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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Dipeptidyl-peptidase 7

dipeptidyl peptidase II, DPP II, quiescent cell proline dipeptidase, QPP
The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DSP, ACID, CD26, DPP8, aminopeptidase
Papers on dipeptidyl peptidase II
Reactivity, characterization of reaction products and immobilization of lead in water and sediments using quercetin pentaphosphate.
Sadik et al., Binghamton, United States. In Environ Sci Process Impacts, Feb 2016
This study reports the application of water soluble quercetin pentaphosphate (QPP), a derivative of quercetin, for the detection and immobilization of Pb(2+) from water and soil samples.
Purification and biochemical characterization of dipeptidyl peptidase-II (DPP7) homologue from germinated Vigna radiata seeds.
Singh et al., India. In Bioorg Chem, Dec 2015
As compared to other members of DPP family, proline containing dipeptide hydrolysing activity of DPP-II (Dipeptidyl peptidase II) is unique as it hydrolyses imino group and plays a key role in protein metabolism.
The Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including Atherosclerosis.
De Meester et al., Antwerp, Belgium. In Front Immunol, 2014
In this review, we provide a comprehensive discussion on the role of prolyl-specific peptidases DPPIV, FAP, DPP8, DPP9, dipeptidyl peptidase II, prolyl carboxypeptidase, and prolyl oligopeptidase in the immune system and its diseases.
Extended structure-activity relationship and pharmacokinetic investigation of (4-quinolinoyl)glycyl-2-cyanopyrrolidine inhibitors of fibroblast activation protein (FAP).
Van der Veken et al., Antwerp, Belgium. In J Med Chem, 2014
We report extensively optimized compounds that display low nanomolar inhibitory potency and high selectivity against the related dipeptidyl peptidases (DPPs) DPPIV, DPP9, DPPII, and prolyl oligopeptidase (PREP).
Novel tetrahydropyran analogs as dipeptidyl peptidase IV inhibitors: Profile of clinical candidate (2R,3S,5R)-2- (2,5-difluorophenyl)-5-(4,6-dihydropyrrolo [3,4-c]pyrazol-5-(1H)-yl)tetrahydro-2H-pyran-3-amine (23) [corrected].
Weber et al., Rahway, United States. In Bioorg Med Chem Lett, 2013
Optimization of the series provided inhibitors with good DPP-4 potency and selectivity over other peptidases (QPP, DPP8, and FAP).
Aza-Michael access to fluoroalkylidene analogues of biomolecules.
Lequeux et al., Caen, France. In J Org Chem, 2013
The resulting aminosulfones open a straightforward access to a series of new fluorinated biomolecules including a potent DPP-II inhibitor and acyclonucleoside analogues as potential enzyme inhibitors.
Interaction of dipeptydil peptidase IV with amyloid peptides.
Hovnanyan et al., Yerevan, Armenia. In Neurochem Int, 2013
Dipeptidyl peptidases II and IV (DPPII and DPPIV) are serine proteases removing N-terminal dipeptides from polypeptides and proteins with proline or alanine on the penultimate position.
Structure based lead optimization approach in discovery of selective DPP4 inhibitors.
Jain et al., Ahmadābād, India. In Mini Rev Med Chem, 2013
A number of catalytically active DPPs distinct from DPP-4 (DPP II, FAP, DPP-8, and DPP-9) have been described that is associated with side-effect and toxicity.
Acylated Gly-(2-cyano)pyrrolidines as inhibitors of fibroblast activation protein (FAP) and the issue of FAP/prolyl oligopeptidase (PREP)-selectivity.
Van der Veken et al., Antwerp, Belgium. In Bioorg Med Chem Lett, 2012
The inhibitors displayed inhibitory potency in the micromolar to nanomolar range and showed good to excellent selectivity with respect to the proline selective dipeptidyl peptidases (DPPs) DPP IV, DPP9 and DPP II.
Dipeptidyl peptidase IV, aminopeptidase N and DPIV/APN-like proteases in cerebral ischemia.
Striggow et al., Magdeburg, Germany. In J Neuroinflammation, 2011
Dipeptidyl peptidase II and aminopeptidase N were up-regulated ipsilaterally from 6 h to 7 days post ischemia, whereas dipeptidyl peptidase 9 and cytosolic alanyl-aminopeptidase were transiently down-regulated at day 3. Dipeptidyl peptidase 8 and aminopeptidase N immunoreactivities were detected in cortical neurons of the contralateral hemisphere.
Interspecies differences in membrane-associated protease activities of thyrocytes and their relevance for thyroid cancer studies.
Wahl et al., Tübingen, Germany. In J Exp Clin Cancer Res, 2011
The lysosomal protease, dipeptidyl peptidase II, was used for comparison.
Current advances and therapeutic potential of agents targeting dipeptidyl peptidases-IV, -II, 8/9 and fibroblast activation protein.
Jiaang et al., Taiwan. In Curr Top Med Chem, 2010
This review summarizes important structural classes of DPP-IV inhibitors, focusing mainly on their inhibitory potency and selectivity for DPP-IV over other related peptidases such as DPP-II, DPP8, DPP9, and FAP.
Expression and prognostic assessment of dipeptidyl peptidase IV and related enzymes in B-cell chronic lymphocytic leukemia.
Kuss et al., Adelaide, Australia. In Cancer Biol Ther, 2010
The constitutive expression of dipeptidyl peptidase II mRNA in chronic lymphocytic leukemia was demonstrated.
Dipeptidyl peptidase 2 is an essential survival factor in the regulation of cell quiescence.
Huber et al., Boston, United States. In Cell Cycle, 2009
DPP2 is essential for maintaining lymphocytes and fibroblasts in G(0), and its inhibition results in apoptosis mediated by induction of c-Myc and p53.
Dipeptidyl peptidase II is not a marker for progression in melanoma.
Garbe et al., In J Dermatol Sci, 2009
DPP II plays a minor role in the progression of malignant melanocytic lesions
Expression pattern of dipeptidyl peptidase IV activity and/or structure homologues in cancer.
Sedo et al., Praha, Czech Republic. In Folia Biol (praha), 2008
Along with canonical DPP-IV this group comprises DPP-IVbeta, DPP-II, DPP6, DPP8, DPP9, DPP10 and fibroblast activation protein alpha (FAP-alpha).
Dipeptidyl peptidase-IV enzymatic activity bearing molecules in human brain tumors--good or evil?
Sedo et al., Praha, Czech Republic. In Front Biosci, 2007
These comprise enzymatically active fibroblast activation protein-alpha, DPP-II, DPP8, DPP9 and enzymatically inactive DPP6 and DPP10 that have been grouped as "DPP-IV activity and/or structure homologues" (DASH).
Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII.
Thornberry et al., Rahway, United States. In Biochem J, 2003
catalytic properties and inhibition of this proline-specific enzyme
Histological and histochemical changes in the digestive tract of white sturgeon larvae during ontogeny.
de la Noüe et al., Québec, Canada. In Fish Physiol Biochem, 1995
The functional development of the pyloric intestine occurred on day 4 and was concomitant with an increase in the activity of brush border and cytoplasmic enzymes such as acetylcholinesterase, dipeptidyl peptidase II, α- and β-galactosidases.
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