Patricia Kane, PhD
Chair and Professor
The central goals of scientists in the Biochemistry and Molecular Biology department are to research fundamental mechanisms in cells and organisms at the molecular level and to train the next generation of scientists. Read More...
Biochemistry and Molecular Biology
Rm. 4265, 766 Irving Ave.
Syracuse, NY 13210
Map & directions
Phone: 315 464-5127
Fax: 315 464-8750
Name: Patricia M Kane, PhD, Chair
The Department of Biochemistry and Molecular Biology offers a highly collaborative research community and an excellent training environment for young scientists.
The field of biochemistry and molecular biology has been transformed in the past decade with the sequencing of the human genome and genomes of other organisms, atomic resolution structures for many important macromolecules, and technological advances that allow integration of this information to address fundamental questions about the structure and function of cells and organisms. These developments create unprecedented opportunities for scientific research and understanding of human health and disease.
- Structure of Lipid Nanodisc-reconstituted Vacuolar ATPase Proton Channel: Defining the Interaction of Rotor and Stator
The Wilkens lab focuses on the structural characterization of the vacuolar ATPase (or V-ATPase) in order to elucidate its mechanism of activity and regulation. V-ATPase is a ubiquitous eukaryotic rotary proton pump that is foiund in the endomembrane system and serves to acidify a variety of intracellular compartments as well as the extracellular space in higher eukaryotes. V-ATPase is essential in animals; full loss of activity is embryonic lethal and partial loss of function has been associated with various human diseases including osteoporosis, male infertility, sensorineural deafness, diabetes and various cancers. Read more...
- The Smc5/6 complex at the crossroads of DNA replication, repair and recombination
Due to the imperfect “steric gate”, DNA polymerase intrinsically mis-incorporates not only mismatched deoxyribonucleosides monophosphates but also ribonucleoside monophosphates (rNMPs) during DNA replication at a rate of 10−7 and 4 × 10−4, respectively (1). To repair these DNA damages it requires specific recognition and excision proteins to remove the damage and create a single-stranded DNA (ssDNA) gap, followed by the DNA polymerase to fill the gap and the DNA ligase to seal the nick. Read more...
- New class of p53-reactivating compounds provides novel mechanism to treat cancer - August 2015
The "Guardian of the Genome," p53, is a tumor suppressing transcription factor that has long been recognized as perhaps the most important protein in human cancer. Approximately 50% of human cancers harbor mutations in p53, which render the protein inactive and unable to protect the cells from cancerous transformation. Read more...
- Mechanism of Ant1-induced human diseases unraveled by the Chen lab - July 2015
Mitochondria are the powerhouses of the cell. About 90% of the energy that cells need is produced in the form of ATP by the OXPHOS apparatus on the mitochondrial inner membrane. After it's synthesis by the F0F1 ATP-synthase, ATP is exported out of mitochondria via adenine nucleotide translocase (Ant) by exchanging with the cytosolic ADP. Read more...
- Using disease-associated mutations to understand the biochemical regulation of a multi-subunit histone methyltransferase complex - June 2014
Eukaryotic DNA is compacted into chromatin, which must be continually remodeled to allow for DNA processes such as transcription. The basic repeating unit of chromatin, the nucleosome, is composed of an octomer of histone proteins around which 147 base pairs of DNA is wrapped. One way chromatin remodeling is achieved is by posttransitional modification of histones. Read more...