The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Functional properties of phosphorylated elongation factor 2
Abstract
The effect of phosphorylation on the functional activity of eukaryotic elongation factor 2 (eEF‐2) was studied using a purified phosphorylated factor. The modified factor was unable to stimulate protein synthesis in an eEF‐2‐dependent rabbit reticulocyte lysate. The functional alteration was further analyzed by measuring the effects of phosphorylation on the ability of the factor to catalyse the ribosome‐dependent hydrolysis of GTP. Kinetic analysis showed that both phosphorylated and unmodified factor was able to hydrolyse GTP with approximately the same maximum rate, indicating that the rate of nucleotide exchange was not impaired by the modification. However, the phosphorylated factor showed a marked reduction in the second‐order rate constant, suggesting that the phosphorylation interfered with ribosome · eEF‐2 complex formation by reducing the affinity of eEF‐2 for the ribosome. This assumption was confirmed by direct measurements of the dissociation constants for the ribosomal complexes containing unmodified and phosphorylated eEF‐2.
Overview
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.
Integrity signals
Registry
Cites
Statistics
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
High resolution two-dimensional electrophoresis of proteins.
O'Farrell, P. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41496-8 · Cited by 19,246
An Efficient mRNA‐Dependent Translation System from Reticulocyte Lysates
PELHAM, H. R. B., & JACKSON, R. J. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10656.x · Cited by 3,926
Bolton, A. E., & Hunter, W. M. (1973) · Biochemical Journal · doi:10.1042/bj1330529 · Cited by 3,254
THE INHIBITION OF CHOLINESTERASE BY PHYSOSTIGMINE AND PROSTIGMINE
Eadie, G. S. (1942) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)72452-6 · Cited by 620
Moldave, K. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.005333 · Cited by 540
Non-Inverted Versus Inverted Plots in Enzyme Kinetics
Hofstee, B. H. J. (1959) · Nature · doi:10.1038/1841296b0 · Cited by 462
Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation
Ryazanov, A. G., Shestakova, E. A., & Natapov, P. G. (1988) · Nature · doi:10.1038/334170a0 · Cited by 454
Initiation of protein synthesis in mammalian cells
Pain, V. M. (1986) · Biochemical Journal · doi:10.1042/bj2350625 · Cited by 350
Nairn, A. C., & Palfrey, H. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45377-x · Cited by 339
Cited by
The mTOR pathway in the control of protein synthesis
Wang, X., & Proud, C. G. (2006) · Physiology · doi:10.1152/physiol.00024.2006 · Cited by 778
Signalling to translation: How signal transduction pathways control the protein synthetic machinery
Proud, C. G. (2007) · Biochemical Journal · doi:10.1042/bj20070024 · Cited by 520
Browne, G. J., Finn, S. G., & Proud, C. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309773200 · Cited by 353
Chan, A. Y. M., Soltys, C.-L. M., Young, M. E., Proud, C. G., & Dyck, J. R. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403528200 · Cited by 331
Role of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise
Jørgensen, S. B., Richter, E. A., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109942 · Cited by 261
Metadata
- Authors
- CARLBERG, U., NILSSON, A., & NYGÅRD, O.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1990-08
- Volume
- 191
- Issue
- 3
- Pages
- 639-645
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1968684991
- Cited by
- 276
- References
- 19
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Functional properties of phosphorylated elongation factor 2. https://app.cochat.ai/papers/10.1111/j.1432-1033.1990.tb19169.x
- The paper
- CARLBERG, U., NILSSON, A., & NYGÅRD, O. (1990). Functional properties of phosphorylated elongation factor 2. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1990.tb19169.x
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
