D. Krylov

发表

Cell-Type-Dependent Activity of the Ubiquitous Transcription Factor USF in Cellular Proliferation and Transcriptional Activation

C. Vinson, T. Lu, Y. Qyang, 1999, Molecular and Cellular Biology.

SREBP-1 Dimerization Specificity Maps to Both the Helix-Loop-Helix and Leucine Zipper Domains

S. Mandrup, C. Vinson, V. Rishi, 2004, Journal of Biological Chemistry.

Cellular Internalization and Degradation of Thrombospondin-1 Is Mediated by the Amino-terminal Heparin Binding Domain (HBD)

I. Mikhailenko, D. Strickland, D. Roberts, 1997, The Journal of Biological Chemistry.

Tissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin

S. Akimov, A. Belkin, D. Krylov, 2000, The Journal of cell biology.

Design of dominant negatives to bHLHZip proteins that inhibit DNA binding.

C. Vinson, E. Taparowsky, D. Krylov, 1997, Current topics in microbiology and immunology.

A Dominant-Negative Inhibitor of CREB Reveals that It Is a General Mediator of Stimulus-Dependent Transcription of c-fos

D. Ginty, M. Olive, C. Vinson, 1998, Molecular and Cellular Biology.

A Dominant Negative to Activation Protein-1 (AP1) That Abolishes DNA Binding and Inhibits Oncogenesis*

M. Olive, C. Vinson, K. Gardner, 1997, The Journal of Biological Chemistry.

Extending dimerization interfaces: the bZIP basic region can form a coiled coil.

M. Olive, C. Vinson, C. Vinson, 1995, The EMBO journal.

A general method to design dominant negatives to B-HLHZip proteins that abolish DNA binding.

C. Vinson, C. Vinson, E. Taparowsky, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Direct transmembrane clustering and cytoplasmic dimerization of focal adhesion kinase initiates its tyrosine phosphorylation.

Kenneth M. Yamada, C. Vinson, J. Gutkind, 2002, Biochimica et biophysica acta.

Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids.

C. Vinson, J. Barchi, D Krylov, 1998, Journal of molecular biology.

Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil.

C. Vinson, L. Szilák, D Krylov, 1997, Biochemistry.

A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.

C. Vinson, I. Mikhailenko, D Krylov, 1994, The EMBO journal.

Phosphorylation destabilizes α-helices

C. Vinson, L. Szilák, J. Moitra, 1997, Nature Structural Biology.

Life without white fat: a transgenic mouse.

M. Olive, M. Reitman, O. Gavrilova, 1998, Genes & development.

Phosphorylation destabilizes alpha-helices.

C. Vinson, L. Szilák, J. Moitra, 1997, Nature structural biology.

Purification of myristoylated and nonmyristoylated neuronal calcium sensor-1 using single-step hydrophobic interaction chromatography.

A. Jeromin, J. Hurley, Y. Sharma, 2000, Protein expression and purification.