Author

A. C. W. Pike

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 4 Research Focus:protein structure prediction· 3 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Assay:cryo-EM· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

E. P. Carpenter· 5 shared N. A. Burgess-Brown· 3 shared S. R. Bushell· 3 shared A. Chu· 2 shared A. Quigley· 2 shared D. B. Sauer· 2 shared G. Chi· 2 shared K. E. J. Rodstrom· 2 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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5 shared papersBiochemistry

E. P. Carpenter

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Author profile →

5 papers

Recent·Most cited

Structural basis of the mechanism and inhibition of a human ceramide synthase

T. C. Pascoa, A. C. W. Pike, C. S. Tautermann, G. Chi, M. Traub, A. Quigley, R. Chalk, S. Stefanic, S. Thamm, A. Pautsch, E. P. Carpenter, G. Schnapp, D. B. Sauer

This study determines the structural mechanism of CerS6, a ceramide synthase, using cryo-EM and biochemical analysis, revealing a ping-pong reaction mechanism and insights into fumonisin B1 inhibition.

bioRxiv · Dec 2, 2023Biochemistry

Extracellular modulation of TREK-2 activity with nanobodies provides insight into the mechanisms of K2P channel regulation

K. E. J. Rodstrom, A. Cloake, J. Sormann, A. Baronina, K. H. M. Smith, A. C. W. Pike, J. Ang, P. Proks, M. Schewe, I. Holland-Kaye, S. R. Bushell, J. Elliott, E. Pardon, T. Baukrowitz, R. J. Owens, , S. J. Tucker

The paper identifies nanobodies that selectively modulate TREK-2 channel activity and reveals their binding mechanisms through structural analysis.

bioRxiv · Oct 19, 2023Biophysics

Structure and function of the SIT1 proline transporter in complex with the COVID-19 receptor ACE2

H. Z. Li, A. C. W. Pike, G. Chi, J. S. Hansen, S. G. Lee, K. E. J. Rodstrom, S. R. Bushell, D. Speedman, A. Evans, D. Wang, D. He, L. Shrestha, C. Nasrallah, N. A. Burgess-Brown, T. R. Dafforn, , D. B. Sauer

The paper determines the structure of the SIT1 proline transporter complexed with ACE2 using cryo-EM, revealing substrate specificity and structural changes related to transport and a disease-causing mutation.

bioRxiv · May 17, 2023Biophysics

A new paradigm for Prelamin A proteolytic processing by ZMPSTE24: the upstream SY^LL cleavage occurs first and there is no CaaX processing by ZMPSTE24

L. Nie, E. Spear, T. D. Babatz, A. Quigley, Y. Y. Dong, A. Chu, B. Rotty, R. Chalk, S. M. M. Mukhopadhyay, N. A. Burgess-Brown, A. C. W. Pike, S. G. Young, S. Michaelis, E. P. Carpenter

This study challenges the established order of prelamin A processing by ZMPSTE24, showing that SY^LL cleavage occurs first and independently of C-terminal modifications.

bioRxiv · May 13, 2020 · PreprintBiochemistry

The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K

S. R. Bushell, A. C. W. Pike, M. E. Falzone, N. J. G. Rorsman, C. M. Ta, R. A. Corey, T. D. Newport, C. A. Shintre, A. Tessitore, A. Chu, Q. Wang, L. Shrestha, S. Mukhopadhyay, J. D. Love, N. A. Burgess-Brown, , E. P. Carpenter

This study identifies TMEM16K as an ER-resident calcium-regulated lipid scramblase and elucidates its structural basis for lipid scrambling and inactivation.

bioRxiv · Dec 12, 2018Biochemistry