Gino Cingolani, PhD

Contact Dr. Cingolani

233 South 10th Street
BLSB Room 826
Philadelphia, PA 19107

(215) 503-4573
(215) 923-2117 fax

Research and Clinical Interests
Molecular cell biology of Nucleocytoplasmic Transport; X-ray crystallography and biophysical analysis of viral DNA-pumping machinery; structure of multi-subunit ATP synthases.

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Publications

Most recent Peer-reviewed Publications

1. Atomic structure of dual-specificity phosphatase 26, a novel p53 phosphatase
2. Crystal structure of a Ba2+-bound gating ring reveals elementary steps in RCK domain activation
3. Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit €
4. Structure of P22 headful packaging nuclease
5. Small terminase couples viral DNA binding to genome-packaging ATPase activity
6. Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin α5
7. Atomic structure of bacteriophage Sf6 tail needle knob
8. The importin β binding domain as a master regulator of nucleocytoplasmic transport
9. A minimal Nuclear Localization Signal (NLS) in human phospholipid scramblase 4 that binds only the Minor NLS-binding site of importin α1
10. Structure of the ATP synthase catalytic complex (F 1) from Escherichia coli in an autoinhibited conformation
11. Erratum: Peering down the barrel of a bacteriophage portal: The genome packaging and release valve in P22 (Structure (2011) 18 (597-603))
12. Three-dimensional structure of a viral genome-delivery portal vertex
13. Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701
14. Three-dimensional structure of a viral genome-delivery portal vertex
15. Peering down the barrel of a bacteriophage portal: The genome packaging and release valve in P22
16. Crystallization of the nonameric small terminase subunit of bacteriophage P22
17. Phosphorylation meets nuclear import: A review
18. Molecular Basis for the Recognition of Phosphorylated STAT1 by Importin α5
19. Conformational selection in the recognition of the snurportin importin β binding domain by importin β
20. The importin β binding domain modulates the avidity of importin β for the nuclear pore complex

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