Risk Factors and Treatments of Lymphoceles in Living Renal Transplants: A Single-Center Experience.

Objectives: This study aimed to determine interventions and identify risk factors for lymphocele formation following kidney transplant.

Materials And Methods: We conducted a retrospective review of 296 adult kidney transplants from 2010 to 2022 to investigate postoperative lymphocele formation. We divided patients into lymphocele cases and nonlymphocele cases.

Subsurface warming associated with Pacific Summer Water transport toward the Chukchi Borderland in the Arctic Ocean.

Recent rapid sea ice reduction in the Pacific sector of the Arctic Ocean is potentially associated with inflow of Pacific-origin water via the Bering Strait. For the first time, we detected remarkable subsurface warming around the Chukchi Borderland in the Arctic Ocean over the recent two decades (i.e.

Prediction of cccDNA dynamics in hepatitis B patients by a combination of serum surrogate markers.

Quantification of intrahepatic covalently closed circular DNA (cccDNA) is a key for evaluating an elimination of hepatitis B virus (HBV) in infected patients. However, quantifying cccDNA requires invasive methods such as a liver biopsy, which makes it impractical to access the dynamics of cccDNA in patients. Although HBV RNA and HBV core-related antigens (HBcrAg) have been proposed as surrogate markers for evaluating cccDNA activity, they do not necessarily estimate the amount of cccDNA.

Persistent Epstein-Barr Virus Infection of Epithelial Cells Leads to APOBEC3C Expression and Induces Mitochondrial DNA Mutations.

Upon infection with the virus, cells increase the expression of cytidine deaminase APOBEC3 family genes. This leads to the accumulation of C-to-T mutations in the replicating viral genome and suppresses viral propagation. In contrast, herpesviruses, including Epstein-Barr virus (EBV), express genes that counteract APOBEC3 during lytic infection.

Structural basis for hepatitis B virus restriction by a viral receptor homologue.

Macaque restricts hepatitis B virus (HBV) infection because its receptor homologue, NTCP (mNTCP), cannot bind preS1 on viral surface. To reveal how mNTCP loses the viral receptor function, we here solve the cryo-electron microscopy structure of mNTCP. Superposing on the human NTCP (hNTCP)-preS1 complex structure shows that Arg158 of mNTCP causes steric clash to prevent preS1 from embedding onto the bile acid tunnel of NTCP.