Author

E. P. Carpenter

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 Biophysics· 5 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 12 Organism:human· 7 Research Focus:protein folding & dynamics· 6 Research Focus:protein structure prediction· 5 Assay:structural biology· 4 Assay:cryo-EM· 3 Research Focus:cell type annotation· 2 Assay:proteomics· 2

Frequent Co-Authors

A. C. W. Pike· 5 shared N. A. Burgess-Brown· 5 shared S. R. Bushell· 5 shared A. Chu· 4 shared L. Nie· 4 shared L. Shrestha· 4 shared A. Quigley· 3 shared S. Michaelis· 3 shared

Activity by Year

2018-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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5 shared papersBiochemistry

A. C. W. Pike

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12 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

The structural basis of fatty acid elongation by the ELOVL elongases

L. Nie, A. C. Pike, T. C. Pascoa, S. R. Bushell, A. Quigley, G. F. Ruda, A. Chu, V. Cole, D. Speedman, T. Moreira, L. Shrestha, S. M. Mukhopadhyay, N. A. Burgess-Brown, J. D. Love, P. E. Brennan, E. P. Carpenter

The paper reports the structure of the human ELOVL7 elongase, revealing its catalytic mechanism and substrate-binding sites, with implications for inhibiting VLCFA accumulation in diseases.

bioRxiv · Nov 11, 2020Biochemistry

Multiple Mechanisms Underlie State-Independent Inhibitory Effects of Norfluoxetine on TREK-2 K2P Channels

P. Proks, M. Schewe, L. J. Conrad, S. Rao, K. Rathje, K. E. Rodstrom, E. P. Carpenter, T. Baukrowitz, S. J. Tucker

This study identifies multiple mechanisms by which norfluoxetine inhibits TREK-2 K2P channels, showing state-independent effects and interactions with filter stability and voltage-dependent gating.

bioRxiv · Oct 29, 2020Biophysics

Cleavage Site Specificity for Processing of Farnesylated Prelamin A by the Zinc Metalloprotease ZMPSTE24

T. D. Babatz, E. D. Spear, W. Xu, O. L. Sun, L. Nie, E. P. Carpenter, S. Michaelis

This study identifies sequence requirements for ZMPSTE24 cleavage of prelamin A, revealing preferences for hydrophobic residues at P1 and sensitivity of C-terminal residues.

bioRxiv · Aug 17, 2020Cell Biology

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

Structural basis for the transport mechanism of the human glutamine transporter SLC1A5 (ASCT2)

X. Yu, O. Plotnikova, P. D. Bonin, T. A. Subashi, T. J. McLellan, D. Dumlao, Y. Che, Y. Dong, E. P. Carpenter, G. M. West, X. Qiu, J. S. Culp, S. Han

This study presents cryo-EM structures of the human glutamine transporter SLC1A5 in an outward-facing conformation, revealing insights into its transport mechanism and substrate recognition.

bioRxiv · Apr 29, 2019 · PreprintBiophysics

Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2 (PC2)

Q. Wang, G. Hedger, P. Aryal, M. Grieben, C. Nasrallah, A. Baronina, A. Pike, J. Shi, E. P. Carpenter, M. Sansom

This study investigates lipid interactions of PC2 using simulations and cryo-EM, identifying PIP and cholesterol binding sites.

bioRxiv · Mar 26, 2019Biophysics

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

ZMPSTE24 Missense Mutations that Cause Progeroid Diseases Decrease Prelamin A Cleavage Activity and/or Protein Stability

E. Spear, E.-T. Hsu, L. Nie, E. P. Carpenter, C. Hrycyna, S. Michaelis

This paper identifies ZMPSTE24 missense mutations that impair prelamin A cleavage, classifying them into activity, stability, or dual defects and showing potential therapeutic rescue strategies.

bioRxiv · May 21, 2018Cell Biology

Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design

Y. Y. Dong, H. Wang, A. C. Pike, S. J. Cochrane, S. Hamedzade, F. J. Wyszynsk, S. R. Bushell, S. F. Royer, D. A. Widdick, A. Sajid, H. I. Boshoff, R. Lucas, W.-M. Liu, S. S. Lee, T. Machida, , E. P. Carpenter

This paper determines the structures of DPAGT1 with substrates and inhibitors, revealing catalytic mechanisms and disease-causing mutations, and designs non-toxic antibiotics for tuberculosis.

bioRxiv · Apr 2, 2018Biochemistry