Daniel L. Minor
Biochemist Faculty Scientist
Research Interests
I have a broad background in ion channel structural biology and functional characterization. My interest in the physical chemistry of biological phenomena began with my undergraduate study in biophysics and biochemistry at the University of Pennsylvania. As a graduate student in the Department of Chemistry at MIT with Prof. Peter S. Kim, I focused on understanding the basic principles of protein folding and molecular interactions. While at MIT, I developed a keen interest in the proteins involved in electrical signaling. To pursue this interest, I worked as a postdoctoral fellow with Dr. Nigel Unwin at the LMB Cambridge and with Prof. Lily Y. Jan at UCSF where I was able to apply my background in structural biology to specific questions regarding ion channel structure and regulation. As a PI, I have focused my laboratory’s efforts on structural and mechanistic understanding of ion channels and in the development of new pharmacological tools for orphaned channel classes. My lab is pursing a research program that combines structural biology, ion channel functional studies, and chemical biology approaches to develop new channel pharmacologies. I am a Professor of Biochemistry and Biophysics and Cellular and Molecular Pharmacology, an Investigator in the Cardiovascular Research Institute at UCSF, and a Faculty Scientist at LBNL. My laboratory has made many contributions to the structural understanding of the function of various classes of ion channels and development of new channel modulators using a multidisciplinary approach employing genetic selections, biophysical approaches, chemical biology, and X-ray crystallography.
Recent Publications
Related News
A Frog Worth Kissing: Natural Defense Against Red Tide Toxin Found in Bullfrogs
A team led by Berkeley Lab faculty biochemist Daniel Minor has discovered how a protein produced by bullfrogs binds to and inhibits the action of saxitoxin, the deadly neurotoxin made by cyanobacteria and dinoflagellates that causes paralytic shellfish poisoning. The findings, published this week in Science Advances, could lead to the first-ever antidote for the compound, which blocks nerve signaling in animal muscles, causing death by asphyxiation when consumed in sufficient quantities.
ALS-ENABLE Helps Decode a Calcium-dependent Switch
The Kv7 family of voltage-gated potassium channels control excitability in the heart, brain, and ear, and harbor mutations associated with arrhythmias, epilepsy, and deafness. A recent study, led by Molecular Biophysics and Integrated Bioimaging (MBIB) faculty scientist Daniel Minor’s group in the Cardiovascular Research Institute at UCSF, used both diffraction and scattering beamlines of ALS-ENABLE to reveal a universal switch mechanism by which the calcium sensor protein calmodulin controls the action of these channels. The findings, reported in the journal Neuron, provide a key link between Kv7 channel activity and cellular signaling pathways. Greg Hura, a research scientist in MBIB, was also a co-author on the paper. Watch a video detailing the work.
