Jenny R. Chang, Ph.D.
Affiliations: | 2009 | Biology | University of Alabama, Birmingham, Birmingham, AL, United States |
Area:
Virology BiologyGoogle:
"Jenny Chang"Parents
Sign in to add mentor| Terje Dokland | grad student | 2009 | UAB | |
| (Scaffolding-mediated capsid size determination in bacteriophages.) | ||||
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Publications
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| Lambert S, Yang Q, De Angelis RW, et al. (2016) Molecular Dissection of the Forces Responsible for Viral Capsid Assembly and Stabilization by Decoration Proteins. Biochemistry |
| Chang JR, Song EH, Nakatani-Webster E, et al. (2014) Phage lambda capsids as tunable display nanoparticles. Biomacromolecules. 15: 4410-9 |
| Spilman MS, Damle PK, Dearborn AD, et al. (2012) Assembly of bacteriophage 80α capsids in a Staphylococcus aureus expression system. Virology. 434: 242-50 |
| Chang JR, Andrews BT, Catalano CE. (2012) Energy-independent helicase activity of a viral genome packaging motor. Biochemistry. 51: 391-400 |
| Dearborn AD, Spilman MS, Damle PK, et al. (2011) The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination. Journal of Molecular Biology. 412: 710-22 |
| Spilman MS, Dearborn AD, Chang JR, et al. (2011) A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80α capsids. Journal of Molecular Biology. 405: 863-76 |
| Dearborn A, Spilman M, Damle P, et al. (2011) Staphylococcus aureus pathogenicity island 1 protein gp6, an internal scaffold in size determination Journal of Back and Musculoskeletal Rehabilitation |
| Spilman M, Dearborn A, Chang J, et al. (2011) Molecular Piracy via Capsid Size Determination by Staphylococcus aureus Pathogenicity Island 1 Microscopy and Microanalysis. 17: 132-133 |
| Chang JR, Spilman MS, Dokland T. (2010) Assembly of bacteriophage P2 capsids from capsid protein fused to internal scaffolding protein. Virus Genes. 40: 298-306 |
| Chang JR, Spilman MS, Rodenburg CM, et al. (2009) Functional domains of the bacteriophage P2 scaffolding protein: identification of residues involved in assembly and protease activity. Virology. 384: 144-50 |