The role of serpins in the surveillance of the secretory pathway

Ragg H (2007)
CELL. MOL. LIFE SCI. 64(21): 2763-2770.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Serpins (serine protease inhibitors) constitute a class of proteins with an unusually wide spectrum of different functions at extracellular sites and within the nucleocytoplasmic compartment that extends from protease inhibition to hormone transport and regulation of chromatin organization. Recent investigations reveal a growing number of serpins acting in secretory pathway organelles, indicating that they are not simply cargo destined for export, but fulfill distinct roles within the classical organelle-coupled trafficking system. These findings imply that some serpins are part of a quality control system that monitors the export and possibly import routes of eukaryotic cells. The molecular targets of these serpins are often unknown, opening new avenues for future research.
Stichworte
neuropeptides; furin; proprotein convertase; protease; secretory; serpin; pathway; golgi
Erscheinungsjahr
2007
Zeitschriftentitel
CELL. MOL. LIFE SCI.
Band
64
Ausgabe
21
Seite(n)
2763-2770
ISSN
1420-682X
eISSN
1420-9071
Page URI
https://pub.uni-bielefeld.de/record/1631413

Zitieren

Ragg H. The role of serpins in the surveillance of the secretory pathway. CELL. MOL. LIFE SCI. 2007;64(21):2763-2770.
Ragg, H. (2007). The role of serpins in the surveillance of the secretory pathway. CELL. MOL. LIFE SCI., 64(21), 2763-2770. https://doi.org/10.1007/s00018-007-7157-0
Ragg, Hermann. 2007. “The role of serpins in the surveillance of the secretory pathway”. CELL. MOL. LIFE SCI. 64 (21): 2763-2770.
Ragg, H. (2007). The role of serpins in the surveillance of the secretory pathway. CELL. MOL. LIFE SCI. 64, 2763-2770.
Ragg, H., 2007. The role of serpins in the surveillance of the secretory pathway. CELL. MOL. LIFE SCI., 64(21), p 2763-2770.
H. Ragg, “The role of serpins in the surveillance of the secretory pathway”, CELL. MOL. LIFE SCI., vol. 64, 2007, pp. 2763-2770.
Ragg, H.: The role of serpins in the surveillance of the secretory pathway. CELL. MOL. LIFE SCI. 64, 2763-2770 (2007).
Ragg, Hermann. “The role of serpins in the surveillance of the secretory pathway”. CELL. MOL. LIFE SCI. 64.21 (2007): 2763-2770.

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Fallahsharoudi A, de Kock N, Johnsson M, Bektic L, Ubhayasekera SJ, Bergquist J, Wright D, Jensen P., G3 (Bethesda) 7(2), 2017
PMID: 27974436
Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni.
Pakchotanon P, Molee P, Nuamtanong S, Limpanont Y, Chusongsang P, Limsomboon J, Chusongsang Y, Maneewatchararangsri S, Chaisri U, Adisakwattana P., Parasitol Res 115(8), 2016
PMID: 27083187
Expression of candidate genes for residual feed intake in Angus cattle.
Al-Husseini W, Gondro C, Quinn K, Herd RM, Gibson JP, Chen Y., Anim Genet 45(1), 2014
PMID: 24134470
High resolution structure of cleaved Serpin 42 Da from Drosophila melanogaster.
Ellisdon AM, Zhang Q, Henstridge MA, Johnson TK, Warr CG, Law RH, Whisstock JC., BMC Struct Biol 14(), 2014
PMID: 24758516
Feeding low or pharmacological concentrations of zinc oxide changes the hepatic proteome profiles in weaned piglets.
Bondzio A, Pieper R, Gabler C, Weise C, Schulze P, Zentek J, Einspanier R., PLoS One 8(11), 2013
PMID: 24282572
Suppression of cancer stemness p21-regulating mRNA and microRNA signatures in recurrent ovarian cancer patient samples.
Gallagher MF, Heffron CC, Laios A, O'Toole SA, Ffrench B, Smyth PC, Flavin RJ, Elbaruni SA, Spillane CD, Martin CM, Sheils OM, O'Leary JJ., J Ovarian Res 5(1), 2012
PMID: 22260314
NMR and mutational identification of the collagen-binding site of the chaperone Hsp47.
Yagi-Utsumi M, Yoshikawa S, Yamaguchi Y, Nishi Y, Kurimoto E, Ishida Y, Homma T, Hoseki J, Nishikawa Y, Koide T, Nagata K, Kato K., PLoS One 7(9), 2012
PMID: 23049894
Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate.
Tyler RE, Pearce MM, Shaler TA, Olzmann JA, Greenblatt EJ, Kopito RR., Mol Biol Cell 23(24), 2012
PMID: 23097496
Global gene expression profiling reveals genes expressed differentially in cattle with high and low residual feed intake.
Chen Y, Gondro C, Quinn K, Herd RM, Parnell PF, Vanselow B., Anim Genet 42(5), 2011
PMID: 21906099
A comparative analysis of serpin genes in the silkworm genome.
Zou Z, Picheng Z, Weng H, Mita K, Jiang H., Genomics 93(4), 2009
PMID: 19150649
Natural occurring polyphenols as template for drug design. Focus on serine proteases.
Cuccioloni M, Mozzicafreddo M, Bonfili L, Cecarini V, Eleuteri AM, Angeletti M., Chem Biol Drug Des 74(1), 2009
PMID: 19519739
Multiple gains of spliceosomal introns in a superfamily of vertebrate protease inhibitor genes.
Ragg H, Kumar A, Köster K, Bentele C, Wang Y, Frese MA, Prib N, Krüger O., BMC Evol Biol 9(), 2009
PMID: 19698129
Effects of leptin deficiency on postnatal lung development in mice.
Huang K, Rabold R, Abston E, Schofield B, Misra V, Galdzicka E, Lee H, Biswal S, Mitzner W, Tankersley CG., J Appl Physiol (1985) 105(1), 2008
PMID: 18467551
Ancestry and evolution of a secretory pathway serpin.
Kumar A, Ragg H., BMC Evol Biol 8(), 2008
PMID: 18793432
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