Structural Basis for Exquisite Specificity of Affinity Clamps, Synthetic Binding Proteins Generated through Directed Domain-interface Evolution
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Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesinSuperglue from bacteria: unbreakable bridges for protein nanotechnologyIsolation of monobodies that bind specifically to the SH3 domain of the Fyn tyrosine protein kinase.Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules.A peptide tag system for facile purification and single-molecule immobilizationMonobodies and other synthetic binding proteins for expanding protein scienceRational conversion of affinity reagents into label-free sensors for Peptide motifs by designed allosteryTULIPs: tunable, light-controlled interacting protein tags for cell biology.Protease-based synthetic sensing and signal amplification.Thermodynamic basis for engineering high-affinity, high-specificity binding-induced DNA clamp nanoswitches.Designed hydrophilic and charge mutations of the fibronectin domain: towards tailored protein biodistribution.Generation of high-performance binding proteins for peptide motifs by affinity clampingSpyLigase peptide-peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture.How to Train a Cell-Cutting-Edge Molecular Tools.Converting a protein into a switch for biosensing and functional regulation.Engineering protein switches: sensors, regulators, and spare parts for biology and biotechnology.Phage Display Engineered T Cell Receptors as Tools for the Study of Tumor Peptide-MHC Interactions.Synthetic Protein Switches: Theoretical and Experimental Considerations.Survey of the 2009 commercial optical biosensor literature.Engineering and Characterizing Synthetic Protease Sensors and Switches.Blueprints for Biosensors: Design, Limitations, and Applications
P2860
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P2860
Structural Basis for Exquisite Specificity of Affinity Clamps, Synthetic Binding Proteins Generated through Directed Domain-interface Evolution
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@ast
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@en
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@nl
type
label
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@ast
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@en
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@nl
prefLabel
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@ast
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@en
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@nl
P2093
P2860
P1476
Structural Basis for Exquisite ...... ted Domain-interface Evolution
@en
P2093
Akiko Koide
Koki Makabe
P2860
P304
P356
10.1016/J.JMB.2009.07.067
P407
P577
2009-10-09T00:00:00Z