Cited by 70Protein Kinase Regulation and GTPase SignalingAdvanced NMR Techniques and ApplicationsProtein Structure and Dynamics

Perturbation of the conformational equilibria in Ras by selective mutations as studied by 31P NMR spectroscopy

Open access
Spoerner, Michael, Wittinghofer, Alfred, Kalbitzer, Hans Robert·2004·FEBS Letters

Abstract

Ras regulates a variety of different signal transduction pathways acting as molecular switch. It was shown by liquid and solid‐state 31 P NMR spectroscopy that Ras exists in the guanosine‐5′‐(β,γ‐imido)triphosphate bound form in at least two conformational states interconverting in millisecond time scale. The relative population between the two conformational states affects drastically the affinity of Ras to its effectors. 31 P NMR spectroscopy shows that the conformational equilibrium can be shifted specifically by point mutations, including mutations with oncogenic potential, thus modifying the effector interactions and their coupling to dynamic properties of the protein.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.febslet.2004.11.020

Cites

20 of 20 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Spoerner, M., Wittinghofer, A., & Kalbitzer, H. R.
Affiliations
  • University of Regensburg (DE)
  • Max Planck Institute of Molecular Physiology (DE)
Corresponding author
Kalbitzer, Hans Robert
Venue
FEBS Letters
Publisher
Wiley
Published
2004-11-23
Volume
578
Issue
3
Pages
305-310
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2018019331
Cited by
70
References
20
Citations by year
2026: 1 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 5 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 4
FWCI
1.07
Type
journal article
Language
en
Open access
Locations
  • FEBS Letters (publishedVersion)
  • PubMed (publishedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
Deutsche Forschungsgemeinschaft (GRK760)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
Ras, conformational equilibrium, point mutations, oncogenic mutations, GTP, GTP-bound state, effector binding, signal transduction, protein dynamics, 31P NMR
MeSH terms
Amino Acid Sequence, Escherichia coli, Guanosine Diphosphate, Humans, Hydrogen-Ion Concentration, Kinetics, Models, Molecular, Phosphorus, Phosphorus Isotopes, Protein Binding, Protein Conformation, Genes, ras, Temperature, Threonine, Genetic Variation, Signal Transduction, Point Mutation, Protein Structure, Tertiary, ras Proteins, Nuclear Magnetic Resonance, Biomolecular, Amino Acid Substitution, GTPase-Activating Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review