Results 61 to 70 of about 119,118 (204)

Puerarin‑Loaded pH‑Responsive ZIF‑90 Nanoparticles Ameliorate Osteoporosis via Enhancing H3K18 Lactylation and Suppressing Aberrant Osteoclast Activation

open access: yesAdvanced Science, EarlyView.
Schematic illustration of the mechanism by which ZIF‐90@PU alleviates osteoporosis via H3K18la‐mediated NFATc1 pathway suppression. ABSTRACT Osteoporosis is characterized by dysregulated osteoclast activity, leading to excessive bone resorption and structural damage.
Jiajia Lu   +5 more
wiley   +1 more source

Data_Sheet_5_Protein Lactylation Critically Regulates Energy Metabolism in the Protozoan Parasite Trypanosoma brucei.ZIP

open access: yes, 2021
Lysine lactylation has been recognized as a novel post-translational modification occurring on histones. However, lactylation in non-histone proteins, especially in proteins of early branching organisms, is not well understood.
Tiandong Guan (11561926)   +7 more
core   +1 more source

Bioenergetic Materials for Tissue Regeneration: Modulating Metabolism to Promote Cellular Anabolism

open access: yesAdvanced Science, EarlyView.
Bioenergetic materials (BEMs) modulate cellular metabolism to promote tissue regeneration. Their principal mechanisms of action include metabolic substrate supplementation, metabolic enzyme modulation, organelle transfer, electrical current regulation, redox homeostasis modulation, and oxygen tension modulation.
Yuchen He   +7 more
wiley   +1 more source

Non-histone lactylation in cancer: current advances and clinical implications

open access: yesFrontiers in Immunology
Lactylation, a novel post-translational modification characterized by the covalent attachment of lactate to specific lysine residues, has emerged as a critical metabolic regulator in cancer.
Robert Le Yang, Yiran Liang
doaj   +1 more source

Lactylation‐Mediated HER2 Stabilization Promotes Trastuzumab Resistance in Gastric Cancer

open access: yesAdvanced Science, EarlyView.
Warburg effect‐derived lactate drives HER2 lactylation and trastuzumab resistance. Mechanistically, AARS1‐mediated lactylation stabilizes HER2 by inhibiting USP11‐dependent degradation and concurrently promotes HER2‐EGFR interaction. Importantly, inhibiting HER2 lactylation resensitizes gastric cancer cells to trastuzumab.
Meng Qian   +11 more
wiley   +1 more source

Data_Sheet_4_Protein Lactylation Critically Regulates Energy Metabolism in the Protozoan Parasite Trypanosoma brucei.ZIP

open access: yes, 2021
Lysine lactylation has been recognized as a novel post-translational modification occurring on histones. However, lactylation in non-histone proteins, especially in proteins of early branching organisms, is not well understood.
Tiandong Guan (11561926)   +7 more
core   +1 more source

ACAT1‐Mediated SP1‐K694 Lactylation Promotes M1 Macrophage Polarization via TREM1 Transcription in COPD

open access: yesAdvanced Science, EarlyView.
Upon cigarette smoke exposure(CSE), LDHA expression is increased in lung macrophages, promoting the conversion of pyruvate to lactate and elevating the lactylation level of SP1 at the K694 site. This, in turn, enhances SP1 enrichment at the TREM1 promoter, increases TREM1 expression, promoted M1 macrophage polarization, and triggers the secretion of ...
Ling Lin   +5 more
wiley   +1 more source

Profiling of lysine lactylation

open access: yes
Tumor cells generate energy through glycolysis, and produces lactate as a byproduct. The lactate can be used as a substrate for lysine lactylation (Kla), a post-translational modification that may contribute to cell's survival and growth in certain ...
Haixia Tu (10180904)
core   +1 more source

Data_Sheet_3_Protein Lactylation Critically Regulates Energy Metabolism in the Protozoan Parasite Trypanosoma brucei.ZIP

open access: yes, 2021
Lysine lactylation has been recognized as a novel post-translational modification occurring on histones. However, lactylation in non-histone proteins, especially in proteins of early branching organisms, is not well understood.
Tiandong Guan (11561926)   +7 more
core   +1 more source

AARS2‐SIRT5‐Driven DLD K445 Lactylation Promotes Cuproptosis Resistance in Glioblastoma Stem Cells

open access: yesAdvanced Science, EarlyView.
Lactylation of DLD at K445 by AARS2 suppresses PDH complex activity and reduces DLAT lipoylation, thereby conferring cuproptosis resistance in glioblastoma stem cells. SIRT5‐mediated delactylation restores PDH function and enhances cuproptosis sensitivity.
Mingtian Ding   +12 more
wiley   +1 more source

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