(Q27729940)

2

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P Holliger

3

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G Winter

4

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R L Williams

A comparison of strategies to stabilize immunoglobulin Fv-fragments

5

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publication date

15 December 1994

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published in

Structure

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volume

2

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page(s)

1217-26

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issue

12

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cites work

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Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli

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Single-chain antigen-binding proteins

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Human anti-self antibodies with high specificity from phage display libraries.

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"Diabodies": small bivalent and bispecific antibody fragments

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Crystallization of single-chain Fv proteins

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Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex.

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Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-A resolution

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Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate Adsorbent

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Canonical structures for the hypervariable regions of immunoglobulins

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Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex

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Crystal structure of a chimeric Fab' fragment of an antibody binding tumour cells

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Local and transmitted conformational changes on complexation of an anti-sweetener Fab

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Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint

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Domain association in immunoglobulin molecules. The packing of variable domains

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Structure of the human class I histocompatibility antigen, HLA-A2

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Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen

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Cloning immunoglobulin variable domains for expression by the polymerase chain reaction

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Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

3280639

3280639

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference