Author

H. Pace

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 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Assay:proteomics· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Organism:C. elegans· 1

Frequent Co-Authors

M. Bally· 5 shared A. Alam· 2 shared A. Nadeem· 2 shared B. E. Uhlin· 2 shared E. Toh· 2 shared F. Bano· 2 shared K. Persson· 2 shared N. Zlatkov· 2 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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5 shared papersBiochemistry

M. Bally

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Recruitment of apolipoprotein E facilitates Herpes simplex virus 1 attachment, entry, and release

L. Liu, K. Thorsteinsson, F. Bano, S. W. Jayaweera, D. Avinens, D. V. Conca, H. Pace, H. Lövheim, A. Olofsson, M. Bally

This study shows that apolipoprotein E enhances herpes simplex virus 1 attachment, entry, and release by modifying its interactions with cell membranes.

bioRxiv · Feb 10, 2023Microbiology

Simultaneous Membrane and RNA Binding by Tick-Borne Encephalitis Virus Capsid Protein

L. I. Pulkkinen, S. V. Barrass, M. Lindgren, H. Pace, A. K. Överby, M. Anastasina, M. Bally, R. Lundmark, S. J. Butcher

This study investigates how tick-borne encephalitis virus capsid protein binds membranes and recruits RNA, showing electrostatic interactions and membrane insertion.

bioRxiv · Oct 6, 2022Biochemistry

Protein-lipid interaction at low pH induces oligomerisation of the MakA cytotoxin from Vibrio cholerae

A. Nadeem, A. Berg, H. Pace, A. Alam, E. Toh, J. Aden, N. Zlatkov, S. L. Myint, K. Persson, G. Gröbner, A. Sjöstedt, M. Bally, J. Barandun, B. E. Uhlin, S. N. Wai

This study shows that MakA, a Vibrio cholerae toxin, forms tube-like structures in acidic conditions through protein-lipid interactions, revealing a novel mechanism of membrane tubulation.

bioRxiv · Sep 10, 2021Cell Biology

A tripartite cytolytic toxin formed by Vibrio cholerae proteins with flagellum-facilitated secretion

A. Nadeem, R. Nagampalli, E. Toh, A. Alam, S. L. Myint, T. V. Heidler, M. Dongre, N. Zlatkov, H. Pace, F. Bano, A. Sjostedt, M. Bally, B. E. Uhlin, S. N. Wai, K. Persson

This paper identifies a tripartite cytolytic toxin from Vibrio cholerae, showing that MakA/B/E proteins are secreted via flagella and form pores in membranes, contributing to bacterial virulence.

bioRxiv · Jun 20, 2021Biochemistry

Membrane insertion mechanism of the caveolae coat protein Cavin1

K.-c. Liu, H. Pace, E. Larsson, S. Hossain, A. Kabedev, A. Shukla, V. Jerschabek, J. Mohan, C. A. S. Bergstrom, M. Bally, C. Schwieger, M. Hubert, R. Lundmark

This study reveals how Cavin1 inserts into membranes through PI(4,5)P2-dependent adsorption and helix insertion, facilitated by flanking regions and co-assembly with Caveolin1.

bioRxiv · Mar 23, 2021Biochemistry