Dual Specificity Phosphatases: From Molecular Mechanisms to Biological Function
Dual specificity phosphatases (DUSPs) constitute a heterogeneous group of protein tyrosine phosphatases with the ability to dephosphorylate Ser/Thr and Tyr residues from proteins, as well as from other non-proteinaceous substrates including signaling lipids. DUSPs include, among others, MAP kinase (...
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Format: | Electronic Book Chapter |
Language: | English |
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MDPI - Multidisciplinary Digital Publishing Institute
2019
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Online Access: | DOAB: download the publication DOAB: description of the publication |
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072 | 7 | |a PS |2 bicssc | |
100 | 1 | |a Pulido, Rafael |4 auth | |
700 | 1 | |a Lang, Roland |4 auth | |
245 | 1 | 0 | |a Dual Specificity Phosphatases: From Molecular Mechanisms to Biological Function |
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520 | |a Dual specificity phosphatases (DUSPs) constitute a heterogeneous group of protein tyrosine phosphatases with the ability to dephosphorylate Ser/Thr and Tyr residues from proteins, as well as from other non-proteinaceous substrates including signaling lipids. DUSPs include, among others, MAP kinase (MAPK) phosphatases (MKPs) and small-size atypical DUSPs. MKPs are enzymes specialized in regulating the activity and subcellular location of MAPKs, whereas the function of small-size atypical DUSPs seems to be more diverse. DUSPs have emerged as key players in the regulation of cell growth, differentiation, stress response, and apoptosis. DUSPs regulate essential physiological processes, including immunity, neurobiology and metabolic homeostasis, and have been implicated in tumorigenesis, pathological inflammation and metabolic disorders. Accordingly, alterations in the expression or function of MKPs and small-size atypical DUSPs have consequences essential to human disease, making these enzymes potential biological markers and therapeutic targets. This Special Issue covers recent advances in the molecular mechanisms and biological functions of MKPs and small-size atypical DUSPs, and their relevance in human disease. | ||
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650 | 7 | |a Biology, life sciences |2 bicssc | |
653 | |a hematopoietic cells | ||
653 | |a DEPArray | ||
653 | |a n/a | ||
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653 | |a liver steatosis | ||
653 | |a MAPK phosphatase | ||
653 | |a DUSP-4 | ||
653 | |a granule neurons | ||
653 | |a neuronal differentiation | ||
653 | |a DUSP10 | ||
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653 | |a asthma | ||
653 | |a E. coli infection | ||
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653 | |a triple-negative breast cancer (TNBC) | ||
653 | |a differentiation | ||
653 | |a HDAC6 (histone deacetylase isoform 6) | ||
653 | |a atypical dual-specificity phosphatases | ||
653 | |a microtubules | ||
653 | |a respiratory viruses | ||
653 | |a MK-STYX (MAPK (mitogen-activated protein kinase) phosphoserine/threonine/tyrosine-binding protein) | ||
653 | |a dual-specificity phosphatase | ||
653 | |a Msg5 | ||
653 | |a TLR signaling | ||
653 | |a mitogen-activated protein kinase | ||
653 | |a fungal MKPs | ||
653 | |a macrophages | ||
653 | |a MAP Kinase Phosphatase-2 | ||
653 | |a inflammation | ||
653 | |a Sdp1 | ||
653 | |a circulating tumor cells (CTCs) | ||
653 | |a MAP kinases | ||
653 | |a MAP kinase phosphatases | ||
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653 | |a integrated omics analysis | ||
653 | |a post-translational modification | ||
653 | |a rhinovirus | ||
653 | |a protein stability | ||
653 | |a ubiquitination | ||
653 | |a dual-specificity phosphatases | ||
653 | |a Mkp-1 | ||
653 | |a cancer | ||
653 | |a brain metastasis | ||
653 | |a HER2 | ||
653 | |a COPD | ||
653 | |a pseudophosphatase | ||
856 | 4 | 0 | |a www.oapen.org |u https://mdpi.com/books/pdfview/book/1856 |7 0 |z DOAB: download the publication |
856 | 4 | 0 | |a www.oapen.org |u https://directory.doabooks.org/handle/20.500.12854/45547 |7 0 |z DOAB: description of the publication |