Results 221 to 230 of about 1,406,847 (366)

Global phosphoproteome analysis identifies PeVYV P4-induced host protein phosphorylation changes that facilitate viral proliferation. [PDF]

open access: yesBMC Plant Biol
Li S   +12 more
europepmc   +1 more source

Multi‐omics and low‐input proteomics profiling reveals dynamic regulation driving pluripotency initiation in early mouse embryos

open access: yesFEBS Open Bio, EarlyView.
Mouse pre‐implantation development involves a transition from totipotency to pluripotency. Integrating transcriptomics, epigenetic profiling, low‐input proteomics and functional assays, we show that eight‐cell embryos retain residual totipotency features, whereas cytoskeletal remodeling regulated by the ubiquitin‐proteasome system drives progression ...
Wanqiong Li   +8 more
wiley   +1 more source

Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics. [PDF]

open access: yesElife
Peshkin L   +7 more
europepmc   +1 more source

BMI‐1 modulation and trafficking during M phase in diffuse intrinsic pontine glioma

open access: yesFEBS Open Bio, EarlyView.
The schematic illustrates BMI‐1 phosphorylation during M phase, which triggers its translocation from the nucleus to the cytoplasm. In cycling cells, BMI‐1 functions within the PRC1 complex to mediate H2A K119 monoubiquitination. Following PTC596‐induced M phase arrest, phosphorylated BMI‐1 dissociates from PRC1 and is exported to the cytoplasm via its
Banlanjo Umaru   +6 more
wiley   +1 more source

A Critical Function for Ser-282 in Cardiac Myosin Binding Protein-C Phosphorylation and Cardiac Function [PDF]

open access: bronze, 2011
Sakthivel Sadayappan   +14 more
openalex   +1 more source

C2α‐carbanion‐protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2‐hydroxyacyl‐CoA lyase

open access: yesFEBS Open Bio, EarlyView.
Enzymes of the 2‐hydroxyacyl‐CoA lyase group catalyze the condensation of formyl‐CoA with aldehydes or ketones. Thus, by structural adaptation of active sites, practically any pharmaceutically and industrially important 2‐hydroxyacid could be biotechnologically synthesized. Combining crystal structure analysis, active site mutations and kinetic assays,
Michael Zahn   +4 more
wiley   +1 more source

Patatin‐domain‐containing (phospho)lipases under control: Mammalian co‐regulators and pathogenic activation mechanisms

open access: yesFEBS Open Bio, EarlyView.
Patatin domain‐containing (phospho)lipases are lipid‐hydrolyzing enzymes central to metabolism, membrane remodeling, and signaling. Their activity relies on precise co‐activation mechanisms involving protein–protein interactions and conformational rearrangements.
Noopur Dubey   +2 more
wiley   +1 more source

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