Results 31 to 40 of about 144,866 (262)

CCDC80 suppresses high‐grade serous ovarian cancer migration via negative regulation of B7‐H3

Molecular Oncology, EarlyView.
PAX8 is a lineage‐specific master regulator of transcription in high‐grade serous ovarian cancer (HGSC) progression. We show for the first time that PAX8 facilitates proliferation and metastasis by repressing the cell autonomous tumor suppressor CCDC80 and inducing B7‐H3 expression.
Aya Saleh, Nitzan Medina‐Itzhaki, Milena Chekov, Eden Gal‐Swisa, Roba Gabesh‐Wahabi, Inbar Savyon, Inna Naroditsky, Hilary A. Kenny, Basem Fares, Lina Korsensky, Einav Girsh, Liron Berger, Ruth Perets   +12 more
wiley   +1 more source

Enzyme-linked immunosorbent assay using a virus type-specific peptide based on a subdomain of envelope protein e(rns) for serologic diagnosis of pestivirus infections in swine

, 2001
Peptides deduced from the C-terminal end (residues 191 to 227) of pestivirus envelope protein Erns were used to develop enzyme-linked immunosorbent assays (ELISAs) to measure specifically antibodies against different types of pestiviruses.
Langedijk, J.P., Smit, J.A., de, Meloen, R.H., Middel, W.G., Kramps, J.A., de Smit, J.A.   +5 more
core   +1 more source

Identification and characterization of a novel non-structural protein of bluetongue virus [PDF]

, 2011
Bluetongue virus (BTV) is the causative agent of a major disease of livestock (bluetongue). For over two decades, it has been widely accepted that the 10 segments of the dsRNA genome of BTV encode for 7 structural and 3 non-structural proteins.
Rixon, F., Palmarini, M., Ratinier Maxime, Ratinier, Maxime, Golder, Matthew, Nunes, S.F., Alessia Armezzani, Sandro Filipe Nunes, Kathryn Allan, Allan Kathryn, Allan, K., Rixon, Frazer, Golder, M., Allan, Kathryn, Nunes Sandro Filipe, Frazer Rixon, Bayoumy, Amr, Shaw, A., Matthew Golder, Franzoni, G., Caporale Marco, Giulia Franzoni, Golder Matthew, Nunes, Sandro Filipe, Bayoumy Amr, Shaw, Andrew, Amr Bayoumy, Palmarini Massimo, Armezzani, A., Shaw Andrew, Palmarini, Massimo, Ratinier, M., Armezzani, Alessia, Franzoni Giulia, Franzoni, Giulia, Maxime Ratinier, Andrew Shaw, Rixon Frazer, Marco Caporale, Massimo Palmarini, Armezzani Alessia, Bayoumy, A., Caporale, Marco, Caporale, M.   +43 more
core   +1 more source

Mycobacterial cell division arrest and smooth‐to‐rough envelope transition using CRISPRi‐mediated genetic repression systems

FEBS Open Bio, EarlyView.
CRISPRI‐mediated gene silencing and phenotypic exploration in nontuberculous mycobacteria. In this Research Protocol, we describe approaches to control, monitor, and quantitatively assess CRISPRI‐mediated gene silencing in M. smegmatis and M. abscessus model organisms.
Vanessa Point, Wafaa Achache, Janïs Laudouze, Eliana Sepulveda Ramos, Mickaël Maziero, Céline Crauste, Stéphane Canaan, Pierre Santucci   +7 more
wiley   +1 more source

MiR‐513a promotes human erythroid differentiation by modulating c‐Jun

FEBS Open Bio, EarlyView.
During early human erythropoiesis, miR‐513a promoted erythroid differentiation in primary human CD34+ hematopoietic stem‐progenitor cells and human TF‐1 erythroleukemic cells by indirectly decreasing c‐Jun and phospho‐c‐Jun expression, which are associated with increased GATA1 expression.
MinJung Kim, Brittany Taylor, Shannon Bolten, Christian L. Eberly, Mahliya Abdurahman, T. Michael Creed, Acong Yang, Taylor L. Hatchet, Tristan Dyson, Shuo Gu, Curt I. Civin, Tami J. Kingsbury   +11 more
wiley   +1 more source

Mechanism of Membrane Fusion by Viral Envelope Proteins

, 2005
Enveloped viruses enter cells by fusing their lipid bilayer membrane with a cellular membrane. Most viral fusion proteins require priming by proteolytic processing, either of the fusion protein itself or of an accompanying protein. The priming step, which often occurs during transport of the fusion protein to the cell surface but may also occur ...
openaire   +2 more sources

Coronavirus Envelope Assembly is Sensitive to Changes in the Terminal Regions of the Viral M Protein [PDF]

, 1998
Recently we demonstrated that the co-expressed coronavirus membrane proteins have the capacity to assemble viral envelopes which are similar to normal virus particles in dimensions and appearance, and which can form independent of a nucleocapsid (Vennema et al., 1996).
de Haan, C A, Vennema, H, Rottier, P J
openaire   +4 more sources

MARCH8 Ubiquitinates the Hepatitis C Virus Nonstructural 2 Protein and Mediates Viral Envelopment [PDF]

Cell Reports, 2019
The mechanisms that regulate envelopment of HCV and other viruses that bud intracellularly and/or lack late-domain motifs are largely unknown. We reported that K63 polyubiquitination of the HCV nonstructural (NS) 2 protein mediates HRS (ESCRT-0 component) binding and envelopment.
Kumar, Sathish, Barouch-Bentov, Rina, Xiao, Fei, Schor, Stanford, Pu, Szuyuan, Biquand, Elise, Lu, Albert, Lindenbach, Brett, Jacob, Yves, Demeret, Caroline, Einav, Shirit   +10 more
openaire   +4 more sources

Loss of AMBRA1 activates MAPK and angiogenesis signaling pathways in melanoma cells

FEBS Open Bio, EarlyView.
Loss of AMBRA1 in melanoma cells activates multiple oncogenic pathways associated with tumor progression. Transcriptomic and protein network analyses revealed that AMBRA1 depletion enhances MAPK/ERK signaling, angiogenesis, TGF‐β/EMT signaling, and Wnt/axon guidance pathways.
Milad Ibrahim, Marco Corazzari, Iman Osman, Jane Armstrong, Noel Carter   +4 more
wiley   +1 more source

Varicellovirus UL 49.5 proteins differentially affect the function of the transporter associated with antigen processing, TAP

, 2008
Cytotoxic T-lymphocytes play an important role in the protection against viral infections, which they detect through the recognition of virus-derived peptides, presented in the context of MHC class I molecules at the surface of the infected cell.
Wiertz, E.J.H.J., Rezende, Marisa Marcondes, Thomas C Mettenleiter, Jacques J Neefjes, Wang, Ying, Koch, J., Mirjam H M Heemskerk, Loch Sandra, Marieke C Verweij, Daus, Franz, Nikolaus Osterrieder, Neefjes, J.J., Tampe, R., Chowdhury, Shafiqul I., Osterrieder, Nikolaus, Loch, S., Edwin Quinten, Rijsewijk, Frans A. M., Quinten, E., Neefjes, Jacques J., Ressing, Maaike E., Lipinska, A.D., Krystyna Bieńkowska-Szewczyk, Verweij Marieke C., Koch Joachim, Danijela Koppers-Lalic, Neefjes Jacques J., Wiertz, Emmanuel J. H. J., Koppers-Lalic, Danijela, Mettenleiter, T.C., Lipińska Andrea D., Rezende Marisa Marcondes, Ressing Maaike E., Emmanuel J H J Wiertz, Lipinska, Andrea D., Tampé Robert, Verweij, M.C., Ressing, M.E., Ying Wang, Wang, Y., Koch, Joachim, Heemskerk, Mirjam H. M., Sandra Loch, Marisa Marcondes Rezende, Tampé, Robert, Daus, F.J., Reits, E.A., Wiertz Emmanuel J. H. J., Shafiqul I Chowdhury, Loch, Sandra, Koppers-Lalic Danijela, Osterrieder, N., Quinten, Edwin, Rezende, M.M., Robert Tampé, Verweij, Marieke C., Joachim Koch, Franz Daus, Mettenleiter Thomas C., Bienkowska-Szewczyk, K., Rijsewijk, F.A.M., Eric A Reits, Heemskerk Mirjam H. M., Mettenleiter, Thomas C., Maaike E Ressing, Reits Eric A., Marcondes Rezende, Marisa, Chowdhury, S.I., Osterrieder Nikolaus, Daus Franz, Quinten Edwin, Koppers-Lalic, D., Reits, Eric A., Bienkowska-Szewczyk, Krystyna, Andrea D Lipińska, Frans A M Rijsewijk, Bieńkowska-Szewczyk Krystyna, Wang Ying, Rijsewijk Frans A. M., Heemskerk, M.H.M., Chowdhury Shafiqul I.   +80 more
core   +1 more source