Work

Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1–Npl4

Year: 2018

Type: article

Source: Nature Structural & Molecular Biology

DOI: 10.1038/s41594-018-0085-x

Authors: Nicholas O. Bodnar, Kelly H. Kim, Zhejian Ji, Thomas E. Wales, Vladimir Svetlov, Evgeny Nudler, John R. Engen, Thomas Walz, Tom A. Rapoport

Institutions: Howard Hughes Medical Institute, Harvard University, Rockefeller University, Northeastern University, New York University

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Howard Hughes Medical Institute, University of California, San Francisco, National Institute of General Medical Sciences, National Center for Research Resources

Awards: Pixel Array Detector for X-ray Crystallography, Medical Scientist Training Program, NE-CAT Center for Advanced Macromolecular Crystallography, Protein Transport Across Membranes

OpenAlex ID: W2810410577

FWCI: 4.715

Cites: 71

Cited by: 101

Related to: 10