Author

R. Augustyniak

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

Biology Disciplines

Click to filter author papers

Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 2 Assay:cryo-EM· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Organism:mouse· 1 Organism:rat· 1

Frequent Co-Authors

I. Lewandowska· 2 shared J. I. Sulkowska· 2 shared A. Kluza· 1 shared A. P. Perlinska· 1 shared B. Belza· 1 shared F. Bruno da Silva· 1 shared J. L. Rubinstein· 1 shared L. E. Kay· 1 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiophysics

I. Lewandowska

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Nucleolar Essential Protein 1 (Nep1): Elucidation of Enzymatic Catalysis Mechanism by Combined Molecular Dynamics Simulation and Quantum Chemical Calculations

M. Jedrzejewski, B. Belza, I. Lewandowska, M. Sadlej, A. P. Perlinska, R. Augustyniak, T. Christian, Y.-M. Hou, M. Kalek, J. I. Sulkowska

This study elucidates the catalytic mechanism of Nep1 using molecular dynamics and quantum chemical calculations, revealing that water mediates proton transfer rather than a conserved serine residue.

bioRxiv · Mar 21, 2023 · PreprintBiophysics

First crystal structure of double knotted protein TrmD-Tm1570 - inside from degradation perspective

F. Bruno da Silva, I. Lewandowska, A. Kluza, S. Niewieczerzal, R. Augustyniak, J. I. Sulkowska

The paper presents the first crystal structure of a double knotted protein TrmD-Tm1570 and shows it can be degraded by the ClpXP system, with simulations explaining degradation kinetics.

bioRxiv · Mar 13, 2023 · PreprintBiophysics

Structure of a AAA+ unfoldase in the process of unfolding substrate

Z. A. Ripstein, R. Huang, R. Augustyniak, L. E. Kay, J. L. Rubinstein

The paper captures the structure of VAT, an AAA+ unfoldase, during substrate unfolding using cryo-EM, revealing a hand-over-hand mechanism.

bioRxiv · Feb 4, 2017Biochemistry