Protein-protein interactions monitored in mammalian cells via complementation of beta -lactamase enzyme fragments. - Wikidata - wikimedia - TriplyDB

Protein-protein interactions monitored in mammalian cells via complementation of beta -lactamase enzyme fragments.

Protein-protein interactions monitored in mammalian cells via complementation of beta -lactamase enzyme fragments.

http://www.wikidata.org/entity/Q34018553

about

Detection and characterization of protein interactions in vivo by a simple live-cell imaging method Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization Using the beta-lactamase protein-fragment complementation assay to probe dynamic protein-protein interactions The use of proteomics to identify novel therapeutic targets for the treatment of disease.Time-lapse imaging of a dynamic phosphorylation-dependent protein-protein interaction in mammalian cells Myoblasts and macrophages share molecular components that contribute to cell-cell fusion Bimolecular fluorescence complementation analysis of inducible protein interactions: effects of factors affecting protein folding on fluorescent protein fragment association.Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies. African trypanosomes as paradigm.Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.Molecular imaging of phosphorylation events for drug development Random dissection to select for protein split sites and its application in protein fragment complementation Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.Expanding the utility of beta-galactosidase complementation: piece by piece.A high-throughput screening system for G-protein-coupled receptors using β-lactamase enzyme complementation technology Protein 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.Dual-color click beetle luciferase heteroprotein fragment complementation assays.Modular extracellular sensor architecture for engineering mammalian cell-based devices.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation.Therapeutic Targeting of Myc.Imaging Tetrahymena ribozyme splicing activity in single live mammalian cells.Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies.Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions.Reporter gene imaging of protein-protein interactions in living subjects Combinatorial library screening for developing an improved split-firefly luciferase fragment-assisted complementation system for studying protein-protein interactions.Monitoring β-arrestin recruitment via β-lactamase enzyme fragment complementation: purification of peptide E as a low-affinity ligand for mammalian bombesin receptors.Molecular imaging with activatable reporter systems Assays of vacuole fusion resolve the stages of docking, lipid mixing, and content mixing Quantification of dynamic protein complexes using Renilla luciferase fragment complementation applied to protein kinase A activities in vivo.In silico protein fragmentation reveals the importance of critical nuclei on domain reassembly.Protein complementation assays: approaches for the in vivo analysis of protein interactions.Mammalian two-hybrids come of age.Biomolecular engineering of intracellular switches in eukaryotes Recent developments of biological reporter technology for detecting gene expression.Embryonic stem cell interactomics: the beginning of a long road to biological function.Bimolecular fluorescence complementation: visualization of molecular interactions in living cells.Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay.

P2860

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P2860

Protein-protein interactions monitored in mammalian cells via complementation of beta -lactamase enzyme fragments.

http://www.wikidata.org/entity/Q34018553

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Protein-protein interactions m ...... a -lactamase enzyme fragments.

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Protein-protein interactions m ...... a -lactamase enzyme fragments.

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Protein-protein interactions m ...... a -lactamase enzyme fragments.

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Protein-protein interactions m ...... a -lactamase enzyme fragments.

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Protein-protein interactions m ...... a -lactamase enzyme fragments.

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Protein-protein interactions m ...... a -lactamase enzyme fragments.

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Protein-protein interactions m ...... a -lactamase enzyme fragments.

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P1433

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Protein-protein interactions m ...... a -lactamase enzyme fragments.

@en

P2093

Benjamin Kleaveland

http://www.w3.org/2001/XMLSchema#string

Helen M Blau

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Jeng-Horng Her

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Robert F Balint

http://www.w3.org/2001/XMLSchema#string

Tom Wehrman

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P2860

Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins

Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution

Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP

A novel genetic system to detect protein-protein interactions

A mammalian protein targeted by G1-arresting rapamycin-receptor complex

Monitoring protein-protein interactions in intact eukaryotic cells by beta-galactosidase complementation

Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue

Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers

AP-1 function and regulation

Interaction blues: protein interactions monitored in live mammalian cells by beta-galactosidase complementation.

P304

3469-3474

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P31

scholarly article

P356

10.1073/PNAS.062043699

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P407

P433

6

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P478

99

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P577

2002-03-01T00:00:00Z

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11460450

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P698

11904411

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P932

122547

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