Results 21 to 30 of about 200 (78)

The dead phosphatases society: a review of the emerging roles of pseudophosphatases

open access: yesThe FEBS Journal, Volume 287, Issue 19, Page 4198-4220, October 2020., 2020
Phosphatases are signaling enzymes that remove phosphate from proteins, lipids and other cellular components. A significant fraction of the human phosphatases bear mutations in one or several catalytic motifs. These members are referred to as pseudophosphatases and are present in most subfamilies of the phosphatome.
Veronika Reiterer   +5 more
wiley   +1 more source

Caenorhabditis elegans phosphatase complexes in UniProtKB and Complex Portal

open access: yesThe FEBS Journal, Volume 287, Issue 13, Page 2664-2684, July 2020., 2020
The UniProt Knowledgebase (UniProtKB) and Complex Portal databases facilitate the understanding of how protein phosphorylation is regulated by providing structural and functional information on phosphatase‐containing macromolecular complexes across a wide range of species.
Hema Bye‐A‐Jee   +4 more
wiley   +1 more source

Identity and functions of inorganic and inositol polyphosphates in plants

open access: yesNew Phytologist, Volume 225, Issue 2, Page 637-652, January 2020., 2020
Summary Inorganic polyphosphates (polyPs) and inositol pyrophosphates (PP‐InsPs) form important stores of inorganic phosphate and can act as energy metabolites and signaling molecules. Here we review our current understanding of polyP and inositol phosphate (InsP) metabolism and physiology in plants.
Laura Lorenzo‐Orts   +2 more
wiley   +1 more source

The enzymes of human diphosphoinositol polyphosphate metabolism

open access: yesThe FEBS Journal, Volume 281, Issue 1, Page 14-33, January 2014., 2014
This review covers the three classes of enzymes involved in the metabolism of diphosphoinositol polyphosphates – inositol hexakisphosphate kinases (IP6K), inositol hexakisphosphate and diphosphoinositol‐pentakisphosphate kinases (PPIP5K), and diphosphoinositol polyphosphate phosphohydrolases (DIPP).
Mark P. Thomas, Barry V. L. Potter
wiley   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

open access: yesFEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

CRISPR/Cas9‐edited tumor‐associated immune cells in cancer immunotherapy

open access: yesVIEW, Volume 6, Issue 5, October 2025.
The recent advancements in the application of CRISPR/Cas9‐edited tumor‐associated immune cells in cancer therapy are summarized, including T lymphoid cells, natural killer cells, macrophages, and B lymphoid cells et al., exhibiting a potential impact on the pathological status of cancer. This review also addresses the current challenges associated with
Yuhui Ma   +6 more
wiley   +1 more source

Enhancing inositol pyrophosphate accumulation in plants alters growth, phosphate homeostasis, and insect herbivory

open access: yesThe Plant Journal, Volume 123, Issue 1, July 2025.
SUMMARY Phosphate (Pi) is a critical nutrient for plants and is often a limiting factor in food production, as many agricultural soils are limited in available Pi. Inositol pyrophosphates (PP‐InsPs) are signaling molecules involved in Pi sensing and jasmonic acid (JA)‐regulated plant defense. Here, we report that overexpression of 1,3,4‐trisphosphate 5/
Caitlin Cridland   +7 more
wiley   +1 more source

Characterization of PPIP5Ks using pharmacological and chemical biology approaches

open access: yes
This thesis describes the development of a chemical tool directed against the kinase domain of PPIP5K. Furthermore, the functions of the phosphatase domain were biochemically characterized, complementing structural investigations. A high-throughput screening was carried out to identify lead structures for PPIP5K2 kinase inhibitors, yielding a single ...
openaire   +1 more source

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