 Procollagen N-Endopeptidase
"Procollagen N-Endopeptidase" 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.
An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in the inherited connective tissue disorder--dermatosparaxis. EC 3.4.24.14.
| Descriptor ID |
D011348
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| MeSH Number(s) |
D08.811.277.656.300.480.664 D08.811.277.656.675.374.664
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| Concept/Terms |
Procollagen N-Endopeptidase- Procollagen N-Endopeptidase
- Procollagen N Endopeptidase
- Procollagen N-Proteinase
- Procollagen N Proteinase
- Procollagen Peptidase
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Below are MeSH descriptors whose meaning is more general than "Procollagen N-Endopeptidase".
Below are MeSH descriptors whose meaning is more specific than "Procollagen N-Endopeptidase".
This graph shows the total number of publications written about "Procollagen N-Endopeptidase" by people in this website by year, and whether "Procollagen N-Endopeptidase" 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 |
|---|
| 2001 | 0 | 2 | 2 | | 2002 | 0 | 4 | 4 | | 2003 | 0 | 1 | 1 | | 2004 | 2 | 2 | 4 | | 2005 | 3 | 0 | 3 | | 2006 | 0 | 1 | 1 | | 2007 | 5 | 1 | 6 | | 2008 | 1 | 2 | 3 | | 2009 | 0 | 1 | 1 | | 2010 | 0 | 1 | 1 | | 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Procollagen N-Endopeptidase" by people in Profiles.
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Malfait AM, Tortorella MD. The "elusive DMOAD": Aggrecanase inhibition from laboratory to clinic. Clin Exp Rheumatol. 2019 Sep-Oct; 37 Suppl 120(5):130-134.
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Lemke AK, Sandy JD, Voigt H, Dreier R, Lee JH, Grodzinsky AJ, Mentlein R, Fay J, Schünke M, Kurz B. Interleukin-1alpha treatment of meniscal explants stimulates the production and release of aggrecanase-generated, GAG-substituted aggrecan products and also the release of pre-formed, aggrecanase-generated G1 and m-calpain-generated G1-G2. Cell Tissue Res. 2010 Apr; 340(1):179-88.
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Tortorella MD, Tomasselli AG, Mathis KJ, Schnute ME, Woodard SS, Munie G, Williams JM, Caspers N, Wittwer AJ, Malfait AM, Shieh HS. Structural and inhibition analysis reveals the mechanism of selectivity of a series of aggrecanase inhibitors. J Biol Chem. 2009 Sep 04; 284(36):24185-91.
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Frank JE, Thompson VP, Brown MP, Sandy JD. Removal of O-linked and N-linked oligosaccharides is required for optimum detection of NITEGE neoepitope on ADAMTS4-digested fetal aggrecans: implications for specific N-linked glycan-dependent aggrecanolysis at Glu373-Ala374. Osteoarthritis Cartilage. 2009 Jun; 17(6):777-81.
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Li X, Phillips FM, An HS, Ellman M, Thonar EJ, Wu W, Park D, Im HJ. The action of resveratrol, a phytoestrogen found in grapes, on the intervertebral disc. Spine (Phila Pa 1976). 2008 Nov 15; 33(24):2586-95.
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Malfait AM, Arner EC, Song RH, Alston JT, Markosyan S, Staten N, Yang Z, Griggs DW, Tortorella MD. Proprotein convertase activation of aggrecanases in cartilage in situ. Arch Biochem Biophys. 2008 Oct 01; 478(1):43-51.
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Hamel MG, Ajmo JM, Leonardo CC, Zuo F, Sandy JD, Gottschall PE. Multimodal signaling by the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) promotes neurite extension. Exp Neurol. 2008 Apr; 210(2):428-40.
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Patel KP, Sandy JD, Akeda K, Miyamoto K, Chujo T, An HS, Masuda K. Aggrecanases and aggrecanase-generated fragments in the human intervertebral disc at early and advanced stages of disc degeneration. Spine (Phila Pa 1976). 2007 Nov 01; 32(23):2596-603.
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Wittwer AJ, Hills RL, Keith RH, Munie GE, Arner EC, Anglin CP, Malfait AM, Tortorella MD. Substrate-dependent inhibition kinetics of an active site-directed inhibitor of ADAMTS-4 (Aggrecanase 1). Biochemistry. 2007 May 29; 46(21):6393-401.
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Hills R, Mazzarella R, Fok K, Liu M, Nemirovskiy O, Leone J, Zack MD, Arner EC, Viswanathan M, Abujoub A, Muruganandam A, Sexton DJ, Bassill GJ, Sato AK, Malfait AM, Tortorella MD. Identification of an ADAMTS-4 cleavage motif using phage display leads to the development of fluorogenic peptide substrates and reveals matrilin-3 as a novel substrate. J Biol Chem. 2007 Apr 13; 282(15):11101-9.
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