Author

P. Mehrabi

Primary ORCID profile (0000-0003-3211-6959 · 4 papers)Unclaimed ORCID profile · follow to get notified of new preprints

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

Same name, identified by ORCID

P. MehrabiiD4 papers · Universität Hamburg

Biology Disciplines

Click to filter author papers

Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 3 Assay:cryo-EM· 2 Organism:human· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

D. von Stetten· 4 shared E. C. Schulz· 3 shared F. Tellkamp· 3 shared H. Schikora· 3 shared A. Prester· 2 shared C. E. Hatton· 2 shared G. Gore· 2 shared J.-P. Leimkohl· 2 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 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

4 shared papersBiophysics

D. von Stetten

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Millisecond cryo-trapping by the spitrobot crystal plunger simplifies time-resolved crystallography

P. Mehrabi, S. Sung, D. von Stetten, A. Prester, C. E. Hatton, S. Kleine-Doepke, A. Berkes, G. Gore, J.-P. Leimkohl, H. Schikora, M. Kollewe, H. Rohde, M. Wilmanns, F. Tellkamp, E. C. Schulz

The paper introduces a device called spitrobot that enables millisecond time-resolved crystallography by cryo-trapping reaction intermediates.

bioRxiv · Sep 20, 2022 · PreprintBiophysics

Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging

B. Norton-Baker, P. Mehrabi, A. O. Kwok, K. W. Roskamp, M. A. Spague-Piercy, D. von Stetten, R. J. D. Miller, R. W. Martin

This study reports six crystal structures of deamidated γS-crystallin variants, showing increased instability, aggregation, and disulfide bond formation, suggesting deamidation accelerates oxidative aging in the human lens.

Structure · May 1, 2022Peer-reviewedBiochemistry

Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography

E. C. Schulz, A. Prester, D. von Stetten, G. Gore, C. E. Hatton, K. Bartels, J.-P. Leimkohl, H. Schikora, H. M. Ginn, F. Tellkamp, P. Mehrabi

The paper introduces an environmental enclosure for serial crystallography to study enzyme kinetics across temperatures, showing temperature-dependent modulation in two enzymes.

bioRxiv · Nov 7, 2021Biophysics

Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison

P. Mehrabi, R. Buecker, G. Bourenkov, H. Ginn, D. von Stetten, H. M. Mueller-Werkmeister, A. Kuo, T. Morizumi, B. Eger, W.-L. Ou, S. Oghbaey, A. Sarracini, J. Besaw, O. Pare-Labrosse, S. Meier, , R. J. D. Miller

This study compares data quality from serial femtosecond and serial synchrotron crystallography for two proteins, finding equivalent quality regardless of radiation source.

bioRxiv · Aug 21, 2020Biophysics