The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
The neurofibromatosis type 1 gene encodes a protein related to GAP
Abstract
cDNA walking and sequencing have extended the open reading frame for the neurofibromatosis type 1 gene (NF1). The new sequence now predicts 2485 amino acids of the NF1 peptide. A 360 residue region of the new peptide shows significant similarity to the known catalytic domains of both human and bovine GAP (GTPase activating protein). A much broader region, centered around this same 360 amino acid sequence, is strikingly similar to the yeast IRA1 product, which has a similar amino acid sequence and functional homology to mammalian GAP. This evidence suggests that NF1 encodes a cytoplasmic GAP-like protein that may be involved in the control of cell growth by interacting with proteins such as the RAS gene product. Mapping of the cDNA clones has confirmed that NF1 spans a t(1;17) translocation mutation and that three active genes lie within an intron of NF1, but in opposite orientation.
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“KRAS proteins primarily bind to guanosine diphosphate (GDP) and are in an inactive conformation maintained by intrinsic guanosine triphosphate (GTP) hydrolytic activity.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [9]
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Oncogenes and signal transduction
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Metadata
- Authors
- Xu, G., O'Connell, P., Viskochil, D., Cawthon, R., Robertson, M., Culver, M., Dunn, D., Stevens, J., Gesteland, R., White, R., & Weiss, R.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Utah (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1990-08
- Volume
- 62
- Issue
- 3
- Pages
- 599-608
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2159096148
- Cited by
- 1,095
- References
- 42
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 19 · 2023: 19 · 2022: 22 · 2021: 22 · 2020: 22 · 2019: 18 · 2018: 22 · 2017: 17 · 2016: 19 · 2015: 21 · 2014: 24 · 2013: 24 · 2012: 45
- FWCI
- 70.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Energy
- Topics
- Health Sciences › Medicine › Clinical Neurology › Neurofibromatosis and Schwannoma Cases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- neurofibromatosis type 1, NF1 gene, GTPase-activating protein, Ras, open reading frames, cDNA cloning, cell growth regulation, protein homology
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cattle, Chromosomes, Human, Pair 1, Chromosomes, Human, Pair 17, Cloning, Molecular, Genes, Humans, Information Systems, Molecular Sequence Data, Neurofibromatosis 1, Proteins, Sequence Homology, Nucleic Acid, Translocation, Genetic, Oligonucleotide Probes, Gene Library, Polymerase Chain Reaction, GTPase-Activating Proteins, ras GTPase-Activating Proteins, Neurofibromin 1
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