Results 191 to 200 of about 1,540,702 (294)

Palmitoyl Acyltransferase Zdhhc17 Promotes Functional Recovery After Spinal Cord Injury by Targeting the Nuclear Transport Factors Kpna2 and Ipo9

open access: yesAdvanced Science, EarlyView.
In this study, we demonstrate that Zdhhc17, acting as a PAT, suppresses neuronal apoptosis and promotes axon regeneration after injury, thereby enhancing functional recovery following SCI. In this context, Kpna2 and Ipo9 serve as novel palmitoylation substrates of Zdhhc17, whose palmitoylation prevents the injury‐induced degradation of their proteins ...
Meixuan Chen   +12 more
wiley   +1 more source

Structural Basis of Lymphangiogenic Receptor VEGFR‐3 Activation Mediated by Distinctive Clustering of the Ligand–Receptor Complex

open access: yesAdvanced Science, EarlyView.
VEGF‐C and its receptor VEGFR‐3 are critical for lymphangiogenesis. Cryo‐EM structures of the VEGFR‐3/VEGF‐C ectodomain complex reveal a canonical 2:2 ligand–receptor hetero‐tetramer that further assembles into higher‐order clusters beyond simple receptor dimerization.
Ryeongeun Cho   +6 more
wiley   +1 more source

Decoding the Neural Circuit Underlying Context‐Cue Association in Retrieval of Morphine Reward Memory

open access: yesAdvanced Science, EarlyView.
Contextual cues recruit the glutamatergic vCA1–dmPFC pathway to retrieve morphine reward memory by reshaping cell‐type‐specific prefrontal microcircuit activity. Distinct regulation of PV+ and SST+ interneurons defines this hippocampal–prefrontal mechanism.
Zhifeng Shi   +8 more
wiley   +1 more source

Nuclear IDH3A Drives Transcriptional Programs in Melanoma via the YBX1–JUN/FOS Axis

open access: yesAdvanced Science, EarlyView.
Genomic amplification drives aberrant nuclear localization of IDH3A in melanoma. Independent of its canonical metabolic activity, nuclear IDH3A cooperates with YBX1 to activate the c‐JUN/c‐FOS transcriptional program, while NONO facilitates its nuclear localization.
Juan Ran   +10 more
wiley   +1 more source

Ammonification Process Is Limited by Transformation of Medium Molecular Weight Nitrogenous Organics but Not Hydrolysis of Proteins

open access: yesAdvanced Science, EarlyView.
A multi‐level analytical framework, integrating protein‐level persistence analysis, nontargeted HRMS formula tracking, peptide‐level proteomics, and targeted monomer quantification under varying redox conditions, together with FMO calculations reveal that ammonification is limited by medium molecular weight nitrogenous multimers.
Jing Li   +4 more
wiley   +1 more source

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