"Protease Nexins" 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.
Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.
| Descriptor ID |
D058255
|
| MeSH Number(s) |
D12.644.822.468 D12.776.645.468
|
| Concept/Terms |
Protease Nexins- Protease Nexins
- Nexins, Protease
- Nexin, Protease
- Protease Nexin
- Nexin, Protease-Associated
- Nexin, Protease Associated
- Protease-Associated Nexin
|
Below are MeSH descriptors whose meaning is more general than "Protease Nexins".
Below are MeSH descriptors whose meaning is more specific than "Protease Nexins".
This graph shows the total number of publications written about "Protease Nexins" by people in this website by year, and whether "Protease Nexins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 0 | 1 | 1 |
| 2003 | 0 | 1 | 1 |
| 2005 | 0 | 1 | 1 |
| 2006 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protease Nexins" by people in Profiles.
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The SERPINE2 gene is associated with chronic obstructive pulmonary disease. Proc Am Thorac Soc. 2006 Aug; 3(6):502.
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The SERPINE2 gene is associated with chronic obstructive pulmonary disease. Am J Hum Genet. 2006 Feb; 78(2):253-64.
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GeneChip microarrays facilitate identification of Protease Nexin-1 as a target gene of the Prx2 (S8) homeoprotein. DNA Cell Biol. 2003 Feb; 22(2):95-105.
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Characterization of the human protease nexin-1 promoter and its regulation by Sp1 through a G/C-rich activation domain. J Neurochem. 1996 Aug; 67(2):498-507.
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Protease nexin-1, a thrombin inhibitor, is regulated by interleukin-1 and dexamethasone in normal human fibroblasts. J Biol Chem. 1993 Sep 05; 268(25):18966-74.
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The Alzheimer's amyloid precursor is cleaved intracellularly in the trans-Golgi network or in a post-Golgi compartment. Ann N Y Acad Sci. 1992 Dec 31; 674:118-28.