Perspectives, Experiences, and Opportunities of Academic Surgeons in the Era of Healthcare Corporatization.

Objective: To characterize contemporary surgeons' viewpoints and perspectives on the academic mission during healthcare corporatization.

Summary Background Data: Academic surgery, traditionally driven by the tripartite missions of excellence in clinical care, scientific research, and education, faces increasing challenges from a corporatized healthcare environment. While previous studies have addressed the financial aspects of corporatization, a comprehensive evaluation of academic surgeons' attitudes and experiences remains lacking.

Perioperative Complications and Omission of Ureteral Stents During Robot-Assisted Radical Cystectomy With Intracorporeal Ileal Conduit.

Purpose: Ureteral stents are commonly placed intraoperatively during radical cystectomy, although their efficacy in reducing complications is unproven. We compared clinical outcomes among patients undergoing robot-assisted radical cystectomy with intracorporeal ileal conduit (RARC-IC) with or without ureteral stents to determine if omission of ureteral stents affects postoperative complications.

Materials And Methods: All RARC-IC surgeries performed at our institution between November 2017 and June 2023 were reviewed.

Programmable protein degraders enable selective knockdown of pathogenic β-catenin subpopulations and .

Aberrant activation of Wnt signaling results in unregulated accumulation of cytosolic β-catenin, which subsequently enters the nucleus and promotes transcription of genes that contribute to cellular proliferation and malignancy. Here, we sought to eliminate pathogenic β-catenin from the cytosol using designer ubiquibodies (uAbs), chimeric proteins composed of an E3 ubiquitin ligase and a target-binding domain that redirect intracellular proteins to the proteasome for degradation. To accelerate uAb development, we leveraged a protein language model (pLM)-driven algorithm called SaLT&PepPr to computationally design "guide" peptides with affinity for β-catenin, which were subsequently fused to the catalytic domain of a human E3 called C-terminus of Hsp70-interacting protein (CHIP).

Discovery of a single-subunit oligosaccharyltransferase that enables glycosylation of full-length IgG antibodies in .

Human immunoglobulin G (IgG) antibodies are one of the most important classes of biotherapeutic agents and undergo glycosylation at the conserved N297 site in the C2 domain, which is critical for IgG Fc effector functions and anti-inflammatory activity. Hence, technologies for producing authentically glycosylated IgGs are in high demand. While attempts to engineer for this purpose have been described, they have met limited success due in part to the lack of available oligosaccharyltransferase (OST) enzymes that can install linked glycans within the QYNST sequon of the IgG C2 domain.