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Di (2-ethylhexyl) phthalate reduces sperm motility by decreasing sperm tail energy supply.
Ecotoxicol Environ Saf
January 2025
Department of Toxicology, School of Public Health; Suzhou Hospital of Anhui Medical University, Hefei 230032, China; Key Laboratory of Environmental Toxicology of Anhui Higher Education Institutes, Hefei 230032, China. Electronic address:
Di (2-ethylhexyl) phthalate (DEHP) is widespread in the environment. It can impair sperm function through damaging the sperm development process. However, few studies have focused on the sperm tail that is directly related to sperm motility.
View Article and Find Full Text PDFTEG-Guided Anticoagulation Assessment in Deep Vein Arterialization: A Prospective Analysis.
Ann Vasc Surg
December 2024
Division of Vascular and Endovascular Surgery, Massachusetts General Hospital, Boston, MA. Electronic address:
Background: Deep vein arterialization (DVA) is an innovative surgical technique aimed at enhancing blood flow in compromised limbs facing amputation. Maintenance of flow postrevascularization is crucial to limb salvage. As this is a new technique, no standardized thromboprophylaxis regime is currently established, and postprocedure thromboprophylaxis is at the discretion of the proceduralist.
View Article and Find Full Text PDFATAD5-BAZ1B interaction modulates PCNA ubiquitination during DNA repair.
Nat Commun
December 2024
Center for Genomic Integrity, Institute for Basic Science, Ulsan, 44919, Republic of Korea.
Article Synopsis
- Mono-ubiquitinated PCNA (mono-Ub-PCNA) helps the DNA replication process bypass obstacles and DNA damage but must be de-ubiquitinated to continue accurate DNA synthesis.
- The protein ATAD5, along with the UAF1-USP1 complex, is responsible for the de-ubiquitination of Ub-PCNA, but the regulation of this process was previously unclear.
- Research shows that BAZ1B, part of a chromatin-remodeling complex, is critical for controlling Ub-PCNA de-ubiquitination; loss of its interaction with ATAD5 can lead to premature de-ubiquitination and increased sensitivity to oxidative stress.
Mutation of a highly conserved isoleucine residue in loop 2 of several β-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for replication.
J Virol
November 2024
Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas, USA.
Unlabelled: All coronaviruses (CoVs) encode for a conserved macrodomain (Mac1) located in non-structural protein 3. Mac1 is an ADP-ribosylhydrolase that binds and hydrolyzes mono-ADP-ribose from target proteins. Previous work has shown that Mac1 is important for virus replication and pathogenesis.
View Article and Find Full Text PDFADP-ribose hydrolases: biological functions and potential therapeutic targets.
Expert Rev Mol Med
October 2024
State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, P. R. China.
ADP-ribosylation (ADPRylation), which encompasses poly(ADP-ribosyl)ation and mono(ADP-ribosyl)ation, is an important post-translational modification catalysed by the poly(ADP-ribose) polymerase (PARP) enzyme superfamily. The process involves writers (PARPs) and erasers (ADP-ribose hydrolases), which work together to precisely regulate diverse cellular and molecular responses. Although the PARP-mediated synthesis of ADP-ribose (ADPr) has been well studied, ADPr degradation by degrading enzymes deserves further investigation.
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