TPP2

TPP2

Tripeptidyl peptidase II, also known as TPP2, is a human gene.cite web | title = Entrez Gene: TPP2 tripeptidyl peptidase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7174| accessdate = ]

PBB_Summary
section_title =
summary_text =

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Tomkinson B, Jonsson AK |title=Characterization of cDNA for human tripeptidyl peptidase II: the N-terminal part of the enzyme is similar to subtilisin. |journal=Biochemistry |volume=30 |issue= 1 |pages= 168–74 |year= 1991 |pmid= 1670990 |doi=
*cite journal | author=Tomkinson B, Zetterqvist O |title=Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin. |journal=Biochem. J. |volume=267 |issue= 1 |pages= 149–54 |year= 1990 |pmid= 1691635 |doi=
*cite journal | author=Tomkinson B |title=Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II. |journal=Biomed. Biochim. Acta |volume=50 |issue= 4-6 |pages= 727–9 |year= 1992 |pmid= 1840501 |doi=
*cite journal | author=Tomkinson B, Wernstedt C, Hellman U, Zetterqvist O |title=Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7508–12 |year= 1987 |pmid= 3313395 |doi=
*cite journal | author=Wilson C, Gibson AM, McDermott JR |title=Purification and characterization of tripeptidylpeptidase-II from post-mortem human brain. |journal=Neurochem. Res. |volume=18 |issue= 7 |pages= 743–9 |year= 1993 |pmid= 8396212 |doi=
*cite journal | author=Martinsson T, Vujic M, Tomkinson B |title=Localization of the human tripeptidyl peptidase II gene (TPP2) to 13q32-q33 by nonradioactive in situ hybridization and somatic cell hybrids. |journal=Genomics |volume=17 |issue= 2 |pages= 493–5 |year= 1993 |pmid= 8406500 |doi= 10.1006/geno.1993.1353
*cite journal | author=Rose C, Vargas F, Facchinetti P, "et al." |title=Characterization and inhibition of a cholecystokinin-inactivating serine peptidase. |journal=Nature |volume=380 |issue= 6573 |pages= 403–9 |year= 1996 |pmid= 8602240 |doi= 10.1038/380403a0
*cite journal | author=Geier E, Pfeifer G, Wilm M, "et al." |title=A giant protease with potential to substitute for some functions of the proteasome. |journal=Science |volume=283 |issue= 5404 |pages= 978–81 |year= 1999 |pmid= 9974389 |doi=
*cite journal | author=Ganellin CR, Bishop PB, Bambal RB, "et al." |title=Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors. |journal=J. Med. Chem. |volume=43 |issue= 4 |pages= 664–74 |year= 2000 |pmid= 10691692 |doi=
*cite journal | author=Lévy F, Burri L, Morel S, "et al." |title=The final N-terminal trimming of a subaminoterminal proline-containing HLA class I-restricted antigenic peptide in the cytosol is mediated by two peptidases. |journal=J. Immunol. |volume=169 |issue= 8 |pages= 4161–71 |year= 2002 |pmid= 12370345 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Lindås AC, Tomkinson B |title=Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II. |journal=Gene |volume=345 |issue= 2 |pages= 249–57 |year= 2005 |pmid= 15716107 |doi= 10.1016/j.gene.2004.11.042
*cite journal | author=Stavropoulou V, Vasquez V, Cereser B, "et al." |title=TPPII promotes genetic instability by allowing the escape from apoptosis of cells with activated mitotic checkpoints. |journal=Biochem. Biophys. Res. Commun. |volume=346 |issue= 2 |pages= 415–25 |year= 2006 |pmid= 16762321 |doi= 10.1016/j.bbrc.2006.05.141
*cite journal | author=York IA, Bhutani N, Zendzian S, "et al." |title=Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation. |journal=J. Immunol. |volume=177 |issue= 3 |pages= 1434–43 |year= 2006 |pmid= 16849449 |doi=
*cite journal | author=Lindås AC, Tomkinson B |title=Characterization of the promoter of the gene encoding human tripeptidyl-peptidase II and identification of upstream silencer elements. |journal=Gene |volume=393 |issue= 1-2 |pages= 62–9 |year= 2007 |pmid= 17343995 |doi= 10.1016/j.gene.2007.01.015

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

Look at other dictionaries:

  • поле позиционного допуска оси (или прямой) в пространстве — 1) Область в пространстве, ограниченная цилиндром, диаметр которого равен позиционному допуску в диаметральном выражении TPP или удвоенному позиционному допуску в радиусном выражении R, а ось совпадает с номинальным расположением рассматриваемой… …   Справочник технического переводчика

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”