Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments.
about
Circular permutation and receptor insertion within green fluorescent proteinsVisualization of biochemical networks in living cellsA bacterial two-hybrid selection system for studying protein-DNA and protein-protein interactionsNovel mobilizable prokaryotic two-hybrid system vectors for high-throughput protein interaction mapping in Escherichia coli by bacterial conjugationLuciferase fragment complementation imaging in preclinical cancer studiesSplit-cre complementation indicates coincident activity of different genes in vivoDissecting virulence pathways of Mycobacterium tuberculosis through protein-protein association.Cell-Based Assay Design for High-Content Screening of Drug CandidatesUsing the beta-lactamase protein-fragment complementation assay to probe dynamic protein-protein interactionsSplit-superpositive GFP reassembly is a fast, efficient, and robust method for detecting protein-protein interactions in vivoTesting the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded formsThree Mycobacterium tuberculosis Rel toxin-antitoxin modules inhibit mycobacterial growth and are expressed in infected human macrophagesEffects of Non-Natural Amino Acid Incorporation into the Enzyme Core Region on Enzyme Structure and Function.Design and semisynthesis of photoactivable split-GFP by incorporation of photocleavable functionality.Combinatorial protein engineering by incremental truncationHigh-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancementGenome-wide protein interaction maps using two-hybrid systems.A coiled-coil enabled split-luciferase three-hybrid system: applied toward profiling inhibitors of protein kinases.Defining interacting partners for drug discovery.Amino-terminal protein fusions to the TraR quorum-sensing transcription factor enhance protein stability and autoinducer-independent activityCombinatorial approaches to novel proteins.Massive sequence perturbation of a small protein.Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening.Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells.Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control.Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitutionRandom dissection to select for protein split sites and its application in protein fragment complementationVersatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanismRapid modification of proteins using a rapamycin-inducible tobacco etch virus protease systemElectrostatic contacts in the activator protein-1 coiled coil enhance stability predominantly by decreasing the unfolding rate.Affinity maturation of a TNFalpha-binding affibody molecule by Darwinian survival selection.Bimolecular fluorescence complementation: lighting up seven transmembrane domain receptor signalling networksProtein fragment bimolecular fluorescence complementation analyses for the in vivo study of protein-protein interactions and cellular protein complex localizations.Kinetics and reaction coordinates of the reassembly of protein fragments via forward flux sampling.Truncation, randomization, and selection: generation of a reduced length c-Jun antagonist that retains high interaction stabilityIsolation of receptor-ligand pairs by capture of long-lived multivalent interaction complexesSplit-protein systems: beyond binary protein-protein interactionsA general approach for receptor and antibody-targeted detection of native proteins utilizing split-luciferase reassembly.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.
P2860
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P2860
Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Oligomerization domain-directe ...... rationally designed fragments.
@ast
Oligomerization domain-directe ...... rationally designed fragments.
@en
type
label
Oligomerization domain-directe ...... rationally designed fragments.
@ast
Oligomerization domain-directe ...... rationally designed fragments.
@en
prefLabel
Oligomerization domain-directe ...... rationally designed fragments.
@ast
Oligomerization domain-directe ...... rationally designed fragments.
@en
P2860
P356
P1476
Oligomerization domain-directe ...... rationally designed fragments
@en
P2093
J N Pelletier
S W Michnick
P2860
P304
12141-12146
P356
10.1073/PNAS.95.21.12141
P407
P577
1998-10-01T00:00:00Z