Results 171 to 180 of about 576,865 (218)

Fibronectin1‐Expressing Subicular Circuits Selectively Govern the Retrieval of Novel Object Recognition

open access: yesAdvanced Science, EarlyView.
Fibronectin 1 (FN1)‐expressing subicular subpopulations encode novel object preference and selectively govern retrieval of novel object recognition (NOR) via affecting excitability of entorhinal‐projecting circuit through large conductance Ca2+‐activated potassium (BK) channel. ABSTRACT Novel object recognition (NOR), referring to the cognitive ability
Fan Fei   +15 more
wiley   +1 more source

Dengue Virus Capsid Protein Interaction With Nucleic Acids. [PDF]

open access: yesBiofactors
Silva NM   +7 more
europepmc   +1 more source

Targeting the PDK1/c‐Myc/SOX10 Signaling in Oligodendrocytes Alleviates Neuropathic Pain

open access: yesAdvanced Science, EarlyView.
This work reveals that oligodendrocyte homeostasis, mediated by PDK1, is a critical determinant of neuropathic pain (NPP) pathogenesis. Disruption of PDK1 in oligodendrocytes impairs SOX10‐dependent myelination programs through c‐Myc accumulation, leading to disrupted myelination and the pathophysiology of NPP.
Pingping Qiao   +7 more
wiley   +1 more source

Genome sequence of seven human herpes simplex virus 2 (HSV2) clinical isolates from Finland. [PDF]

open access: yesMicrobiol Resour Announc
Bowen CD   +5 more
europepmc   +1 more source

Agnuside Stabilizes the Complex I Assembly Factor NDUFAF6 to Reinforce Mitochondrial Efficiency and Thermogenic Responsiveness

open access: yesAdvanced Science, EarlyView.
ABSTRACT Brown and beige adipocytes dissipate energy as heat, yet effective strategies to enhance their mitochondrial efficiency remain limited. Here, we identify Agnuside (AGN) as a selective stabilizer of the complex I assembly factor NDUFAF6. AGN directly binds cytosolic NDUFAF6, suppresses its ubiquitination, prolongs its half‐life, and facilitates
Qingwen Zhao   +7 more
wiley   +1 more source

Protein Disulfide Isomerase Disassembles TDP‐43/G3BP1 Condensates and Antagonizes TDP‐43 Pathological Aggregates

open access: yesAdvanced Science, EarlyView.
Cytoplasmic aggregation of TDP‐43 is a common pathological feature in amyotrophic lateral sclerosis, frontotemporal lobar degeneration, and Alzheimer's disease with TDP‐43 pathology. This study reports that wild‐type PDI slows down phase separation of TDP‐43 through direct interaction with TDP‐43.
Jia‐Qi Liu   +14 more
wiley   +1 more source

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