Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alexander F.A. Keszei"'
Autor:
Apurva A. Govande, Sichen Shao, Rotem Sorek, Alexander F.A. Keszei, Gal Ofir, Adi Millman, B.R. Morehouse, Philip J. Kranzusch, B. Lowey
Publikováno v:
Nature
Stimulator of interferon genes (STING) is a receptor in human cells that senses foreign cyclic dinucleotides that are released during bacterial infection and in endogenous cyclic GMP-AMP signalling during viral infection and anti-tumour immunity1-5.
Discovery of C13-Aminobenzoyl Cycloheximide Derivatives that Potently Inhibit Translation Elongation
Autor:
Jason Murray, Brian B. Liau, Sichen Shao, Yumi Koga, Yongho Park, Eileen M Hoang, Alexander F.A. Keszei
Publikováno v:
J Am Chem Soc
Employed for over half a century to study protein synthesis, cycloheximide (CHX, 1) is a small molecule natural product that reversibly inhibits translation elongation. More recently, CHX has been applied to ribosome profiling, a method for mapping r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03d1e2aed01a92ff958bddfd9ac70104
https://europepmc.org/articles/PMC9482341/
https://europepmc.org/articles/PMC9482341/
Autor:
Matthew C.J. Yip, Qing Feng, Michael J. McKenna, Sichen Shao, Vincent Chu, Alexander F.A. Keszei
Publikováno v:
Nature Structural & Molecular Biology. 26:343-349
Aberrantly stalled ribosomes initiate the ribosome-associated quality control (RQC) and mRNA surveillance pathways for the degradation of potentially toxic peptides and faulty mRNAs. During RQC, ANKZF1 (yeast Vms1p) releases ubiquitinated nascent pro
Autor:
Sadie P. Antine, Amy S. Lee, Ian T. Mathews, B. Lowey, Mohit Jain, Victor J. Cabrera, John J. Mekalanos, Alexander F.A. Keszei, Frank Schwede, Aaron T. Whiteley, Sichen Shao, B.R. Morehouse, Percy Niemann, Dmitry Kashin, Philip J. Kranzusch
Publikováno v:
Cell. 182(1)
cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzymes are immune sensors that synthesize nucleotide second messengers and initiate antiviral responses in bacterial and animal cells. Here, we discover Enterobacter cloacae CD-NTase-associated protei
Autor:
Alexander F.A. Keszei, Carmel Avraham, Tevie Mehlman, B.R. Morehouse, Avigail Stokar-Avihail, Sichen Shao, Taya Fedorenko, Erez Yirmiya, Adi Millman, Rotem Sorek, Yaara Oppenheimer-Shaanan, Philip J. Kranzusch, Gil Amitai, Nitzan Tal, Alexander Brandis, Ehud Herbst
Publikováno v:
Cell
The cyclic pyrimidines 3',5'-cyclic cytidine monophosphate (cCMP) and 3',5'-cyclic uridine monophosphate (cUMP) have been reported in multiple organisms and cell types. As opposed to the cyclic nucleotides 3',5'-cyclic adenosine monophosphate (cAMP)
Autor:
Alexander F.A. Keszei, Pankaj Garg, Frank Sicheri, Sachdev S. Sidhu, Derek F. Ceccarelli, Igor Kurinov
Publikováno v:
J Mol Biol
Ubiquitin-conjugating E2 enzymes are central to the ubiquitination cascade and have been implicated in cancer and other diseases. Despite strong interest in developing specific E2 inhibitors, the shallow and exposed active site has proven recalcitran
Autor:
Frank Sicheri, Alexander F.A. Keszei
IpaH enzymes are secreted bacterial effectors that function within host cells as E3 ubiquitin (Ub) ligases. Catalytic activity is imparted by a conserved novel E3 ligase (NEL) domain that is unique to Gram-negative pathogens and whose activity is rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0798b134653a7d22c9c49be7c7a24c7c
https://europepmc.org/articles/PMC5307447/
https://europepmc.org/articles/PMC5307447/
Autor:
Xiaojing Tang, Mike Tyers, Craig McCormick, Elton Zeqiraj, Alexander F.A. Keszei, Frank Sicheri, John R. Rohde
Publikováno v:
Molecular and Cellular Biology. 34:362-373
IpaH proteins are bacterium-specific E3 enzymes that function as type three secretion system (T3SS) effectors in Salmonella, Shigella, and other Gram-negative bacteria. IpaH enzymes recruit host substrates for ubiquitination via a leucine-rich repeat
Publikováno v:
The Journal of biological chemistry. 287(1)
The IpaH family of novel E3 ligase (NEL) enzymes occur in a variety of pathogenic and commensal bacteria that interact with eukaryotic hosts. We demonstrate that the leucine-rich repeat (LRR) substrate recognition domains of different IpaH enzymes au