Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries.
about
The development and application of a quantitative peptide microarray based approach to protein interaction domain specificity spaceMUSI: an integrated system for identifying multiple specificity from very large peptide or nucleic acid data setsPDZ domains and their binding partners: structure, specificity, and modificationElucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domainsDirected Evolution Reveals the Binding Motif Preference of the LC8/DYNLL Hub Protein and Predicts Large Numbers of Novel Binders in the Human ProteomeStructural snapshots reveal distinct mechanisms of procaspase-3 and -7 activationIdentification of a Small Peptide That Inhibits PCSK9 Protein Binding to the Low Density Lipoprotein ReceptorSuperbinder SH2 domains act as antagonists of cell signalingAn allosteric switch for pro-HGF/Met signaling using zymogen activator peptidesBayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins.Motif mediated protein-protein interactions as drug targetsLarge-scale interaction profiling of PDZ domains through proteomic peptide-phage display using human and viral phage peptidomesThe multiple-specificity landscape of modular peptide recognition domainsProteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of synteninHigh-throughput analysis of peptide-binding modulesClustering of disulfide-rich peptides provides scaffolds for hit discovery by phage display: application to interleukin-23A graph kernel approach for alignment-free domain-peptide interaction prediction with an application to human SH3 domainsSH3 interactome conserves general function over specific form.Domain-mediated protein interaction prediction: From genome to network.Isolation of monobodies that bind specifically to the SH3 domain of the Fyn tyrosine protein kinase.Identification of specificity determining residues in peptide recognition domains using an information theoretic approach applied to large-scale binding mapsPotent and selective inhibition of pathogenic viruses by engineered ubiquitin variants.MOTIPS: automated motif analysis for predicting targets of modular protein domainsImprovements to the Kunkel mutagenesis protocol for constructing primary and secondary phage-display libraries.Identification of target ligands of CORYNE in Arabidopsis by phage display library.A specificity map for the PDZ domain familyPhage-displayed combinatorial peptide libraries in fusion to beta-lactamase as reporter for an accelerated clone screening: Potential uses of selected enzyme-linked affinity reagents in downstream applications.Anti-idiotypic monobodies derived from a fibronectin scaffold.Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1))A systematic approach to identify novel cancer drug targets using machine learning, inhibitor design and high-throughput screening.Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Anti-idiotypic monobodies for immune response profiling.Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7.Generating conformation-specific synthetic antibodies to trap proteins in selected functional statesQuantifying protein-protein interactions in high throughput using protein domain microarrays.Engineering an improved light-induced dimer (iLID) for controlling the localization and activity of signaling proteins.Characterizing WW domain interactions of tumor suppressor WWOX reveals its association with multiprotein networks.Turning on caspases with genetics and small moleculesWW domains of the yes-kinase-associated-protein (YAP) transcriptional regulator behave as independent units with different binding preferences for PPxY motif-containing ligands.Development and characterization of recombinant antibody fragments that recognize and neutralize in vitro Stx2 toxin from Shiga toxin-producing Escherichia coli.
P2860
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P2860
Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries.
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Identifying specificity profil ...... e-displayed peptide libraries.
@ast
Identifying specificity profil ...... e-displayed peptide libraries.
@en
type
label
Identifying specificity profil ...... e-displayed peptide libraries.
@ast
Identifying specificity profil ...... e-displayed peptide libraries.
@en
prefLabel
Identifying specificity profil ...... e-displayed peptide libraries.
@ast
Identifying specificity profil ...... e-displayed peptide libraries.
@en
P2093
P356
P1433
P1476
Identifying specificity profil ...... e-displayed peptide libraries.
@en
P2093
Charles Boone
Raffi Tonikian
Sachdev S Sidhu
Yingnan Zhang
P2888
P304
P356
10.1038/NPROT.2007.151
P577
2007-01-01T00:00:00Z
P5875
P6179
1009394762