Author

J. Pajak

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 4 Biochemistry· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Assay:cryo-EM· 4 Research Focus:protein folding & dynamics· 4 Research Focus:cell signaling & trafficking· 3 Approach:statistical model· 3 Organism:yeast· 3 Organism:bacteria (other)· 2 Approach:biophysical modeling· 2

Frequent Co-Authors

B. A. Kelch· 5 shared G. Arya· 4 shared X. Liu· 3 shared C. Gaubitz· 2 shared A. Bartesaghi· 1 shared B. J. Hilbert· 1 shared B. K. Cizubu· 1 shared E. Agnello· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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5 shared papersBiochemistry

B. A. Kelch

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Differences in clamp loader mechanism between bacteria and eukaryotes

J. T. Landeck, J. Pajak, E. K. Norman, E. L. Sedivy, B. A. Kelch

This study compares the clamp loader mechanism in bacteria and eukaryotes, revealing structural and functional differences in clamp opening and p/t-junction binding.

bioRxiv · Nov 30, 2023 · PreprintBiochemistry

Structure and assembly of an extremely long bacteriophage tail tube

E. Agnello, J. Pajak, X. Liu, B. A. Kelch

This study presents the structure of the P74-26 bacteriophage tail tube and proposes a model for its assembly mechanism based on cryo-EM data and complementary experiments.

bioRxiv · Oct 3, 2022 · PreprintBiophysics

A second DNA binding site on RFC facilitates clamp loading at gapped or nicked DNA

X. Liu, C. Gaubitz, J. Pajak, B. A. Kelch

This paper identifies a second DNA binding site in yeast RFC that facilitates clamp loading at nicked or gapped DNA, enhancing DNA repair processes.

bioRxiv · Jan 31, 2022Biochemistry

Molecular Dynamics of DNA Translocation by FtsK

J. Pajak, G. Arya

This study uses molecular simulations to reveal how FtsK coordinates DNA translocation with ATPase activity through conformational changes and force generation.

bioRxiv · Jan 3, 2022Biophysics

Cryo-EM structures reveal high-resolution mechanism of a DNA polymerase sliding clamp loader

C. Gaubitz, X. Liu, J. Pajak, N. P. Stone, J. A. Hayes, G. Demo, B. A. Kelch

The paper presents cryo-EM structures of the yeast clamp loader RFC bound to PCNA, revealing the mechanism of clamp opening and DNA binding without ATP hydrolysis.

bioRxiv · Sep 23, 2021Biochemistry

Redox sensitive E2 Rad6 controls cellular response to oxidative stress via K63 ubiquitination of ribosomes.

V. Simoes, L. Harley, B. K. Cizubu, Y. Zhou, J. Pajak, N. A. Snyder, J. Bouvette, M. J. Borgnia, G. Arya, A. Bartesaghi, G. M. Silva

The paper identifies Rad6 as a redox-sensitive E2 enzyme that modifies ribosomes with K63 ubiquitin during oxidative stress, linking it to translation control and stress response.

bioRxiv · Apr 22, 2021Cell Biology

Viral Packaging ATPases Utilize a Glutamate Switch to Couple ATPase Activity and DNA Translocation

J. Pajak, R. Atz, B. J. Hilbert, M. Morais, B. A. Kelch, P. Jardine, G. Arya

This study identifies a glutamate switch mechanism in viral packaging ATPases that couples ATP binding to DNA translocation through conformational changes.

bioRxiv · Dec 1, 2020Biophysics

A viral genome packaging motor transitions between cyclic and helical symmetry to translocate dsDNA

M. Woodson, J. Pajak, W. Zhao, W. Zhang, G. Arya, M. A. White, P. J. Jardine, M. C. Morais

The paper shows that viral DNA packaging motors switch between helical and planar symmetry to translocate double-stranded DNA.

bioRxiv · May 23, 2020Biophysics