Search Results - "Padlan, E A"
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1
Anatomy of the antibody molecule
Published in Molecular immunology (01-02-1994)“…The structures of the various regions of an antibody molecule are analysed and correlated with biological function. The structural features which relate to…”
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Structure of an Antibody-Antigen Complex: Crystal Structure of the HyHEL-10 Fab-Lysozyme Complex
Published in Proceedings of the National Academy of Sciences - PNAS (01-08-1989)“…The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 angstrom…”
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Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
Published in The Journal of biological chemistry (25-11-1988)“…The three-dimensional structure of the alpha 2 beta 2 complex of tryptophan synthase from Salmonella typhimurium has been determined by x-ray crystallography…”
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Three-Dimensional Structure of an Antibody--Antigen Complex
Published in Proceedings of the National Academy of Sciences - PNAS (01-11-1987)“…We have determined the three-dimensional structure of two crystal forms of an antilysozyme Fab-lysozyme complex by x-ray crystallography. The epitope on…”
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On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands
Published in Proteins, structure, function, and bioinformatics (1990)“…A detailed analysis of the structural aspects of antibody-antigen interactions has been made possible by the availability of X-ray structures for three…”
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Antibody-antigen complexes
Published in The Journal of biological chemistry (05-08-1988)“…A minireview is presented…”
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Binding of a Reduced Peptide Inhibitor to the Aspartic Proteinase from Rhizopus chinensis: Implications for a Mechanism of Action
Published in Proceedings of the National Academy of Sciences - PNAS (01-10-1987)“…A peptide inhibitor, having the sequence D-His-Pro-Phe-His-PheΨ [CH2-NH]Phe-Val-Tyr, with a reduced bond between the two adjacent phenylalanines, has been…”
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Conformations of immunoglobulin hypervariable regions
Published in Nature (London) (21-12-1989)“…On the basis of comparative studies of known antibody structures and sequences it has been argued that there is a small repertoire of main-chain conformations…”
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Peptide blocking of IgE/receptor interaction: possibilities and pitfalls
Published in Allergy (Copenhagen) (01-12-1997)“…The central role of IgE antibodies in immediate hypersensitivity responses has been extensively documented since their identification as the mediator of the…”
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The codon for the methionine at position 129 (M129) in the human prion protein provides an alternative initiation site for translation and renders individuals homozygous for M129 more susceptible to prion disease
Published in Medical hypotheses (2005)“…Single amino-acid substitutions in the prion protein have been found to lead to resistance or susceptibility to amyloid fibril formation. In humans, the…”
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A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties
Published in Molecular immunology (01-04-1991)“…It is proposed to reduce the immunogenicity of allogeneic antibody variable domains, while preserving ligand-binding properties, by reducing their antigenicity…”
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Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
Published in Journal of molecular biology (20-08-1986)“…The crystal structure of the Fab of McPC603, a phosphocholine-binding mouse myeloma protein, has been refined at 2.7 A resolution by a combination of…”
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Why don’t humans get scrapie from eating sheep? A possible explanation based on secondary structure predictions
Published in Medical hypotheses (2005)“…In an effort to find a structural explanation for the lack of direct transmission of scrapie from sheep to humans, secondary structure predictions are used to…”
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14
Model-Building Study of the Combining Sites of Two Antibodies to α (1→ 6)dextran
Published in Proceedings of the National Academy of Sciences - PNAS (01-09-1988)“…Models of the Fv portion (containing the variable regions of the heavy and light chains) of two monoclonal anti-α (1→ 6)dextran antibodies, W3129 and 19.1.2,…”
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Are humans getting ‘mad-cow disease’ from eating beef, or something else?
Published in Medical hypotheses (01-05-2003)“…Bovine spongiform encephalopathy (BSE) or ‘mad-cow disease’ is believed to have been caused by the consumption of scrapie-infected sheep matter that had been…”
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Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal
Published in The Journal of biological chemistry (15-07-1985)“…The refined crystal structure of deoxyhemoglobin S (Padlan, E. A., and Love, W. E. (1985) J. Biol. Chem. 260, 8272-8279) was used to analyze in detail the…”
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A humanized form of a CD4-specific monoclonal antibody exhibits decreased antigenicity and prolonged plasma half-life in rhesus monkeys while retaining its unique biological and antiviral properties
Published in AIDS research and human retroviruses (20-07-1997)“…Certain monoclonal antibodies (MAbs) directed against CD4 can efficiently block HIV-1 replication in vitro. To explore CD4-directed passive immunotherapy for…”
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Development of a minimally immunogenic variant of humanized anti-carcinoma monoclonal antibody CC49
Published in Critical reviews in oncology/hematology (01-04-2001)“…Monoclonal antibody (MAb) CC49 reacts with a pancarcinoma antigen, tumor associated glycoprotein (TAG)-72. To circumvent human anti-murine antibody (HAMA)…”
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Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution
Published in The Journal of biological chemistry (15-07-1985)“…The crystal structure of deoxyhemoglobin S has been refined at 3.0-A resolution using the Hendrickson-Konnert restrained least-squares method. Comparison with…”
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Antibody-Antigen Complexes
Published in Annual review of biochemistry (1990)“…Antibodies are made in all vertebrates as part of the immune response to antigenic challenge by foreign substances. The diversity of this response is…”
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