Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain. - Wikidata - wikimedia - TriplyDB

Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain.

Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain.

http://www.wikidata.org/entity/Q41762336

about

Methods to Design and Synthesize Antibody-Drug Conjugates (ADCs)Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological function Structure of an isolated unglycosylated antibody CH2 domain Insulin analog with additional disulfide bond has increased stability and preserved activity Novel Covalently Linked Insulin Dimer Engineered to Investigate the Function of Insulin Dimerization Improving biophysical properties of a bispecific antibody scaffold to aid developability Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds Structural characterization of a recombinant fusion protein by instrumental analysis and molecular modeling Pathogenic Cysteine Removal Mutations in FGFR Extracellular Domains Stabilize Receptor Dimers and Perturb the TM Dimer Structure.Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing.Inhibition of Plasmodium berghei Development in Mosquitoes by Effector Proteins Secreted from Asaia sp. Bacteria Using a Novel Native Secretion Signal Formylbenzene diazonium hexafluorophosphate reagent for tyrosine-selective modification of proteins and the introduction of a bioorthogonal aldehyde.Post-translational structural modifications of immunoglobulin G and their effect on biological activity.Survival and digestibility of orally-administered immunoglobulin preparations containing IgG through the gastrointestinal tract in humans The road to the first, fully active and more stable human insulin variant with an additional disulfide bond.Production and characterization of a CD25-specific scFv-Fc antibody secreted from Pichia pastoris.A detergent-based procedure for the preparation of IgG-like bispecific antibodies in high yield.Increased aggregation propensity of IgG2 subclass over IgG1: role of conformational changes and covalent character in isolated aggregates.Effect of thanatophoric dysplasia type I mutations on FGFR3 dimerization.Material-Efficient Microfluidic Platform for Exploratory Studies of Visible-Light Photoredox Catalysis.Unraveling solvent-mediated reaction pathways leading to regiospecific mechanochemical cleavage of disulfide bonds in peptides.Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics.An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity.Assigning Peptide Disulfide Linkage Pattern Among Regio-Isomers via Methoxy Addition to Disulfide and Tandem Mass Spectrometry.Direct mass spectrometric characterization of disulfide linkages.Antibody-Drug Conjugates for Cancer Therapy: Chemistry to Clinical Implications.

P2860

Q26768654-0CF7218F-2EBD-49B5-9E2D-4A748A50966A Q26823047-22AC16F9-7824-44A8-80B1-F64B95BC0F73 Q27652565-8A0E0436-981F-4DEC-A8A3-39196C260F8C Q27675686-CE4EC96B-4258-408C-B07A-C6E18C80E4FD Q27677467-3B4ECED3-5FEC-4889-8FB1-82E060717838 Q27679445-4333454D-5D73-4392-BAEC-2A5EFCBC4450 Q28478914-EF144DEC-3F02-45C8-B3CC-2C9337FD28B0 Q28487616-13B2DE88-52D5-47E3-82AB-8F1440DD8E3E Q33810258-799EC551-A3C1-4196-854C-E6FF2A291AFB Q34357104-2E403BAB-F328-46BD-8AA9-4833DBBA4269 Q35860846-99BED7DA-9358-4686-BE4F-AC3225927513 Q36478887-CD3F18A2-EEF8-443E-843F-8B6D146EDB2E Q38246996-CA8FDC9C-343A-4E85-9D14-1452A3AB36CD Q38423920-0DB93F90-C0AC-4B74-91AE-FA0034FCC2E3 Q38561423-7D142239-9709-423F-B379-4517344B6EC8 Q39224359-C1B6BFEF-837D-4F8B-B049-9B131775C384 Q42351565-6F3D298C-A0E7-4505-94D4-315D34552B65 Q42378916-96486FBB-D2CA-42CB-A6D4-CC2B2C3964AC Q42554214-E0FC01F6-EF57-41E8-A0F2-4443406CAE58 Q44873460-2D18B978-9216-462B-ACB8-7A3C223CFD6C Q47374112-AD73AF6D-EFFF-4E33-BD3E-6EF572BC791B Q47548498-0DB5CD2B-C8F0-42DD-8676-9E3EE5E4CF00 Q50079312-F5AAF1CD-78BA-472B-9695-1C69A41E96BD Q51138760-504A9312-9A02-4CDA-B93D-EBF3999EC3FA Q51749053-542EDFA5-187E-45FE-965E-91B558C79AFD Q52593621-DAFB4148-9623-477C-BEFF-ADCFC1A88ABC

P2860

Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain.

http://www.wikidata.org/entity/Q41762336

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Contributions of a disulfide b ...... uman IgG1 antibody CH3 domain.

@en

type

label

Contributions of a disulfide b ...... uman IgG1 antibody CH3 domain.

@en

prefLabel

Contributions of a disulfide b ...... uman IgG1 antibody CH3 domain.

@en

P1433

Q41762336-5899C85C-33D6-41DE-8D10-E9E79D533D6F

P1476

Q41762336-D257FCB4-CF97-43D0-9DFB-95972B98E385

P2093

Q41762336-06FA1227-014E-4CE2-AE5C-AF66F3094DAE

Q41762336-1A36A3DC-796F-4251-A4AD-FAD2D94A1AF0

Q41762336-2DC8720F-BE13-4C78-8184-96F23B247969

Q41762336-4184E1E1-46A3-4A31-A5FA-B00CA8C61A01

Q41762336-65DE8CD8-C7B6-49B8-8362-1C7489E54CE8

Q41762336-6CCE15F4-6217-4096-AD01-46A9B76C8CE8

Q41762336-798F0F80-4EE8-4BD3-86A5-D1A5B743EA17

Q41762336-7E47053C-AFE2-4EE7-9BF1-CA25AF42698F

Q41762336-CA42CADF-46B1-4381-9ED8-E52DD894C462

Q41762336-ED5214B0-3D82-4EE9-BD2C-EF95982CC43C

P2860

Q41762336-02200DD8-7A8A-4F5F-8C4C-D6F1B69966A7

Q41762336-0CB220F3-F63F-473A-859A-7A02A8158CAA

Q41762336-10CD4EB9-DAE9-46FC-8258-9D07FBDAA987

Q41762336-12972FCA-C7D0-42ED-8F8B-633034452EAC

Q41762336-19A6A5BA-1AF6-484B-8C67-DA7F7D94167D

Q41762336-221B0C83-435C-4A0B-BD9E-C0A59AA1F955

Q41762336-231B59A4-E532-48FC-A5D2-DDFE0FD51B0B

Q41762336-26A8F75C-68BC-40E2-A642-05C62BE9B8E1

Q41762336-279BCDB6-96FA-4F0A-AE73-747398F1656B

Q41762336-4013FC5B-9F67-4A80-A41A-8BCB0DE5E1BB

P304

Q41762336-B8320BA3-6886-4A13-8843-F51CFF18BAEC

P31

Q41762336-F9288B50-D24D-4B95-BEC9-64F8B31AFF42

P356

Q41762336-8F933A1A-A6D9-4B64-B386-E0DC714FF1E6

P433

Q41762336-9ACE5E1B-AB34-419B-AEC5-22B1D98F67A8

P478

Q41762336-8EAA33B3-7BBC-4D44-AADF-ABEA349F7C70

P577

Q41762336-50D8F469-0687-411D-AEA0-2CBDF50A83F1

P5875

Q41762336-003E0779-62E9-4EE5-9577-DA4D8AD07C13

P698

Q41762336-7839DB30-1890-4BCE-B85F-25FFA3192CCE

P932

Q41762336-87969D50-F65B-4CA8-B07E-B452B3AC9E3C

P356

P1433

Protein Science

P1476

Contributions of a disulfide b ...... uman IgG1 antibody CH3 domain.

@en

P2093

Arnold McAuley

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

Carl G Kolvenbach

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

David N Brems

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

Douglas Rehder

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

Gerd R Kleemann

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

Hyo Jin Lee

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

Jaby Jacob

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

Kimberly Westland

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

Masazumi Matsumura

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

Stephen R Brych

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

P2860

Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization

Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design

Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution

How to measure and predict the molar absorption coefficient of a protein

Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds

Folding mechanism of the CH2 antibody domain.

The three-dimensional structure of an intact monoclonal antibody for canine lymphoma.

Reexamination of the folding of BPTI: predominance of native intermediates.

Optimization and applications of CDAP labeling for the assignment of cysteines.

Antibody engineering via genetic engineering of the mouse: XenoMouse strains are a vehicle for the facile generation of therapeutic human monoclonal antibodies.

P304

95-106

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

P31

scholarly article

P356

10.1110/PS.073134408

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

P433

1

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

P478

17

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

P577

2008-01-01T00:00:00Z

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

P5875

5693693

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

P698

18156469

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

P932

2144599

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