Results 221 to 230 of about 774,968 (312)

OsNRT1.1B‐OsCNGC14/16‐Ca2+‐OsNLP3 Pathway: Phosphorylation‐Mediated Maintenance of Nitrogen Homeostasis

open access: yesAdvanced Science, EarlyView.
OsNRT1.1B forms a membrane complex with OsCNGC14/16 that mediates nitrate‐triggered calcium influx. This calcium signal phosphorylates OsNLP3 at Ser193, accelerating its nuclear translocation and activating nitrogen‐responsive genes. The calcium‐dependent pathway complements the established ubiquitination‐mediated pathway, dynamically regulating ...
Xiaohan Wang   +9 more
wiley   +1 more source

The CtrCBL1/CtrCIPK6 Complex of Citrus Phosphorylates CtrBBX32 to Regulate CtrSTP1‐Mediated Sugar Accumulation and Cold Tolerance

open access: yesAdvanced Science, EarlyView.
The CtrCBL1‐CtrCIPK6 module of trifoliate orange (Citrus trifoliata L.) phosphorylates CtrBBX32, triggering its protein degradation under cold conditions, thereby relieving CtrBBX32‐mediated transcriptional repression of CtrZAT10 and CtrSTP1. The consequent upregulation of CtrZAT10 further activates CtrSTP1 expression, which enhances hexose transport ...
Xiangming Shang   +10 more
wiley   +1 more source

Smart Gated Hollow Mesoporous Silica Hydrogel for Targeting Endoplasmic Reticulum Stress and Promoting Periodontal Tissue Regeneration

open access: yesAdvanced Science, EarlyView.
The hollow mesoporous silica loaded with quercetin (HM‐QU@PEG) is combined with a thermosensitive anti‐bacterial matrix (TF127) to prepare HQUP@TF127. HQUP@TF127 effectively eliminates excessive ROS, alleviates endoplasmic reticulum stress, relieves mitochondrial calcium overload, and blocks the p53‐dependent apoptotic cascade. Furthermore, it enhances
Guichun Wang   +14 more
wiley   +1 more source

A Case Report of a Novel Balanced Reciprocal Translocation t(2;14)(q11;q24) in a Young Woman with Two Pregnancy Losses [PDF]

open access: diamond, 2019
Mohammad Reza Farzaneh   +3 more
openalex   +1 more source

ATP Hydrolysis by α‐Synuclein Amyloids is Mediated by Enclosing β‐Strand

open access: yesAdvanced Science, EarlyView.
Pathological amyloids have been considered chemically inert until recently. Here it is shown that α‐synuclein amyloids catalyze the hydrolysis of the universal energy molecule, ATP. The cryo‐EM structure of the complex reveals an additional β‐strand (purple) that encloses the ATP‐binding site. Within the cavity, several lysine residues are required for
Lukas Frey   +6 more
wiley   +1 more source

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