224264-1E5E857B-E64F-4A5D-9E0B-2E97BAB41094 Q38246996-18A097F7-D6E7-4B82-8CFC-051C771E340C Q38762019-5D759975-9FA5-4A99-957C-0D4F9DB5B803 Q38807919-F7D95890-0B40-4D3E-8D74-A36C9C22BCA9 Q38831148-57C08303-A023-438B-AF4D-791858ADB55D Q38907094-96E5B626-56BF-4607-840A-B36E5808A67D Q39545373-F99E7489-FB19-4DDF-A7B3-B9EDFFA82B16 Q39742032-0ED0E8EC-9C9F-4A33-A357-8CB36B6A688E Q40353652-E4681879-727D-4A29-81C4-E3E277C059D8 Q41880655-45764390-817E-45B7-9CEC-C722A8172F7D Q42132914-D0595E58-6BCA-40B4-A10A-0499ADB77205 Q42390704-55876984-F922-4B3D-8979-6AC29F142832 Q42869354-B49BF034-F90F-4757-A0DC-51155AC8715D Q43072108-62937B4C-608A-46FA-86A4-204A863E9CA7 Q44001064-CE6D4D8F-309C-46BA-A036-6A30A164D5B6 Q46360891-A2618EC2-883D-41EF-BF20-BB03724A83B9 Q46850981-A3E7A2C3-7F58-4FE2-B021-82A3D2713E42 Q50237001-1418D0D9-2AE8-42B9-A6F6-2789A3D216F5 Q52669512-4E18B62C-9C7A-41AA-8DFF-BF7DF067077C Q54382464-7D423C53-DD55-46B3-AC9E-E0B14FC0271B Q58765419-5276319F-21BD-4820-94B7-0F18139C834A

P2860

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

http://www.wikidata.org/entity/Q46272691

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年学术文章

@wuu

2008年学术文章

@zh

2008年学术文章

@zh-cn

2008年学术文章

@zh-hans

2008年学术文章

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh-hant

name

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@en

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@nl

type

label

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@en

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@nl

prefLabel

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@en

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@nl

P1433

Q46272691-C4983D3F-F507-4703-8855-F6AD65998F0B

P1476

Q46272691-618B95CD-9B1B-4870-B786-9B29E53DEDD5

P2093

Q46272691-6DD02887-0974-4588-949C-B70FD69396E6

Q46272691-E34B6AD7-A6BC-43AE-A75F-2B7AFF44137A

Q46272691-EC0B207A-977C-4BE3-86B5-BD857BA09E48

P2860

Q46272691-2E1B6180-D273-4293-A6CC-9C1FD3BB1C9D

Q46272691-5D11D1F1-D982-4ECA-A569-AF997271CFC5

Q46272691-73771A2C-2E30-47D6-9A47-4B3B9BEDC702

Q46272691-8719428B-82BD-4F71-856D-37D39686AEE2

Q46272691-A72D509D-56C7-4E9B-96B8-0A6975F83BBE

Q46272691-AF6C5518-3AC2-458F-A20B-7FBBDCA75317

Q46272691-B982D916-A990-4E42-8019-654840EF021A

Q46272691-C03EEE65-AEF4-461B-BEDD-DCED59681DC8

Q46272691-D01A37AA-E093-4BF7-97CE-58C690FB3DE1

Q46272691-DF0BC06C-368A-4BCF-86CC-ABB026A19382

P304

Q46272691-00699171-DB6D-4F66-929C-3B399CEF4FCF

P31

Q46272691-51819C8C-AF07-463F-AE27-82EF8B08DF39

P356

Q46272691-FEB2D90D-FC94-4C5F-BD35-EB6CDF6CD3E5

P433

Q46272691-CA3B124F-53C5-4369-BB0C-D8A411E4C520

P478

Q46272691-0482A8BD-595E-4D4F-8581-5B1594317BCC

P577

Q46272691-0EAADF70-FC99-4200-91CE-B898D3E6CEAA

P5875

Q46272691-7BBB73E3-387C-4703-B168-6979AF4C546A

P698

Q46272691-7ACA0952-A9C1-4783-B0F7-EE5CBA8A74A3

P921

Q46272691-981FCE9A-52DA-4771-A9CD-E5F788D214E6

P356

P1433

P1476

The effect of Fc glycan forms on human IgG2 antibody clearance in humans.

@en

P2093

Gregory C Flynn

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

Xiaoyu Chen

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

Y Diana Liu

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

P2860

Characterization of a cDNA encoding a novel human Golgi alpha 1, 2-mannosidase (IC) involved in N-glycan biosynthesis

Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases

Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys.

The mannose receptor and other macrophage lectins.

Human IgG2 antibodies display disulfide-mediated structural isoforms.

Glycosylation of recombinant antibody therapeutics.

Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1.

Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types.

Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients.

Structural and functional characterization of disulfide isoforms of the human IgG2 subclass.

P304

240-249

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

P31

scholarly article

P356

10.1093/GLYCOB/CWN120

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

P433

3

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

P478

19

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

P577

2008-10-30T00:00:00Z

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

P5875

23441773

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

P698

18974198

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

P921