Richard Mann

Richard Mann

Titles

Higgins Professor of Biochemistry and Molecular Biophysics

Affiliations

Department of Biochemistry and Molecular Biophysics
Department of Systems Biology

Phone

(212) 305-7731

Richard Mann is the Higgins Professor of Biochemistry and Molecular Biophysics, and holds an Interdisciplinary Faculty appointment in the Department of Systems Biology. He uses the fruit fly Drosophila melanogaster as a model system for studying a range of problems related to how transcription factors coordinate complex processes during animal development. The lab is particularly interested in the Hox family of homeodomain genes, which code for transcription factors that specifiy tissue and cellular identities across the animal kingdom. The Hox projects address how these transcription factors are able to specifically regulate their target genes during development. Their studies have also focused on motor neuron differentiation in the fly leg, the development of the proximal-distal axis in leg development, and the regulation of tissue growth and organ size. In collaborations with Barry Honig and Harmen Bussemaker, the Mann Lab is also developing novel computational tools to discover transcriptional regulatory regions and analyze DNA binding specificities on a global scale.

More News

News

Four Columbia Systems Biology Papers Named among Top Publications
The ISCB/RECOMB Conference on Regulatory and Systems Genomics has announced its top 10 papers of 2014-2015. Four of them involve investigators from the Columbia University Department of Systems Biology.
Three CUMC Faculty Members Receive Interdisciplinary Appointments
Columbia University Medical Center professors Oliver Hobert, Richard Mann, and Rodney Rothstein have joined the Department of Systems Biology to facilitate collaborative research.
Structural Nuance in the Double Helix and its Biological Role
In two recent papers in Cell and Nature, Barry Honig, Richard Mann, and colleagues have shown that sequence-dependent variations in the helix shape allow DNA-binding proteins to recognize their specific binding sites.