Author

A. J. Pierik

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· 5 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:cell signaling & trafficking· 3 Assay:proteomics· 3 Approach:biophysical modeling· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2

Frequent Co-Authors

C. M. Blinn· 2 shared A. Buzuk· 1 shared A. Hushka· 1 shared A. Treuner-Lange· 1 shared B. Rashid· 1 shared C. Greth· 1 shared D. J. A. Netz· 1 shared D. L. Perlstein· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

C. M. Blinn

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Author profile →

6 papers

Recent·Most cited

Requirements for the Biogenesis of Proteinsin the Human and Yeast Cytosol

J. J. Braymer, O. Stehling, M. Stuempfig, R. Roesser, F. Spantgar, C. M. Blinn, U. Muehlenhoff, A. J. Pierik, R. Lill

This study identifies the molecular requirements for cytosolic [2Fe-2S] protein maturation in human and yeast, showing it depends on mitochondrial ISC machinery, Atm1/ABCB7, and GSH but not CIA or cGrxs.

Proceedings of the National Academy of Sciences · May 14, 2024Peer-reviewedBiochemistry

Cytosolic iron-sulfur protein assembly system identifies clients by a C-terminal tripeptide

M. D. Marquez, C. Greth, A. Buzuk, Y. Liu, C. M. Blinn, S. Beller, L. Leiskau, A. Hushka, K. Wu, K. Nur, D. J. A. Netz, D. L. Perlstein, A. J. Pierik

The paper identifies a C-terminal tripeptide that directs Fe-S cluster insertion into cytosolic and nuclear proteins by binding to the CIA-targeting complex.

bioRxiv · May 19, 2023Biochemistry

The structure of the F420-dependent sulfite-detoxifying enzyme from Methanococcales reveals a prototypical sulfite-reductase with assimilatory traits.

M. Jespersen, A. J. Pierik, T. Wagner

This paper reports the X-ray structures of Fsr enzymes from two methanogens, revealing their unique architecture and electron transfer mechanism.

bioRxiv · Apr 7, 2022 · PreprintBiochemistry

A natural fusion of flavodiiron, rubredoxin, and NADH:rubredoxin oxidoreductase domains is the highly efficient water-forming oxidase of T. vaginalis

E. N. Abdulaziz, T. A. Bell, B. Rashid, M. L. Heacock, O. S. Skinner, M. A. Yaseen, L. H. Chao, V. K. Mootha, A. J. Pierik, V. Cracan

This study identifies a unique fusion protein in T. vaginalis that efficiently catalyzes oxygen reduction to water using NADH, providing structural and functional insights into its redox system.

bioRxiv · Feb 2, 2022Biochemistry

A repurposed, non-canonical cytochrome c, chaperones calcium binding by PilY1 for type IVa pili formation

M. Herfurth, A. Treuner-Lange, T. Glatter, N. Wittmaack, E. Hoiczyk, A. J. Pierik, L. Sogaard-Andersen

The paper identifies a non-canonical cytochrome c, TfcP, that binds calcium to stabilize PilY1.1, enabling T4aP function across a broader range of calcium concentrations.

bioRxiv · Jul 28, 2021 · PreprintMicrobiology

Exchange of a single amino acid residue in the cryptophyte phycobiliprotein lyase GtCPES expands its substrate specificity

N. Tomazic, K. E. Overkamp, M. Aras, A. J. Pierik, E. Hofmann, N. Frankenberg-Dinkel

This study shows that a single amino acid change in GtCPES expands its substrate specificity to include phycocyanobilin.

bioRxiv · Mar 31, 2020Biochemistry