 Protein-Tyrosine Kinases
"Protein-Tyrosine Kinases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
| Descriptor ID |
D011505
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| MeSH Number(s) |
D08.811.913.696.620.682.725
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| Concept/Terms |
Protein-Tyrosine Kinases- Protein-Tyrosine Kinases
- Kinases, Protein-Tyrosine
- Protein Tyrosine Kinases
- Tyrosine Kinase
- Kinase, Tyrosine
- Tyrosine Protein Kinase
- Kinase, Tyrosine Protein
- Tyrosylprotein Kinase
- Kinase, Tyrosylprotein
- Tyrosine-Specific Protein Kinase
- Kinase, Tyrosine-Specific Protein
- Protein Kinase, Tyrosine-Specific
- Tyrosine Specific Protein Kinase
- Tyrosine-Specific Protein Kinases
- Kinases, Tyrosine-Specific Protein
- Protein Kinases, Tyrosine-Specific
- Tyrosine Specific Protein Kinases
- Protein-Tyrosine Kinase
- Kinase, Protein-Tyrosine
- Protein Tyrosine Kinase
- Tyrosine Protein Kinases
- Kinases, Tyrosine Protein
- Protein Kinases, Tyrosine
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Below are MeSH descriptors whose meaning is more general than "Protein-Tyrosine Kinases".
Below are MeSH descriptors whose meaning is more specific than "Protein-Tyrosine Kinases".
This graph shows the total number of publications written about "Protein-Tyrosine Kinases" by people in this website by year, and whether "Protein-Tyrosine Kinases" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 1 | 0 | 1 | | 1999 | 0 | 2 | 2 |
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Below are the most recent publications written about "Protein-Tyrosine Kinases" by people in Profiles.
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Homayouni R, Rice DS, Sheldon M, Curran T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J Neurosci. 1999 Sep 01; 19(17):7507-15.
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Cappadona C, Redmond EM, Theodorakis NG, McKillop IH, Hendrickson R, Chhabra A, Sitzmann JV, Cahill PA. Phenotype dictates the growth response of vascular smooth muscle cells to pulse pressure in vitro. Exp Cell Res. 1999 Jul 10; 250(1):174-86.
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Meydan N, Grunberger T, Dadi H, Shahar M, Arpaia E, Lapidot Z, Leeder JS, Freedman M, Cohen A, Gazit A, Levitzki A, Roifman CM. Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature. 1996 Feb 15; 379(6566):645-8.
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Heruth DP, Wetmore LA, Leyva A, Rothberg PG. Influence of protein tyrosine phosphorylation on the expression of the c-myc oncogene in cancer of the large bowel. J Cell Biochem. 1995 May; 58(1):83-94.
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Alvarez E, Northwood IC, Gonzalez FA, Latour DA, Seth A, Abate C, Curran T, Davis RJ. Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase. J Biol Chem. 1991 Aug 15; 266(23):15277-85.
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Abate C, Luk D, Curran T. Transcriptional regulation by Fos and Jun in vitro: interaction among multiple activator and regulatory domains. Mol Cell Biol. 1991 Jul; 11(7):3624-32.
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Owen TA, Bortell R, Yocum SA, Smock SL, Zhang M, Abate C, Shalhoub V, Aronin N, Wright KL, van Wijnen AJ, et al. Coordinate occupancy of AP-1 sites in the vitamin D-responsive and CCAAT box elements by Fos-Jun in the osteocalcin gene: model for phenotype suppression of transcription. Proc Natl Acad Sci U S A. 1990 Dec; 87(24):9990-4.
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Gius D, Cao XM, Rauscher FJ, Cohen DR, Curran T, Sukhatme VP. Transcriptional activation and repression by Fos are independent functions: the C terminus represses immediate-early gene expression via CArG elements. Mol Cell Biol. 1990 Aug; 10(8):4243-55.
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Macgregor PF, Abate C, Curran T. Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene. 1990 Apr; 5(4):451-8.
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Abate C, Luk D, Gentz R, Rauscher FJ, Curran T. Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly. Proc Natl Acad Sci U S A. 1990 Feb; 87(3):1032-6.
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