Shelly Rozen
Papers
1
Total Citations
32
H-Index
1
About
Shelly Rozen is a structural biologist whose work has significantly advanced the understanding of protein complex architecture through innovative mass spectrometry techniques. Her research centers on the subunit diversity and dynamic assembly of macromolecular machines, particularly within the ubiquitin-proteasome system and chromatin remodeling complexes. Rozen’s major contribution lies in developing and applying native mass spectrometry approaches to expose the compositional heterogeneity of protein complexes, revealing how variations in subunit stoichiometry and post-translational modifications dictate functional specificity. Her landmark 2013 paper, "Exposing the subunit diversity within protein complexes: A mass spectrometry approach," has garnered 32 citations, establishing a methodological framework that bridges structural biology and proteomics. This work has been instrumental in characterizing the assembly pathways of the 26S proteasome and the SAGA complex, offering insights into how subunit exchange regulates cellular processes. Rozen’s achievements include pioneering the use of ion mobility-mass spectrometry to resolve coexisting conformations of large assemblies, a technique now widely adopted. Her research continues to illuminate the molecular logic of protein complex organization, making her a key figure in the field of integrative structural biology.
Research Focus
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Top Papers
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