Author

D. Peterle

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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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

J. R. Engen· 3 shared T. E. Wales· 2 shared A. Negro· 1 shared A. Pagotto· 1 shared C. M. Radu· 1 shared D. DePice· 1 shared E. A. Bullitt· 1 shared E. S. Klimtchuk· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersBiochemistry

J. R. Engen

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4 papers

Recent·Most cited

Role of Complementarity-Determining Regions 1 and 3 in Pathologic Amyloid Formation by Human Immunoglobulin κ1 Light Chains

E. S. Klimtchuk, D. Peterle, E. A. Bullitt, L. H. Connors, J. R. Engen, O. Gursky

This study investigates how mutations in CDR1 and CDR3 regions of human immunoglobulin κ1 light chains influence amyloid formation through structural and dynamic analyses.

bioRxiv · Feb 1, 2023Biochemistry

Increase the flow rate and improve hydrogen deuterium exchange mass spectrometry

D. Peterle, D. DePice, T. E. Wales, J. R. Engen

This paper improves hydrogen deuterium exchange mass spectrometry by increasing flow rates under quench conditions, enhancing separation efficiency and deuterium recovery.

Journal of Chromatography A · Jan 1, 2023Peer-reviewedBiophysics

Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase

Z. Ji, H. Li, D. Peterle, J. A. Paulo, S. B. Ficarro, T. E. Wales, J. Marto, S. Gygi, J. R. Engen, T. A. Rapoport

This study elucidates how the Cdc48 ATPase complex unfolds and translocates polyubiquitinated protein substrates through cooperative binding with Ufd1/Npl4.

bioRxiv · Oct 21, 2021Biochemistry

Human -Synuclein Inhibits Platelets Aggregation in vitro by Interfering with the -Thrombin/Protease-Activated Receptor 1 Functional Axis

G. Pontarollo, L. Acquasaliente, C. M. Radu, D. Peterle, I. Artusi, A. Pagotto, F. Uliana, P. Simioni, A. Negro, V. De Filippis

This study shows that human -synuclein inhibits platelet aggregation by interfering with the -thrombin/PAR1 functional axis through direct and indirect mechanisms.

bioRxiv · Mar 28, 2021 · PreprintBiochemistry