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Diverse structural solutions to catalysis in a family of antibodies
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scholarly article
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title
Diverse structural solutions to catalysis in a family of antibodies
(English)
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author name string
B Gigant
series ordinal
1
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T Tsumuraya
series ordinal
2
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I Fujii
series ordinal
3
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M Knossow
series ordinal
4
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language of work or name
English
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based on heuristic
inferred from title
publication date
15 November 1999
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published in
Structure
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volume
7
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issue
11
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page(s)
1385-93
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cites work
Nature of Forces between Large Molecules of Biological Interest*
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Catalytic antibodies
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Selective chemical catalysis by an antibody
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Catalytic antibodies--reaching adolescence?
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Immune versus natural selection: antibody aldolases with enzymic rates but broader scope
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Catalytic antibodies
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Site-directed mutagenesis of a catalytic antibody: an arginine and a histidine residue play key roles
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inferred from DOI database lookup
Generation of a catalytic antibody by site-directed mutagenesis
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Creation of a ribonuclease abzyme through site-directed mutagenesis
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Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
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26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity
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Structure and specificity of the anti-digoxin antibody 40-50
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Analysis of hapten binding and catalytic determinants in a family of catalytic antibodies
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7 January 2021
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Mechanistically different catalytic antibodies obtained from immunization with a single transition-state analog
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Isoabzymes: structurally and mechanistically similar catalytic antibodies from the same immunization
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Structural convergence in the active sites of a family of catalytic antibodies
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A comparison of the crystallographic structures of two catalytic antibodies with esterase activity
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Correlation between Antigen-Combining-Site Structures and Functions within a Panel of Catalytic Antibodies Generated against a Single Transition State Analog
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A common ancestry for multiple catalytic antibodies generated against a single transition-state analog.
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A structural basis for transition-state stabilization in antibody-catalyzed hydrolysis: crystal structures of an abzyme at 1. 8 A resolution.
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Antibody-antigen interactions: new structures and new conformational changes
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Similarities of hydrolytic antibodies revealed by their X-ray structures: a review.
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Conformations of the third hypervariable region in the VH domain of immunoglobulins.
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Crossreactivity, efficiency and catalytic specificity of an esterase-like antibody
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Hydrolytic antibodies: variations on a theme
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Site-directed mutagenesis of active site contact residues in a hydrolytic abzyme: evidence for an essential histidine involved in transition state stabilization
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Mechanistic studies of a tyrosine-dependent catalytic antibody
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Prodrug activation via catalytic antibodies
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Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1
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The Protein Data Bank: a computer-based archival file for macromolecular structures
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Basic local alignment search tool
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Improved methods for building protein models in electron density maps and the location of errors in these models
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
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Checking your imagination: applications of the free R value
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PROCHECK: a program to check the stereochemical quality of protein structures
1 reference
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Standard conformations for the canonical structures of immunoglobulins
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Environment and exposure to solvent of protein atoms. Lysozyme and insulin
1 reference
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catELISA: a facile general route to catalytic antibodies
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7 January 2021
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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The CCP4 suite: programs for protein crystallography
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Identifiers
DOI
10.1016/S0969-2126(00)80028-3
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4540884
OpenCitations bibliographic resource ID
4540884
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4540884
PubMed ID
10574796
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4540884
ResearchGate publication ID
12726042
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