about
De novo designed cyclic-peptide heme complexesMolecular markers of serine protease evolutionN-terminal protein modification using simple aminoacyl transferase substratesSelection of catalytically active biotin ligase and trypsin mutants by phage display.Investigating and Engineering Enzymes by Genetic Selection.Generation of a broad esterolytic subtilisin using combined molecular evolution and periplasmic expression.A novel strategy for the functional cloning of enzymes using filamentous phage display: the case of nucleotidyl transferases.Function-based isolation of novel enzymes from a large library.Substrate turnover and inhibitor binding as selection parameters in directed evolution of blood coagulation factor Xa.Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization.Selection of an active enzyme by phage display on the basis of the enzyme's catalytic activity in vivo.Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection.Phage display in molecular imaging and diagnosis of cancer.Parallel in vivo and in vitro selection using phage display identifies protease-dependent tumor-targeting peptides.Sampling the N-terminal proteome of human blood.Inflammatory stimuli regulate caspase substrate profiles.Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.IBC's 22nd Annual Antibody Engineering and 9th Annual Antibody Therapeutics International Conferences and the 2011 Annual Meeting of The Antibody Society, December 5-8, 2011, San Diego, CA.An enigmatic peptide ligation reaction: protease-catalyzed oligomerization of a native protein segment in neat aqueous solution.Selection strategies for improved biocatalysts.Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.Phage-Enabled Nanomedicine: From Probes to Therapeutics in Precision MedicineBioinformatic approaches for predicting substrates of proteases.Ab initio folding of terminal segments with secondary structures reveals the fine difference between two closely related all-atom statistical energy functionsEnzyme-catalyzed substrate attachment to phage surfaces for the selection of catalytic activities.Improved Enantioselectivity of Subtilisin Carlsberg towards Secondary Alcohols by Protein Engineering.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Selection for improved subtiligases by phage display.
@ast
Selection for improved subtiligases by phage display.
@en
type
label
Selection for improved subtiligases by phage display.
@ast
Selection for improved subtiligases by phage display.
@en
prefLabel
Selection for improved subtiligases by phage display.
@ast
Selection for improved subtiligases by phage display.
@en
P2860
P356
P1476
Selection for improved subtiligases by phage display.
@en
P2093
P2860
P304
P356
10.1073/PNAS.96.17.9497
P407
P577
1999-08-01T00:00:00Z