2013 - Fellow of the American Association for the Advancement of Science (AAAS)
His scientific interests lie mostly in Cell biology, Endoplasmic reticulum, Endoplasmic-reticulum-associated protein degradation, Biochemistry and Chaperone. His biological study focuses on Transport protein. His Endoplasmic reticulum research integrates issues from SEC61 Translocon, Secretory protein and Cytosol.
His Secretory protein study combines topics in areas such as Unfolded protein response and Er associated degradation. The study incorporates disciplines such as Cytoplasm, Saccharomyces cerevisiae, Proteasome, Calnexin and Secretory pathway in addition to Endoplasmic-reticulum-associated protein degradation. The concepts of his Chaperone study are interwoven with issues in Heat shock protein, ATPase, Signal transduction, Binding site and Translocon.
Jeffrey L. Brodsky mainly investigates Cell biology, Endoplasmic reticulum, Biochemistry, Endoplasmic-reticulum-associated protein degradation and Chaperone. His research in Cell biology intersects with topics in Ubiquitin and Membrane protein. In his study, Sec61 is strongly linked to Secretory protein, which falls under the umbrella field of Endoplasmic reticulum.
Yeast, Saccharomyces cerevisiae, Mutant, Hsp70 and Apolipoprotein B are among the areas of Biochemistry where the researcher is concentrating his efforts. His studies deal with areas such as Integral membrane protein, Plasma protein binding, Protein degradation and Cystic fibrosis transmembrane conductance regulator as well as Endoplasmic-reticulum-associated protein degradation. His Chaperone study incorporates themes from Heat shock protein, ATPase and Biogenesis.
His primary scientific interests are in Cell biology, Endoplasmic reticulum, Endoplasmic-reticulum-associated protein degradation, Proteasome and Ubiquitin. His research integrates issues of Biochemistry and Membrane protein in his study of Cell biology. His research investigates the connection with Biochemistry and areas like Potassium channel which intersect with concerns in Intracellular.
Jeffrey L. Brodsky has included themes like Glycosylation, Biogenesis and Cellular homeostasis in his Endoplasmic reticulum study. His work on ERAD pathway as part of general Endoplasmic-reticulum-associated protein degradation study is frequently linked to Bartter syndrome, bridging the gap between disciplines. His studies in Ubiquitin integrate themes in fields like Small molecule, Protein degradation, Cystic fibrosis transmembrane conductance regulator and Calmodulin.
Jeffrey L. Brodsky mostly deals with Cell biology, Endoplasmic reticulum, Endoplasmic-reticulum-associated protein degradation, Proteasome and Membrane protein. Jeffrey L. Brodsky interconnects Secretion and Ubiquitin in the investigation of issues within Cell biology. His Endoplasmic reticulum research is multidisciplinary, relying on both Cellular homeostasis and Protein aggregation.
His Endoplasmic-reticulum-associated protein degradation research entails a greater understanding of Biochemistry. Jeffrey L. Brodsky specializes in Biochemistry, namely Chaperone. His Membrane protein study integrates concerns from other disciplines, such as Ubiquitin-Protein Ligases and Transmembrane domain.
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)
Daniel J. Klionsky;Amal Kamal Abdel-Aziz;Sara Abdelfatah;Mahmoud Abdellatif.
Autophagy (2021)
Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
Daniel J. Klionsky;Hagai Abeliovich;Patrizia Agostinis;Devendra K. Agrawal.
Autophagy (2008)
One step at a time: endoplasmic reticulum-associated degradation
Shruthi S. Vembar;Jeffrey L. Brodsky.
Nature Reviews Molecular Cell Biology (2008)
Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
Eric D. Werner;Jeffrey L. Brodsky;Ardythe A. McCracken.
Proceedings of the National Academy of Sciences of the United States of America (1996)
ER protein quality control and proteasome-mediated protein degradation.
Jeffrey L. Brodsky;Ardythe A. McCracken;Ardythe A. McCracken.
Seminars in Cell & Developmental Biology (1999)
Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
Shuh-ichi Nishikawa;Sheara W. Fewell;Yoshihito Kato;Jeffrey L. Brodsky.
Journal of Cell Biology (2001)
Cleaning Up: ER-Associated Degradation to the Rescue
Jeffrey L. Brodsky.
Cell (2012)
From CFTR biology toward combinatorial pharmacotherapy: expanded classification of cystic fibrosis mutations.
Gudio Veit;Radu G. Avramescu;Annette N. Chiang;Scott A. Houck.
Molecular Biology of the Cell (2016)
The Action of Molecular Chaperones in the Early Secretory Pathway
Sheara W. Fewell;Kevin J. Travers;Jonathan S. Weissman;Jeffrey L. Brodsky.
Annual Review of Genetics (2001)
The Requirement for Molecular Chaperones during Endoplasmic Reticulum-associated Protein Degradation Demonstrates That Protein Export and Import Are Mechanistically Distinct
Jeffrey L. Brodsky;Eric D. Werner;Maria E. Dubas;Jennifer L. Goeckeler.
Journal of Biological Chemistry (1999)
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