Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A RasGTP-induced conformational change in C-RAF is essential for accurate molecular recognition.

Biophysical journal - 2 Sept 2009

Hibino Kayo, Shibata Tatsuo, Yanagida Toshio, Sako Yasushi

Abstract excerpt

The dysregulation of Ras-RAF signaling is associated with many types of human cancer. However, the kinetic and dynamic features of the mutual molecular recognition of Ras and RAF remain unknown. Here, we developed a technique for imaging single-pair fluorescence resonance energy transfer in living cells, and coupled this technique to single-molecule kinetic analysis to investigate how C-RAF (a subtype of RAF)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Epidermal Growth Factor
Share to Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to Intracellular Space

Share to Microscopy, Confocal

Share to Proto-Oncogene Proteins c-raf

Share to Video Recording

Source

Open in PubMed Open full text

Identifiers

PMID: 19720015
DOI: 10.1016/j.bpj.2009.05.048
PMCID: PMC3325157

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A RasGTP-induced conformational change in C-RAF is essential for accurate molecular recognition.PMID 19720015Read ↗

Activation kinetics of RAF protein in the ternary complex of RAF, RAS-GTP, and kinase on the plasma membrane of living cells: single-molecule imaging analysis.Semantic proximity Read ↗

Imaging activation of two Ras isoforms simultaneously in a single cell.Semantic proximity Read ↗

Dynamic polymorphism of Ras observed by single molecule FRET is the basis for molecular recognition.Semantic proximity Read ↗

Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase.Semantic proximity Read ↗

Inhibitors that stabilize a closed RAF kinase domain conformation induce dimerization.Semantic proximity Read ↗

Improved binding of raf to Ras.GDP is correlated with biological activity.Semantic proximity Read ↗

An improved Ras sensor for highly sensitive and quantitative FRET-FLIM imaging.Semantic proximity Read ↗

Mimicking transient activation of protein kinases in living cells.Semantic proximity Read ↗

What makes Ras an efficient molecular switch: a computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf.Semantic proximity Read ↗

In vivo monitoring of the recruitment and activation of AP-1 by Arf1.Semantic proximity Read ↗

Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells.Semantic proximity Read ↗

Structural determinants of Ras-Raf interaction analyzed in live cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.