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Design of protein function leaps by directed domain interface evolution

লেখক

Shohei Koide

এতে প্রকাশিত: Proceedings of the National Academy of Sciences of the United States of America

তারিখে প্রকাশিত: 2008-05-06

ভাষা: ইংরেজি ভাষা

মূল বিষয়: protein design, protein evolution

Cites articles 42

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শিরোনাম

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High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries

Shohei Koide
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High-affinity single-domain binding proteins with a binary-code interface

Valentina Tereshko, Shohei Koide
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Engineering by homologous recombination: exploring sequence and function within a conserved fold

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The generation of new protein functions by the combination of domains

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Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain

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The design of evolution and the evolution of design

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Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display

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Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies

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A focused antibody library for improved hapten recognition

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Conformation-specific affinity purification of proteins using engineered binding proteins: application to the estrogen receptor

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The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF

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নিবন্ধ - wd:Q27650480

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