Relevant bibliographies by topics / Signal-peptide-peptidase [SPP]

Contents

  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Signal-peptide-peptidase [SPP]'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Signal-peptide-peptidase [SPP].'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Signal-peptide-peptidase [SPP]"

1

Hope, R. Graham, Marion J. McElwee, and John McLauchlan. "Efficient cleavage by signal peptide peptidase requires residues within the signal peptide between the core and E1 proteins of hepatitis C virus strain J1." Journal of General Virology 87, no. 3 (2006): 623–27. http://dx.doi.org/10.1099/vir.0.81371-0.

Full text
Abstract:
Maturation of hepatitis C virus (HCV) core protein requires cleavage by signal peptidase (SP) and signal peptide peptidase (SPP) at a signal peptide between core and the E1 glycoprotein. For HCV strain Glasgow, amino acids Ala180, Ser183 and Cys184 within the signal peptide have previously been shown to be essential for efficient SPP cleavage. By contrast, these residues apparently did not contribute to core maturation in HCV strain J1. In the present study, the source of this discrepancy has been analysed and it is concluded that interpretation of the strain J1 data was incorrect, due to the
APA, Harvard, Vancouver, ISO, and other styles
2

Mentrup, Torben, Ann-Christine Loock, Regina Fluhrer, and Bernd Schröder. "Signal peptide peptidase and SPP-like proteases - Possible therapeutic targets?" Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1864, no. 11 (2017): 2169–82. http://dx.doi.org/10.1016/j.bbamcr.2017.06.007.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Voss, Matthias, Bernd Schröder, and Regina Fluhrer. "Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases." Biochimica et Biophysica Acta (BBA) - Biomembranes 1828, no. 12 (2013): 2828–39. http://dx.doi.org/10.1016/j.bbamem.2013.03.033.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Schröder, Bernd, and Paul Saftig. "Molecular insights into mechanisms of intramembrane proteolysis through signal peptide peptidase (SPP)." Biochemical Journal 427, no. 3 (2010): e1-e3. http://dx.doi.org/10.1042/bj20100391.

Full text
Abstract:
The processing of membrane-anchored signalling molecules and transcription factors by RIP (regulated intramembrane proteolysis) is a major signalling paradigm in eukaryotic cells. Intramembrane cleaving proteases liberate fragments from membrane-bound precursor proteins which typically fulfil functions such as cell signalling and regulation, immunosurveillance and intercellular communication. Furthermore, they are thought to be involved in the development and propagation of several diseases, such as Alzheimer's disease and hepatitis C virus infection. In this issue of the Biochemical Journal,
APA, Harvard, Vancouver, ISO, and other styles
5

Schrul, Bianca, Katja Kapp, Irmgard Sinning, and Bernhard Dobberstein. "Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes." Biochemical Journal 427, no. 3 (2010): 523–34. http://dx.doi.org/10.1042/bj20091005.

Full text
Abstract:
SPP (signal peptide peptidase) is an aspartyl intramembrane cleaving protease, which processes a subset of signal peptides, and is linked to the quality control of ER (endoplasmic reticulum) membrane proteins. We analysed SPP interactions with signal peptides and other membrane proteins by co-immunoprecipitation assays. We found that SPP interacts specifically and tightly with a large range of newly synthesized membrane proteins, including signal peptides, preproteins and misfolded membrane proteins, but not with all co-expressed type II membrane proteins. Signal peptides are trapped by the ca
APA, Harvard, Vancouver, ISO, and other styles
6

Hirano, Junki, Sachiyo Yoshio, Yusuke Sakai, et al. "Hepatitis C virus modulates signal peptide peptidase to alter host protein processing." Proceedings of the National Academy of Sciences 118, no. 22 (2021): e2026184118. http://dx.doi.org/10.1073/pnas.2026184118.

Full text
Abstract:
Immunoevasins are viral proteins that prevent antigen presentation on major histocompatibility complex (MHC) class I, thus evading host immune recognition. Hepatitis C virus (HCV) evades immune surveillance to induce chronic infection; however, how HCV-infected hepatocytes affect immune cells and evade immune recognition remains unclear. Herein, we demonstrate that HCV core protein functions as an immunoevasin. Its expression interfered with the maturation of MHC class I molecules catalyzed by the signal peptide peptidase (SPP) and induced their degradation via HMG-CoA reductase degradation 1
APA, Harvard, Vancouver, ISO, and other styles
7

Wang, Shaohui, Ujjaldeep Jaggi, Jack Yu, and Homayon Ghiasi. "Blocking HSV-1 glycoprotein K binding to signal peptide peptidase reduces virus infectivity in vitro and in vivo." PLOS Pathogens 17, no. 8 (2021): e1009848. http://dx.doi.org/10.1371/journal.ppat.1009848.

Full text
Abstract:
HSV glycoprotein K (gK) is an essential herpes protein that contributes to enhancement of eye disease. We previously reported that gK binds to signal peptide peptidase (SPP) and that depletion of SPP reduces HSV-1 infectivity in vivo. To determine the therapeutic potential of blocking gK binding to SPP on virus infectivity and pathogenicity, we mapped the gK binding site for SPP to a 15mer peptide within the amino-terminus of gK. This 15mer peptide reduced infectivity of three different virus strains in vitro as determined by plaque assay, FACS, and RT-PCR. Similarly, the 15mer peptide reduced
APA, Harvard, Vancouver, ISO, and other styles
8

Boname, Jessica M., Stuart Bloor, Michal P. Wandel, et al. "Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins." Journal of Cell Biology 205, no. 6 (2014): 847–62. http://dx.doi.org/10.1083/jcb.201312009.

Full text
Abstract:
The regulated turnover of endoplasmic reticulum (ER)–resident membrane proteins requires their extraction from the membrane lipid bilayer and subsequent proteasome-mediated degradation. Cleavage within the transmembrane domain provides an attractive mechanism to facilitate protein dislocation but has never been shown for endogenous substrates. To determine whether intramembrane proteolysis, specifically cleavage by the intramembrane-cleaving aspartyl protease signal peptide peptidase (SPP), is involved in this pathway, we generated an SPP-specific somatic cell knockout. In a stable isotope lab
APA, Harvard, Vancouver, ISO, and other styles
9

Heimann, Manuela, Gleyder Roman Sosa, Bruno Martoglio, Heinz-Jürgen Thiel, and Till Rümenapf. "Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase." Journal of Virology 80, no. 4 (2006): 1915–21. http://dx.doi.org/10.1128/jvi.80.4.1915-1921.2006.

Full text
Abstract:
ABSTRACT The core protein of pestiviruses is released from the polyprotein by viral and cellular proteinases. Here we report on an additional intramembrane proteolytic step that generates the C terminus of the core protein. C-terminal processing of the core protein of classical swine fever virus (CSFV) was blocked by the inhibitor (Z-LL)2-ketone, which is specific for signal peptide peptidase (SPP). The same effect was obtained by overexpression of the dominant-negative SPP D265A mutant. The presence of (Z-LL)2-ketone reduced the viability of CSFV almost 100-fold in a concentration-dependent m
APA, Harvard, Vancouver, ISO, and other styles
10

Majeau, Nathalie, Valérie Gagné, Marilène Bolduc, and Denis Leclerc. "Signal peptide peptidase promotes the formation of hepatitis C virus non-enveloped particles and is captured on the viral membrane during assembly." Journal of General Virology 86, no. 11 (2005): 3055–64. http://dx.doi.org/10.1099/vir.0.81174-0.

Full text
Abstract:
The maturation of the core protein (C) of Hepatitis C virus (HCV) is controlled by the signal peptidase (sp) and signal peptide peptidase (spp) of the host. To date, it remains unknown whether spp cleavage influences viral infectivity and/or the assembly process. Here, evidence is provided that cleavage by spp is not required for assembly of nucleocapsid-like particles (NLPs) in yeast (Pichia pastoris). The immature NLPs (not processed by spp) show a density of 1·11 g ml−1 on sucrose gradients and a diameter of 50 nm. Co-expression of human spp (hspp) with C generates the 21 kDa mature form of
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Signal-peptide-peptidase [SPP]"

1

Vauloup-Fellous, Christelle. "Morphogenèse du virus de l'hépatite C : rôle du clivage de la protéine de capside par la signal -peptide-peptidase." Paris 6, 2007. http://www.theses.fr/2007PA066380.

Full text
Abstract:
La capside du virus de l’hépatite C (VHC) semble constituée par la forme mature de la protéine de capside (protéine C), la p21. Sa forme immature, la p23, est libérée de la polyprotéine par clivage par la signal peptidase (SP). La p21 est issue du clivage intramembranaire de la p23, par la signal peptide peptidase (SPP). Nous avons étudié le rôle du clivage de la protéine C par la SPP au cours de la morphogenèse virale grâce à 2 systèmes expérimentaux : l’un permettant de visualiser des pseudo-particules de VHC bourgeonnant dans le RE grâce à un vecteur basé sur les propriétés de réplication d
APA, Harvard, Vancouver, ISO, and other styles
2

Pène, Véronique. "Chronologie et rôles des clivages de la protéine C dans le cycle du virus de l'hépatite C." Paris 6, 2007. http://www.theses.fr/2007PA066486.

Full text
Abstract:
La forme p23 de la protéine C du VHC est libérée de la polyprotéine virale au site C/E1 par clivage par la signal peptidase (SP) cellulaire, mais reste ancrée dans la membrane du RE par le peptide signal à la jonction C/E1. La p21 est issue du clivage intramembranaire de ce peptide signal par la signal-peptide-peptidase (SPP). Le but de ce travail a été de déterminer le rôle de ces clivages dans le cycle infectieux du virus. Le clivage de la protéine C par la SP est dans tous les cas un préalable au clivage par la SPP. D’autre part, la morphogenèse du VHC semble favorisée lorsque la protéine C
APA, Harvard, Vancouver, ISO, and other styles
3

Pinter, Niko. "Analysis of Clp1-dependent UPR modulation in Ustilago maydis." Doctoral thesis, 2019. http://hdl.handle.net/21.11130/00-1735-0000-0003-C12F-F.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Signal-peptide-peptidase [SPP]' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography