refine search
Authors
Locations
Journals
Publication Dates
Find concepts in Knowledge Base
Explore current query
documentsstatisticstop authorclipboard
3 documents found
1: Title: Molecular basis of caspase-1 polymerization and its inhibition by a new capping mechanism.
Authors: Lu, Alvin, et.al. .
Journal: Nature structural & molecular biology (Nat Struct Mol Biol), Vol. 23 (5): 416-25, 2016 .
Snippet: In this study, we determined the structure of the human caspase-1 CARD domain (caspase-1(CARD)) filament by cryo-electron microscopy and investigated the biophysical properties of two caspase-1-like CARD-only proteins: human inhibitor of CARD (INCA or CARD17) and ICEBERG (CARD18).
Affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA. Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, Massachusetts, USA. Whitehead Institute for Biomedical Research, Cambridge, Massachusetts, USA. Center for Quantitative Biology, Peking-Tsinghua Joint Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Beijing, China. Department of Cancer Immunology and Virology, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA. Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA. .
Related Products: order online
2: Title: Oligomerized CARD16 promotes caspase-1 assembly and IL-1β processing.
Authors: Karasawa, Tadayoshi, et.al. .
Journal: FEBS open bio, Vol. 5, 2015 .
Snippet: Mutated CARD16D27G, mimicking the CARD17 amino acid sequence, formed a homo-oligomer but failed to form a filament-like structure.
Affiliation: Division of Inflammation Research, Center for Molecular Medicine, Jichi Medical University, Tochigi, Japan. Department of Molecular Oncology, Shinshu University Graduate School of Medicine, Nagano, Japan. .
Related Products: order online
3: Title: NLRC4 Inflammasome Is an Important Regulator of Interleukin-18 Levels in Patients With Acute Coronary Syndromes: Genome-Wide Association Study in the PLATelet inhibition and patient Outcomes Trial (PLATO).
Authors: Johansson, Åsa, et.al. .
Journal: Circulation. Cardiovascular genetics (Circ Cardiovasc Genet), Vol. 8 (3): 498-506, 2015 .
Snippet: CONCLUSIONS: Our results show that genetic variants play an important role in determining IL-18 levels in patients with acute coronary syndrome and we have identified genetic variants located in the IL-18 gene (IL18) or close to genes that are involved in procaspase-1 activation (NLRC4 and CARD16, CARD17, and CARD18).
Related Products: order online
Documents per page: 20 | 50 | 100