scholarly journals Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma virus encodes for a transmembrane receptorlike molecule.

1986 ◽  
Vol 6 (8) ◽  
pp. 3000-3004 ◽  
Author(s):  
H Matsushime ◽  
L H Wang ◽  
M Shibuya
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Transmembrane Domain ◽  
Human Gene ◽  
Kinase Domain ◽  
Glycosylation Site ◽  
Tyrosine Kinase Domain ◽  
Base Pairs ◽  
Human Insulin Receptor ◽  
Sarcoma Virus

We isolated a human gene (designated c-ros-1) homologous to the v-ros sequence of UR2 sarcoma virus. Ten exons, 1,414 base pairs spanning 26 kilobases, contained a tyrosine kinase domain, a transmembrane domain, and a part of an extracellular domain carrying an N glycosylation site which was not acquired by UR2 sarcoma virus. The predicted structure of c-ros-1 is unique among the src family and clearly distinct from the human insulin receptor.

Human c-ros-1 gene homologous to the v-ros sequence of UR2 sarcoma virus encodes for a transmembrane receptorlike molecule

1986 ◽  
Vol 6 (8) ◽  
pp. 3000-3004
Author(s):  
H Matsushime ◽  
L H Wang ◽  
M Shibuya
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Transmembrane Domain ◽  
Human Gene ◽  
Kinase Domain ◽  
Glycosylation Site ◽  
Tyrosine Kinase Domain ◽  
Base Pairs ◽  
Human Insulin Receptor ◽  
Sarcoma Virus

We isolated a human gene (designated c-ros-1) homologous to the v-ros sequence of UR2 sarcoma virus. Ten exons, 1,414 base pairs spanning 26 kilobases, contained a tyrosine kinase domain, a transmembrane domain, and a part of an extracellular domain carrying an N glycosylation site which was not acquired by UR2 sarcoma virus. The predicted structure of c-ros-1 is unique among the src family and clearly distinct from the human insulin receptor.

N.m.r. structural studies on the tyrosine kinase domain of the human insulin receptor

1989 ◽  
Vol 17 (5) ◽  
pp. 899-899
Author(s):  
ROBERT A. ATKINSON ◽  
WAYNE J. FAIRBROTHER ◽  
BARRY A. LEVINE ◽  
JEREMY TAVARÈ ◽  
BEA CLACK ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Structural Studies ◽  
Human Insulin Receptor

Crystal structure of the tyrosine kinase domain of the human insulin receptor

Nature ◽  
1994 ◽  
Vol 372 (6508) ◽  
pp. 746-754 ◽  
Author(s):  
Stevan R. Hubbard ◽  
Lei Wei ◽  
Wayne A. Hendrickson
Keyword(s):  
Crystal Structure ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Human Insulin Receptor

NIDDM associated with mutation in tyrosine kinase domain of insulin receptor gene

Diabetes ◽  
1992 ◽  
Vol 41 (4) ◽  
pp. 521-526 ◽  
Author(s):  
S. Cocozza ◽  
A. Porcellini ◽  
G. Riccardi ◽  
A. Monticelli ◽  
G. Condorelli ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Gene ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Insulin Receptor Gene

Characteristics of EGFR uncommon mutations in Chinese cancer patients.

2020 ◽  
Vol 38 (15_suppl) ◽  
pp. e13527-e13527
Author(s):  
Minghui Wang ◽  
Shuben Li ◽  
Hongbiao Wang ◽  
Jianjiang Xie ◽  
Junhang Zhang ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Transmembrane Domain ◽  
Kinase Domain ◽  
Copy Number Variations ◽  
Chinese Patients ◽  
Next Generation Sequencing Data ◽  
Egfr Mutations ◽  
Tyrosine Kinase Domain ◽  
Lung Cancers ◽  
Exon 19

e13527 Background: Exon 19 deletions and exon 21 L858R substitutions are the most common mutations of epidermal growth factor receptor (EGFR) in cancers, and the remaining other mutations are called uncommon mutations. Recent studies have shown the clinical relevance of EGFR uncommon mutations with tyrosine kinase inhibitors (TKI) therapies and immunotherapies. Therefore, understanding the distribution and characteristics of EGFR uncommon mutations in cancers would provide evidence for future design of trials and drug development. Methods: Next-generation sequencing data were obtained from 3,026 Chinese tumor samples which have been identified with EGFR mutations. Single nucleotide variations (SNV), short and long insertions/deletions (indel), copy number variations and gene rearrangements were assessed. All tests were carried out in a College of American Pathologists (CAP) accredited and Clinical Laboratory Improvement Amendments (CLIA) certified laboratory in Shanghai, China. Results: EGFR mutations including 32% L858R substitutions, 28% exon 19 deletions, and 40% uncommon mutations were detected in this cohort. EGFR uncommon mutations were most frequently detected in lung cancers, followed by esophageal and gastric cancers. The uncommon mutations of EGFR including 54% SNVs, 30% amplifications, and 9% rare types of mutations such as rearrangement, long indels and complex mutations were detected. The SNVs in exon 18 to 21 which encode the tyrosine kinase domain of EGFR consisted of 16% EGFR mutations. Among them, the mostly frequently SNV was G719X in exon 18 and had 3% EGFR mutations. Mutations in other function domain of EGFR, including extracellular EGF binding domain (0.8%), transmembrane domain (0.03%) and intracellular autophosphorylation domain (0.7%) were also detected. Conclusions: Our data indicated that EGFR uncommon mutations were widely distributed in a variety of cancer types in Chinese patients, mostly in lung cancers. SNVs in the tyrosine kinase domain were the most frequent uncommon mutations. These data will provide clues for future clinical studies.

scholarly journals Antibodies to insulin receptor tyrosine kinase stimulate its activity towards exogenous substrates without inducing receptor autophosphorylation

1989 ◽  
Vol 260 (3) ◽  
pp. 749-756 ◽  
Author(s):  
V Baron ◽  
N Gautier ◽  
N Rochet ◽  
R Ballotti ◽  
B Rossi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Insulin Receptor Tyrosine Kinase ◽  
Substrate Phosphorylation ◽  
Exogenous Substrates

Anti-peptide antibodies directed against a highly-conserved sequence of the insulin receptor tyrosine kinase domain have been used to study the relationship between this specific region and kinase activation. Antibodies have been prepared by the injection into a rabbit of a synthetic peptide (P2) corresponding to residues 1110-1125 of the proreceptor. The peptide exhibits 88-95% sequence similarity with the corresponding sequence in the v-ros protein and in receptors for epidermal growth factor and for insulin-like growth factor 1. Two antibodies with different specificities could be separated from total antiserum obtained after immunization with P2. One antibody [anti-(P-Tyr)] cross-reacted with phosphotyrosine and immunoprecipitated solely autophosphorylated receptors. This antibody was shown to increase or decrease the receptor tyrosine kinase activity depending on its concentration. In all circumstances receptor autophosphorylation and substrate phosphorylation were modulated in a parallel fashion. The second antibody (anti-P2) failed to immunoprecipitate the insulin receptor, but was found to interact with both the peptide and the receptor by e.l.i.s.a. assay. Using a tyrosine co-polymer we found that anti-P2 activated the insulin receptor kinase leading to substrate phosphorylation at a level similar to that observed with insulin. This effect was additive to the hormonal effect. In contrast, receptor autophosphorylation was not modified by the anti-peptide. The differential effect of this anti-peptide further supports the idea that receptor autophosphorylation and kinase activity towards exogenous substrates might be independently regulated. Finally, our data suggest that conformational changes in the receptor tyrosine kinase domain may be sufficient for activation of its enzymic activity.

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