 Endopeptidase K
"Endopeptidase K" 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 enzyme that catalyzes the hydrolysis of keratin, and of other proteins with subtilisin-like specificity. It hydrolyses peptide amides. Endopeptidase K is from the mold Tritirachium album Limber. (Enzyme Nomenclature, 1992) EC 3.4.21.64.
| Descriptor ID |
D019286
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| MeSH Number(s) |
D08.811.277.656.300.760.247 D08.811.277.656.959.350.247
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| Concept/Terms |
Endopeptidase K- Endopeptidase K
- Protease K
- Proteinase K
- Tritirachium Alkaline Proteinase
- Alkaline Proteinase, Tritirachium
- Proteinase, Tritirachium Alkaline
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Below are MeSH descriptors whose meaning is more general than "Endopeptidase K".
Below are MeSH descriptors whose meaning is more specific than "Endopeptidase K".
This graph shows the total number of publications written about "Endopeptidase K" by people in this website by year, and whether "Endopeptidase K" 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 |
|---|
| 1992 | 0 | 1 | 1 | | 1993 | 0 | 1 | 1 | | 1995 | 0 | 1 | 1 | | 1996 | 0 | 1 | 1 | | 2001 | 0 | 1 | 1 | | 2002 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2005 | 0 | 2 | 2 | | 2017 | 0 | 1 | 1 | | 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Endopeptidase K" by people in Profiles.
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Qin K, Zhao L, Solanki A, Busch C, Mastrianni J. Anle138b prevents PrP plaque accumulation in Tg(PrP-A116V) mice but does not mitigate clinical disease. J Gen Virol. 2019 06; 100(6):1027-1037.
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Meents A, Wiedorn MO, Srajer V, Henning R, Sarrou I, Bergtholdt J, Barthelmess M, Reinke PYA, Dierksmeyer D, Tolstikova A, Schaible S, Messerschmidt M, Ogata CM, Kissick DJ, Taft MH, Manstein DJ, Lieske J, Oberthuer D, Fischetti RF, Chapman HN. Pink-beam serial crystallography. Nat Commun. 2017 11 03; 8(1):1281.
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Pan T, Chang B, Wong P, Li C, Li R, Kang SC, Robinson JD, Thompsett AR, Tein P, Yin S, Barnard G, McConnell I, Brown DR, Wisniewski T, Sy MS. An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrP(Sc) aggregates. J Virol. 2005 Oct; 79(19):12355-64.
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Norstrom EM, Mastrianni JA. The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation. J Biol Chem. 2005 Jul 22; 280(29):27236-43.
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Marraffini LA, Schneewind O. Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC. J Biol Chem. 2005 Apr 22; 280(16):16263-71.
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Beeler JA, Yan SZ, Bykov S, Murza A, Asher S, Tang WJ. A soluble C1b protein and its regulation of soluble type 7 adenylyl cyclase. Biochemistry. 2004 Dec 14; 43(49):15463-71.
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Biswas TK, Getz GS. Import of yeast mitochondrial transcription factor (Mtf1p) via a nonconventional pathway. J Biol Chem. 2002 Nov 22; 277(47):45704-14.
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Jeffrey M, Martin S, Barr J, Chong A, Fraser JR. Onset of accumulation of PrPres in murine ME7 scrapie in relation to pathological and PrP immunohistochemical changes. J Comp Pathol. 2001 Jan; 124(1):20-8.
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Lee VT, Schneewind O. Type III machines of pathogenic yersiniae secrete virulence factors into the extracellular milieu. Mol Microbiol. 1999 Mar; 31(6):1619-29.
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Cheley S, Malghani MS, Song L, Hobaugh M, Gouaux JE, Yang J, Bayley H. Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel. Protein Eng. 1997 Dec; 10(12):1433-43.
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