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The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity.

Zhong M, Munzer JS, Basak A, Benjannet S, Mowla SJ, Decroly E, Chrétien M, Seidah NG.

J Biol Chem. 1999 Nov 26;274(48):33913-20.


The RGD motif and the C-terminal segment of proprotein convertase 1 are critical for its cellular trafficking but not for its intracellular binding to integrin alpha5beta1.

Rovère C, Luis J, Lissitzky JC, Basak A, Marvaldi J, Chrétien M, Seidah NG.

J Biol Chem. 1999 Apr 30;274(18):12461-7.


Proprotein cleavage of E-cadherin by furin in baculovirus over-expression system: potential role of other convertases in mammalian cells.

Posthaus H, Dubois CM, Laprise MH, Grondin F, Suter MM, Müller E.

FEBS Lett. 1998 Nov 6;438(3):306-10.


Furin and proprotein convertase 7 (PC7)/lymphoma PC endogenously expressed in rat liver can be resolved into distinct post-Golgi compartments.

Wouters S, Leruth M, Decroly E, Vandenbranden M, Creemers JW, van de Loo JW, Ruysschaert JM, Courtoy PJ.

Biochem J. 1998 Dec 1;336 ( Pt 2):311-6.


Identification of inhibitors of prohormone convertases 1 and 2 using a peptide combinatorial library.

Apletalina E, Appel J, Lamango NS, Houghten RA, Lindberg I.

J Biol Chem. 1998 Oct 9;273(41):26589-95.


Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain.

Schäcke H, Schumann H, Hammami-Hauasli N, Raghunath M, Bruckner-Tuderman L.

J Biol Chem. 1998 Oct 2;273(40):25937-43.


PC5-A-mediated processing of pro-neurotensin in early compartments of the regulated secretory pathway of PC5-transfected PC12 cells.

Barbero P, Rovère C, De Bie I, Seidah N, Beaudet A, Kitabgi P.

J Biol Chem. 1998 Sep 25;273(39):25339-46.


Deficient processing and activity of type I insulin-like growth factor receptor in the furin-deficient LoVo-C5 cells.

Lehmann M, André F, Bellan C, Remacle-Bonnet M, Garrouste F, Parat F, Lissitsky JC, Marvaldi J, Pommier G.

Endocrinology. 1998 Sep;139(9):3763-71.


The Notch1 receptor is cleaved constitutively by a furin-like convertase.

Logeat F, Bessia C, Brou C, LeBail O, Jarriault S, Seidah NG, Israël A.

Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8108-12.


Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins.

Aplin AE, Howe A, Alahari SK, Juliano RL.

Pharmacol Rev. 1998 Jun;50(2):197-263. Review. No abstract available.


alpha1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent.

Jean F, Stella K, Thomas L, Liu G, Xiang Y, Reason AJ, Thomas G.

Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7293-8.


Precursor convertases: an evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins.

Seidah NG, Day R, Marcinkiewicz M, Chrétien M.

Ann N Y Acad Sci. 1998 May 15;839:9-24. Review. No abstract available.


Expression of PACE4 in chemically induced carcinomas is associated with spindle cell tumor conversion and increased invasive ability.

Hubbard FC, Goodrow TL, Liu SC, Brilliant MH, Basset P, Mains RE, Klein-Szanto AJ.

Cancer Res. 1997 Dec 1;57(23):5226-31.


Eukaryotic protein processing: endoproteolysis of precursor proteins.

Seidah NG, Chrétien M.

Curr Opin Biotechnol. 1997 Oct;8(5):602-7. Review.


Biosynthesis, distinct post-translational modifications, and functional characterization of lymphoma proprotein convertase.

van de Loo JW, Creemers JW, Bright NA, Young BD, Roebroek AJ, Van de Ven WJ.

J Biol Chem. 1997 Oct 24;272(43):27116-23.


Alpha1-antitrypsin Portland inhibits processing of precursors mediated by proprotein convertases primarily within the constitutive secretory pathway.

Benjannet S, Savaria D, Laslop A, Munzer JS, Chrétien M, Marcinkiewicz M, Seidah NG.

J Biol Chem. 1997 Oct 17;272(42):26210-8.


The alpha v beta 3 integrin "vitronectin receptor".

Horton MA.

Int J Biochem Cell Biol. 1997 May;29(5):721-5. Review.

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