نتایج جستجو برای: caspase cleavage motif

تعداد نتایج: 121225  

Journal: :iranian journal of virology 0
sh shahsavandi razi vaccine and serum research institute, p.o. box 31975-148, karaj, iran mm ebrahimi razi vaccine and serum research institute, p.o. box 31975-148, karaj, iran k sadeghi razi vaccine and serum research institute, p.o. box 31975-148, karaj, iran

background and aims: the caspases are unique proteases that mediate the host cell apoptosis during viral infection. in this study, we identified the caspase cleavage motifs of h5n1 and h9n2 influenza viruses isolated during 1998-2012. materials and methods: amino acid sequences of the eleven proteins encoded by the viruses as the caspase substrates downloaded from ncbi. the caspase cleavage mot...

Kaveh Sadeghi , Mohammad Majid Ebrahimi, Shahla Shahsavandi ,

Background and Aims: The caspases are unique proteases that mediate the host cell apoptosis during viral infection. In this study, we identified the caspase cleavage motifs of H5N1 and H9N2 influenza viruses isolated during 1998-2012. Materials and Methods: Amino acid sequences of the eleven proteins encoded by the viruses as the caspase substrates downloaded from NCBI. The caspase cleavage mot...

2016
Emilio Boada-Romero Inmaculada Serramito-Gómez María P. Sacristán David L. Boone Ramnik J. Xavier Felipe X. Pimentel-Muiños

A coding polymorphism of human ATG16L1 (rs2241880; T300A) increases the risk of Crohn's disease and it has been shown to enhance susceptibility of ATG16L1 to caspase cleavage. Here we show that T300A also alters the ability of the C-terminal WD40-repeat domain of ATG16L1 to interact with an amino acid motif that recognizes this region. Such alteration impairs the unconventional autophagic activ...

Journal: :Cell 1997
Michael H Cardone Guy S Salvesen Christian Widmann Gary Johnson Steven M Frisch

Certain cell types undergo apoptosis when they lose integrin-mediated contacts with the extracellular matrix ("anoikis"). The Jun N-terminal kinase (JNK) pathway is activated in and promotes anoikis. This activation requires caspase activity. We presently report that a DEVD motif-specific caspase that cleaves MEKK-1 specifically is activated when cells lose matrix contact. This cleavage is requ...

Journal: :The Biochemical journal 2007
Jean-Bernard Denault Brendan P Eckelman Hwain Shin Cristina Pop Guy S Salvesen

During apoptosis, the initiator caspase 9 is activated at the apoptosome after which it activates the executioner caspases 3 and 7 by proteolysis. During this process, caspase 9 is cleaved by caspase 3 at Asp(330), and it is often inferred that this proteolytic event represents a feedback amplification loop to accelerate apoptosis. However, there is substantial evidence that proteolysis per se ...

Journal: :The EMBO journal 1997
E Rhéaume L Y Cohen F Uhlmann C Lazure A Alam J Hurwitz R P Sékaly F Denis

Caspase-3 is an ICE-like protease activated during apoptosis induced by different stimuli. Poly(ADP-ribose) polymerase (PARP), the first characterized substrate of caspase-3, shares a region of homology with the large subunit of Replication Factor C (RF-C), a five-subunit complex that is part of the processive eukaryotic DNA polymerase holoenzymes. Caspase-3 cleaves PARP at a DEVD-G motif prese...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2007
Cary A Moody Amelie Fradet-Turcotte Jacques Archambault Laimonis A Laimins

The life cycle of human papillomaviruses (HPVs) is linked to epithelial differentiation, with late viral events restricted to the uppermost stratified layers. Our studies indicated that HPV activates capases-3, -7, and -9 upon differentiation, whereas minimal activation was observed in differentiating normal keratinocytes. Activation occurred in the absence of significant levels of apoptosis, s...

Journal: :Journal of virology 2008
Michael P Guy Paul D Friesen

Baculovirus proteins P49 and P35 are potent suppressors of apoptosis in diverse organisms. Although related, P49 and P35 inhibit initiator and effector caspases, respectively, during infection of permissive insect cells. The molecular basis of this novel caspase specificity is unknown. To advance strategies for selective inhibition of the cell death caspases, we investigated biochemical differe...

Journal: :The Journal of biological chemistry 2009
Young Eun Choi Michael Butterworth Srinivas Malladi Colin S Duckett Gerald M Cohen Shawn B Bratton

Inhibitor of apoptosis (IAP) proteins are widely expressed throughout nature and suppress cell death under a variety of circumstances. X-linked IAP, the prototypical IAP in mammals, inhibits apoptosis largely through direct inhibition of the initiator caspase-9 and the effector caspase-3 and -7. Two additional IAP family members, cellular IAP1 (cIAP1) and cIAP2, were once thought to also inhibi...

2014
Sonu Kumar Bram J. van Raam Guy S. Salvesen Piotr Cieplak Shawn B. Bratton

Caspases are enzymes belonging to a conserved family of cysteine-dependent aspartic-specific proteases that are involved in vital cellular processes and play a prominent role in apoptosis and inflammation. Determining all relevant protein substrates of caspases remains a challenging task. Over 1500 caspase substrates have been discovered in the human proteome according to published data and new...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید