Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization
about
Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological functionThe crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bipImproving biophysical properties of a bispecific antibody scaffold to aid developabilityDimerization of translationally controlled tumor protein is essential for its cytokine-like activityDynamics of inter-heavy chain interactions in human immunoglobulin G (IgG) subclasses studied by kinetic Fab arm exchange.A case study of 2,2-dimethylthiazolidine as locked cis proline amide bond: synthesis, NMR and molecular modeling studies of a delta-conotoxin EVIA peptide analog.Hierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase.The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner.Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing.Protein Folding Mechanism of the Dimeric AmphiphysinII/Bin1 N-BAR Domain.Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum.Engineered soluble monomeric IgG1 CH3 domain: generation, mechanisms of function, and implications for design of biological therapeutics.How antibodies foldWhat lessons can be learned from studying the folding of homologous proteins?Understanding the complex mechanisms of β2-microglobulin amyloid assembly.Proteins improving recombinant antibody production in mammalian cells.Following nature's roadmap: folding factors from plasma cells led to improvements in antibody secretion in S. cerevisiae.Molecular cloning and characterization of the α-chain gene of goose immunoglobulin heavy chain.Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain.An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.Recognition of E-cadherin by integrin alpha(E)beta(7): requirement for cadherin dimerization and implications for cadherin and integrin function.Cyclosporin A produces distal renal tubular acidosis by blocking peptidyl prolyl cis-trans isomerase activity of cyclophilin.Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase
P2860
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P2860
Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Folding and association of the ...... rization preceeds dimerization
@ast
Folding and association of the ...... rization preceeds dimerization
@en
Folding and association of the ...... rization preceeds dimerization
@nl
type
label
Folding and association of the ...... rization preceeds dimerization
@ast
Folding and association of the ...... rization preceeds dimerization
@en
Folding and association of the ...... rization preceeds dimerization
@nl
prefLabel
Folding and association of the ...... rization preceeds dimerization
@ast
Folding and association of the ...... rization preceeds dimerization
@en
Folding and association of the ...... rization preceeds dimerization
@nl
P2093
P3181
P356
P1476
Folding and association of the ...... rization preceeds dimerization
@en
P2093
P3181
P356
10.1006/JMBI.1999.3128
P407
P577
1999-10-15T00:00:00Z