The AP-4 accessory protein tepsin exhibits multivalent binding to LC3B.

Saved in:
Bibliographic Details
Title: The AP-4 accessory protein tepsin exhibits multivalent binding to LC3B.
Authors: Cohen CI; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA., Kendall AK; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA., Wallace NS; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA., McCorkle ML; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA., Jackson LP; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA; Department of Biochemistry, Vanderbilt University, Nashville, TN, USA. Electronic address: lauren.p.jackson@vanderbilt.edu.
Source: Advances in biological regulation [Adv Biol Regul] 2026 Jan; Vol. 99, pp. 101124. Date of Electronic Publication: 2025 Oct 27.
Publication Type: Journal Article; Research Support, N.I.H., Extramural
Journal Info: Publisher: Elsevier Country of Publication: England NLM ID: 101572336 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2212-4934 (Electronic) Linking ISSN: 22124926 NLM ISO Abbreviation: Adv Biol Regul Subsets: MEDLINE
Database: MEDLINE Ultimate
Be the first to leave a comment!
You must be logged in first