Johannes Rudolph - Nanotechnology

Author Information

J. Rudolph is affiliated with the Department of Biochemistry at the University of Colorado Boulder, Boulder, CO, United States. As a researcher in the field of nanotechnology, J. Rudolph has made significant contributions to understanding molecular mechanisms and protein dynamics, particularly focusing on PARP inhibitors and DNA damage repair mechanisms.

Research Contributions

J. Rudolph has authored numerous research papers that highlight significant advancements in the field of nanotechnology and biochemistry. The research primarily focuses on the mechanisms of PARP inhibitors, the dynamics of PARP1 and PARP2 during DNA damage, and the role of histone parylation factors. Notable works include studies on the architecture and assembly mechanism of human LACTB, dynamics revealed by live-cell single-molecule imaging, and the structural understanding of protein recruitment kinetics to DNA damage sites.

Aliases

Johannes Rudolph, John Rudolph, J. M. Rudolph, J Rudolph, J. Rudolph

Publication and Citation Metrics

Metric	Value
Citation Count	3151
h-index	32
Paper Count	93

Publications:

Architecture and Assembly Mechanism of Human LACTB

DOI: 10.1101/2022.04.21.489104

Year: 2022

PARP inhibitors trap PARP2 and alter the mode of recruitment of PARP2 at DNA damage sites

DOI: 10.1093/nar/gkac188

Year: 2022

Inhibitors of PARP: Number crunching and structure gazing

DOI: 10.1073/pnas.2121979119

Year: 2022

Dynamics of endogenous PARP1 and PARP2 during DNA damage revealed by live-cell single-molecule imaging

DOI: 10.1101/2022.03.12.484081

Year: 2022

Extracting Protein Recruitment Kinetics to DNA Damage using qFADD.py

DOI: 10.1016/J.BPJ.2020.11.712

Year: 2021

Histone Parylation factor 1 contributes to the inhibition of PARP1 by cancer drugs.

DOI: 10.1038/s41467-021-20998-8

Year: 2021

Author response: HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase

DOI: 10.7554/ELIFE.65773.SA2

Year: 2021

HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase

DOI: 10.7554/eLife.65773

Year: 2021

The BRCT Domain of PARP1 Binds Intact DNA and Mediates Intrastrand Transfer

DOI: 10.2139/ssrn.3883595

Year: 2021

The BRCT domain of PARP1 binds intact DNA and mediates intrastrand transfer.

DOI: 10.1016/j.molcel.2021.11.014

Year: 2021

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