ArticleThe Journal of biological chemistry1992
Expression of the GTPase activating domain of the neurofibromatosis type 1 (NF1) gene in Escherichia coli and role of the conserved lysine residue.
Article in The Journal of biological chemistry, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 55 citations in OpenAlex.
- ARAF protein kinase activates RAS by antagonizing its binding to RASGAP NF1.Molecular cell · 2022Article
- Computational insights of K1444N substitution in GAP-related domain of NF1 gene associated with neurofibromatosis type 1 disease: a molecular modeling and dynamics approach.Metabolic brain disease · 2018Article
- Article
- Transition state structures and the roles of catalytic residues in GAP-facilitated GTPase of Ras as elucidated by (18)O kinetic isotope effects.Biochemistry · 2009Article
- Oncogenic insertional mutations in the P-loop of Ras are overactive in MAP kinase signaling.Oncogene · 2000Article
- Structural analysis of the GAP-related domain from neurofibromin and its implications.The EMBO journal · 1998Article
- RanGAP1 induces GTPase activity of nuclear Ras-related Ran.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Functional significance of lysine 1423 of neurofibromin and characterization of a second site suppressor which rescues mutations at this residue and suppresses RAS2Val-19-activated phenotypes.Molecular and cellular biology · 1994Article
- Suppression of oncogenic Ras by mutant neurofibromatosis type 1 genes with single amino acid substitutions.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Differential regulation of cellular activities by GTPase-activating protein and NF1.Molecular and cellular biology · 1993Article
Corrections and comments
- Comment on
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A small catalytic domain from the neurofibromatosis type 1 gene, NF1-333, consisting of 333 amino acids between residues 1197 and 1528, including an additional N-terminal methionine, was expressed in Escherichia coli as a soluble protein. Its catalytic activity under non-saturating conditions is similar to the full-length p120-GAP but different from truncated GAP-334. Under saturating conditions its kcat and KM are lower. Lys-1422, which is totally conserved in all GAP proteins, was mutated and the properties of the mutant protein investigated. Lys-1422 seems to be essential for the stability of the proteins and not for its catalytic activity.
Indexed as
Identifiers
1587809W1608400430What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.