Results 41 to 50 of about 76,328 (190)

Global analysis of lysine acetylation in strawberry leaves [PDF]

open access: yesFrontiers in Plant Science, 2015
Protein lysine acetylation is a reversible and dynamic post-translational modification. It plays an important role in regulating diverse cellular processes including chromatin dynamic, metabolic pathways, and transcription in both prokaryotes and eukaryotes.
Fang, Xianping   +10 more
openaire   +3 more sources

Hydrogel‐Based Airway‐on‐Tube With Perfusable Endothelial Lumen and Outward Epithelialization

open access: yesAdvanced Materials, EarlyView.
A hydrogel‐based airway‐on‐tube platform featuring a perfusable endothelial lumen and outward epithelialization is presented. The system supports primary human bronchial epithelial and lung microvascular endothelial coculture under air‐liquid interface conditions.
Ali Doryab   +8 more
wiley   +1 more source

Protein Lysine Acetylation [PDF]

open access: yesCellular and Molecular Gastroenterology and Hepatology, 2021
openaire   +4 more sources

Chronic Hypoxia Disrupts Spermatogenesis Through ASXL2–EZH2–Mediated Microtubule Destabilization

open access: yesAdvanced Science, EarlyView.
This study reveals the mechanism by which chronic hypoxia impairs spermatogenesis via the ASXL2–EZH2 axis, hindering the transition of spermatids from round to elongated forms. Key findings reveal that under hypoxic conditions, downregulated ASXL2 expression reduces EZH2 binding to the CEP162 promoter, leading to decreased H3K27me3 modification and ...
Jun Yin   +11 more
wiley   +1 more source

Lysine Acetylation Activates Mitochondrial Aconitase in the Heart [PDF]

open access: yesBiochemistry, 2015
High-throughput proteomics studies have identified several thousand acetylation sites on more than 1000 proteins. Mitochondrial aconitase, the Krebs cycle enzyme that converts citrate to isocitrate, has been identified in many of these reports. Acetylated mitochondrial aconitase has also been identified as a target for sirtuin 3 (SIRT3)-catalyzed ...
Jolyn, Fernandes   +6 more
openaire   +2 more sources

USP9X as a Candidate Mediator of Prenatal Aspirin‐Induced Ovarian Reserve Reduction in Offspring Mice

open access: yesAdvanced Science, EarlyView.
This study suggests that prenatal aspirin exposure is associated with reduced ovarian reserve in offspring, associated with HDAC1‐linked epigenetic downregulation of Usp9x as a candidate mechanism. These preclinical findings provide new insights into fetal‐origin ovarian disorders and contribute to the evidence base concerning aspirin's gestational ...
Yating Li   +11 more
wiley   +1 more source

Plant protein lysine acetylation

open access: yes, 2018
"December 2013." ; "A Dissertation presented to the Faculty of the Graduate School at the University of Missouri--Columbia In Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy." ; Dissertation supervisor: Dr. Ján A. Miernyk. ; Includes vita.
openaire   +2 more sources

Mammalian Proteome Profiling Reveals Readers and Antireaders of Strand‐Symmetric and ‐Asymmetric 5‐Hydroxymethylcytosine‐Modifications in DNA

open access: yesAdvanced Science, EarlyView.
We investigate by proteomics studies how strand‐symmetric and ‐asymmetric cytosine 5‐modifications in DNA are selectively recognized by the nuclear proteome. Using promoter probes with defined modification patterns, we identify tissue‐specific reader proteinsincluding MYC, MAX, and RFX5that discriminate 5‐hydroxymethylcytosine symmetry and sequence ...
Lena Engelhard   +8 more
wiley   +1 more source

Regulation of Cellular Metabolism by Protein Lysine Acetylation [PDF]

open access: yesScience, 2010
Metabolic Regulation Through Acetylation Covalent modification of lysine residues in various proteins in the nucleus is a recognized mechanism for control of transcription. Now two papers suggest that acetylation may represent an important regulatory mechanism controlling the function of metabolic enzymes (see the
Shimin, Zhao   +21 more
openaire   +2 more sources

PBRM1 Deficiency Reshapes an Immune Suppressive Microenvironment Through Epigenetic Tuning of PBRM1‐KDM5C‐IL6 Axis in ccRCC

open access: yesAdvanced Science, EarlyView.
PBRM1 ranks as the second most commonly mutated gene in ccRCC. This study reveals that PBRM1 loss promotes an immunosuppressive microenvironment by elevating M2 TAMs via the KDM5C–IL‐6 axis. These M2 TAMs, along with CAFs, form a barrier that excludes CD8+ T cells. Targeting IL‐6 synergizes with anti‐PD1 therapy, offering a promising strategy for PBRM1‐
Wenjiao Xia   +14 more
wiley   +1 more source

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