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Open AccessJournal ArticleDOI

Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation

TLDR
It is demonstrated that large oligomers of sHsps are necessary for chaperone action and resistance against oxidative stress whereas phosphorylation down-regulates these activities by dissociation of s Hsps complexes to tetramers.
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This article is published in Journal of Biological Chemistry.The article was published on 1999-07-02 and is currently open access. It has received 734 citations till now. The article focuses on the topics: Heat shock protein & Hsp27.

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Erk and p38 mapk-activated protein kinases: a family of protein kinases with diverse biological functions

TL;DR: The identities of the MK substrates indicate that they play important roles in diverse biological processes, including mRNA translation, cell proliferation and survival, and the nuclear genomic response to mitogens and cellular stresses.
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Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases

TL;DR: The mechanisms of MAPKAPK activation by the different MAPKs are reviewed and their physiological roles based on established substrates and recent discoveries are discussed.
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Hsp27 negatively regulates cell death by interacting with cytochrome c

TL;DR: Hsp27 binds to cytochrome c released from the mitochondria to the cytosol and prevents cy tochrome-c-mediated interaction of Apaf-1 with procaspase-9, which interferes specifically with the mitochondrial pathway of caspases-dependent cell death.
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Heat shock proteins: endogenous modulators of apoptotic cell death.

TL;DR: A review of apoptosis-regulatory function of HSPs concludes that HSP27 and HSP70 may participate in carcinogenesis and should be considered as suspects in the development of cancer.
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The Global Phosphorylation Landscape of SARS-CoV-2 Infection.

Mehdi Bouhaddou, +77 more
- 06 Aug 2020 - 
TL;DR: A quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells reveals dramatic rewiring of phosphorylation on host and viral proteins, revealing potential COVID-19 therapies.
References
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Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells

TL;DR: Results show that, depending on cellular context, activation of MAP kinase kinase is necessary and sufficient for cell differentiation or proliferation.
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Alpha-crystallin can function as a molecular chaperone

TL;DR: It is shown that alpha-crystallin refracts light and protects proteins from aggregation in the transparent eye lens and that in nonlens cells alpha-Crystallin may have other functions in addition to its capacity to suppress aggregation of proteins.
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Small heat shock proteins are molecular chaperones

TL;DR: It is shown that all sHsps investigated act as molecular chaperones in these folding reactions and at stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins.
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Transformation of mammalian cells by constitutively active MAP kinase kinase

TL;DR: It is found that constitutive activation of MAPKK is sufficient to promote cell transformation and is associated with highly tumorigenic in nude mice.
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Crystal structure of a small heat-shock protein.

TL;DR: The crystal structure of a small heat-shock protein from Methanococcus jannaschii, a hyperthermophilic archaeon is reported and it is shown that the monomeric folding unit is a composite β-sandwich in which one of the β-strands comes from a neighbouring molecule.
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