John R. Zupan

发表

Tobacco mosaic virus movement protein associates with the cytoskeleton in tobacco cells.

P. Zambryski, B. McLean, J. Zupan, 1995, The Plant cell.

Phosphorylation of tobacco mosaic virus cell-to-cell movement protein by a developmentally regulated plant cell wall-associated protein kinase.

V. Citovsky, P. Zambryski, B. McLean, 1993, Genes & development.

The transfer of DNA from agrobacterium tumefaciens into plants: a feast of fundamental insights.

P. Zambryski, T. Muth, P Zambryski, 2000, The Plant journal : for cell and molecular biology.

The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: Implications for nuclear uptake of DNA in plant cells

V. Citovsky, P. Zambryski, J. Zupan, 1992, Cell.

The Agrobacterium DNA Transfer Complex

V. Citovsky, P. Zambryski, J. Zupan, 1997 .

Assembly of the VirB transport complex for DNA transfer from Agrobacterium tumefaciens to plant cells.

P. Zambryski, J. Zupan, D. Ward, 1998, Current opinion in microbiology.

Agrobacterium VirE2 protein mediates nuclear uptake of single-stranded DNA in plant cells.

V. Citovsky, P. Zambryski, J. Zupan, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Nuclear localization of Agrobacterium VirE2 protein in plant cells.

V. Citovsky, P. Zambryski, J. Zupan, 1992, Science.

Transfer of T-DNA from Agrobacterium to the Plant Cell

P. Zambryski, J. Zupan, J. R. Zupan, 1995, Plant physiology.

Dynamic FtsA and FtsZ localization and outer membrane alterations during polar growth and cell division in Agrobacterium tumefaciens

P. Zambryski, James Anderson-Furgeson, Todd A. Cameron, 2013, Proceedings of the National Academy of Sciences.

VirB1* Promotes T-Pilus Formation in the vir-Type IV Secretion System of Agrobacterium tumefaciens

P. Zambryski, J. Zupan, Cheryl A Hackworth, 2007, Journal of bacteriology.

The N- and C-Terminal Portions of theAgrobacterium VirB1 Protein Independently Enhance Tumorigenesis

C. Baron, P. Zambryski, M. Llosa, 2000, Journal of bacteriology.

Peptidoglycan Synthesis Machinery in Agrobacterium tumefaciens During Unipolar Growth and Cell Division

P. Zambryski, J. Zupan, J. Zik, 2014, mBio.

Loss of PodJ in Agrobacterium tumefaciens Leads to Ectopic Polar Growth, Branching, and Reduced Cell Division

P. Zambryski, R. Grangeon, J. Zupan, 2016, Journal of bacteriology.

PopZ identifies the new pole, and PodJ identifies the old pole during polar growth in Agrobacterium tumefaciens

P. Zambryski, R. Grangeon, J. Zupan, 2015, Proceedings of the National Academy of Sciences.

Membrane and Core Periplasmic Agrobacterium tumefaciens Virulence Type IV Secretion System Components Localize to Multiple Sites around the Bacterial Perimeter during Lateral Attachment to Plant Cells

P. Zambryski, J. Zupan, J. Aguilar, 2011, mBio.

Agrobacterium type IV secretion system and its substrates form helical arrays around the circumference of virulence-induced cells

P. Zambryski, J. Zupan, J. Aguilar, 2010, Proceedings of the National Academy of Sciences.

The essential features and modes of bacterial polar growth.

P. Zambryski, J. Zupan, T. Cameron, 2015, Trends in microbiology.

GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape in Agrobacterium tumefaciens

P. Zambryski, R. Grangeon, J. Zupan, 2019, Proceedings of the National Academy of Sciences.

Loss of PopZAt activity in Agrobacterium tumefaciens by Deletion or Depletion Leads to Multiple Growth Poles, Minicells, and Growth Defects

P. Zambryski, R. Grangeon, J. Zupan, 2017, mBio.

Agrobacterium tumefaciens Growth Pole Ring Protein: C Terminus and Internal Apolipoprotein Homologous Domains Are Essential for Function and Subcellular Localization

P. Zambryski, J. Zupan, Zisheng Guo, 2021, mBio.

Segregation of four Agrobacterium tumefaciens replicons during polar growth: PopZ and PodJ control segregation of essential replicons

P. Zambryski, J. Zupan, A. Chávez-Arroyo, 2020, Proceedings of the National Academy of Sciences.

TOUSLED Is a Nuclear Serine/Threonine Protein Kinase That Requires a Coiled-coil Region for Oligomerization and Catalytic Activity*

T. Durfee, P. Repetti, P. Zambryski, 1997, The Journal of Biological Chemistry.