Author

J. Mak

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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Biophysics· 4 Biochemistry· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:host-pathogen & immune response· 4 Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Organism:human· 3 Approach:microscopy & imaging analysis· 2 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Research Focus:cancer & tumor microenvironment· 1

Frequent Co-Authors

C. Favard· 5 shared D. MURIAUX· 5 shared R. DIBSY· 3 shared E. Bremaud· 2 shared N. Yandrapalli· 2 shared P. Merida· 2 shared A. Antebi· 1 shared A. dePoret· 1 shared

Activity by Year

2016-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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5 shared papersBiophysics

C. Favard

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

A primordial TFEB-TGFβ signaling axis systemically regulates diapause and stem cell longevity

T. J. Nonninger, J. Mak, B. Gerisch, V. Ramponi, K. Kawamura, K. Schilling, C. Latza, J. Koelschbach, R. Ripa, M. Serrano, A. Antebi

The paper identifies a TFEB-TGFβ signaling axis that regulates diapause and stem cell longevity across species by coordinating nutrient availability with growth signals.

bioRxiv · Oct 6, 2023 · PreprintCell Biology

HIV-1 diverts actin debranching mechanismsfor particle assembly and release in CD4 Tlymphocytes.

R. DIBSY, E. Bremaud, J. MAK, C. Favard, D. MURIAUX

This study shows HIV-1 uses actin debranching to enhance virus assembly and release by recruiting Arpin in CD4 T lymphocytes.

bioRxiv · Dec 15, 2022 · PreprintMicrobiology

Quantification of membrane binding and diffusion using Fluorescence Correlation Spectroscopy diffusion laws

A. Mouttou, E. Bremaud, J. Noero, R. Dibsy, C. Arone, J. Mak, D. MURIAUX, H. Berry, C. Favard

This study develops an FCS diffusion law to quantify membrane binding and diffusion of proteins, validated with simulations and experiments on retroviral Gag proteins.

bioRxiv · Sep 12, 2022 · PreprintBiophysics

Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53.

K. Inamdar, F.-C. Tsai, A. dePoret, R. Dibsy, J. Manzi, P. Merida, R. Muller, P. Lappalainen, P. Roingeard, J. Mak, P. Bassereau, C. Favard, D. MURIAUX

This study shows that IRSp53 assists HIV-1 in forming membrane curvature necessary for complete particle assembly.

bioRxiv · Feb 10, 2021Biophysics

Analysis of pluripotency transcription factor interactions reveals preferential binding of NANOG to SOX2 rather than NANOG or OCT4

T. K. Mistri, D. Kelly, J. Mak, D. Colby, N. Mullin, I. Chambers

This study investigates the interactions of pluripotency transcription factors Nanog, Sox2, and Oct4, revealing Nanog's preferential binding to Sox2 over Oct4 and its ability to form homomultimers.

bioRxiv · Jun 24, 2020 · PreprintBiochemistry

HIV-1 Gag specifically restricts PI(4,5)P2 and cholesterol mobility in living cells creating a nanodomain platform for virus assembly.

C. Favard, J. Chojnacki, P. Merida, N. Yandrapalli, J. Mak, C. Eggeling, D. Muriaux

bioRxiv · Feb 21, 2019Biophysics

Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P2/Cholesterolnanoclusters.

N. Yandrapalli, Q. Lubart, H. S. Tanwar, C. PICART, J. Mak, D. Muriaux, C. Favard

This study shows HIV-1 Gag self-assembly creates PIP2/cholesterol nanoclusters on lipid membranes during virus assembly.

bioRxiv · Oct 27, 2016Biophysics