J. Goeckeler

Cloning, sequencing, and nucleolar targeting of the basal-body-binding nucleolar protein BN46/51.

J. Brodsky, C. Walsh, G. M. Trimbur, 1999, Journal of cell science.

Cloning , sequencing , and nucleolar targeting of the basal-body-binding nucleolar protein BN 46 / 51

J. Brodsky, C. Walsh, G. M. Trimbur, 1999 .

The Hsp110 Molecular Chaperone Stabilizes Apolipoprotein B from Endoplasmic Reticulum-associated Degradation (ERAD)*

E. Fisher, J. Brodsky, D. Habiel, 2007, Journal of Biological Chemistry.

The Requirement for Molecular Chaperones during Endoplasmic Reticulum-associated Protein Degradation Demonstrates That Protein Export and Import Are Mechanistically Distinct*

J. Brodsky, A. McCracken, M. Dubas, 1999, The Journal of Biological Chemistry.

BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.

R. Schekman, J. Brodsky, J. Goeckeler, 1995, Proceedings of the National Academy of Sciences of the United States of America.

The yeast Hsp110, Sse1p, exhibits high‐affinity peptide binding

G. Chiosis, J. Brodsky, Cristina C. Clement, 2008, FEBS letters.

The Function of the Yeast Molecular Chaperone Sse1 Is Mechanistically Distinct from the Closely Related Hsp70 Family*

J. Brodsky, K. Morano, L. Shaner, 2004, Journal of Biological Chemistry.

Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity.

J. Brodsky, A. Caplan, J. Goeckeler, 2002, Molecular biology of the cell.

Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum‐associated degradation

J. Brodsky, J L Brodsky, J L Goeckeler, 2010, Diabetes, obesity & metabolism.