News

Dr. Jeff Ranish Promoted to Professor

We are pleased to announce the promotion of Jeff Ranish to Professor. Jeff has been a pioneer in the fields of mass spectrometry and gene regulation. His impressive history of innovation in mass spectrometry technology has produced novel protein-crosslinking approaches to identify large scale protein-protein interactions in complex mixtures. He has applied the innovations to important biological problems, resulting in notable findings such as the characterization of multiple topological and functional regions within transcription factor TFIIH, identification of multiple regulatory factors in the system of liver X receptor-retinoic acid receptor (LXR-RXR) heterodimers, and a quantitative approach to identify amounts of transcription factors during erythropoiesis. Jeff’s numerous collaborations with leading biologists have maximized the impact of his technological advances and produced significant advances in the understanding of transcriptional regulation. We look forward to Jeff’s continued success with research efforts that combine technological innovation with rigorous experimentation, providing an indispensable bridge between molecular biology and the systems perspective at ISB.

Recent Articles

  • A Better Understanding of DNA Unpacking

    Jie Luo and Jeff Ranish collaborated on a project to determine the molecular architecture of the NuA4/Tip60 co-activator complex. This protein complex functions to allow proper control of gene expression and DNA repair by allowing other proteins to access the DNA in the cell nucleus. The new information about the structure and function of TIP60 could provide insight into different diseases where the protein complex plays a role, such as Alzheimer’s and various cancers. The work was published in Science.

  • Ranish lab published a preprint describing a new crosslinking mass spectrometry technology

    Dynamic conformational and structural changes in proteins and protein complexes play a central and ubiquitous role in the regulation of protein function, yet it is very challenging to study these changes, especially for large protein complexes, under physiological conditions. To address this challenge, we created a novel isobaric crosslinker, Qlinker, for studying conformational and structural changes in proteins and protein complexes using quantitative crosslinking mass spectrometry (qCLMS).

  • Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells

    Completing a years-long collaboration with the Taatjes and Kaplan labs, we publish an article in JBC that identifies key residues within the p52/Tfb2 subunit that control TFIIH function at transcription start sites in human and yeast cells.