Results 251 to 260 of about 578,436 (295)
Some of the next articles are maybe not open access.
2013
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 800 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
Dorstyn, L., Kumar, S.
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The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 800 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
Dorstyn, L., Kumar, S.
openaire +3 more sources
2008
The main effectors of apoptosis encompass proteases from the caspase family, which reside as latent precursors in most nucleated animal cells. The apoptotic caspases constitute a minimal two-step signaling pathway. The apical (initiator) caspases are activated within oligomeric signaling complexes in response to apoptotic stimuli.
Guy S, Salvesen, Stefan J, Riedl
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The main effectors of apoptosis encompass proteases from the caspase family, which reside as latent precursors in most nucleated animal cells. The apoptotic caspases constitute a minimal two-step signaling pathway. The apical (initiator) caspases are activated within oligomeric signaling complexes in response to apoptotic stimuli.
Guy S, Salvesen, Stefan J, Riedl
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The International Journal of Biochemistry & Cell Biology, 2000
Caspase-9 is a member of caspase family of cysteine proteases that have been implicated in apoptosis and cytokine processing. When cells receive apoptotic stimuli, mitochondria releases cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP.
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Caspase-9 is a member of caspase family of cysteine proteases that have been implicated in apoptosis and cytokine processing. When cells receive apoptotic stimuli, mitochondria releases cytochrome c which then binds to Apaf-1, the mammalian Ced-4 homologue, together with dATP.
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2014
Caspase-2 has been shown to function in apoptosis and in some non-apoptotic pathways, including tumor suppression and aging. Caspase-2 has some unique features and is the only caspase that constitutively localizes to the nucleus, although its nuclear function remains unknown.
Dorstyn, L., Kumar, S.
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Caspase-2 has been shown to function in apoptosis and in some non-apoptotic pathways, including tumor suppression and aging. Caspase-2 has some unique features and is the only caspase that constitutively localizes to the nucleus, although its nuclear function remains unknown.
Dorstyn, L., Kumar, S.
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Caspase cascades and caspase targets
2000Apoptosis is an evolutionarily conserved form of cell suicide. Cells that die by apoptosis are disassembled in a stereotypical manner resulting in a characteristic ‘apoptotic morphology’. It was this characteristic, uniform morphology displayed by cells during apoptosis which led to the assumption that cells contain a similar execution machinery ...
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Recognition and maturation of IL-18 by caspase-4 noncanonical inflammasome
Nature, 2023Yanjie Hou, Yong Cao, Meng-Qiu Dong
exaly
Caspase-6 Is a Key Regulator of Innate Immunity, Inflammasome Activation, and Host Defense
Cell, 2020Min Zheng, Rajendra Karki, Peter Vogel
exaly
Molecular mechanisms of caspase regulation during apoptosis
Nature Reviews Molecular Cell Biology, 2004Yigong Shi
exaly

