johnson mak

Professor

Griffith University

Australia

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Professor Johnson Mak is a faculty member at Griffith University in Australia. His research primarily focuses on advanced techniques for blood cell separation, the mechanisms of HIV-1 assembly and transmission, and the structural dynamics of RNA isoforms within cells. Recent publications include studies on glycan-mediated interactions and membrane binding, contributing valuable insights into viral entry processes and host-pathogen interactions.

Articles (14)

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2025

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2023

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2023

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2023

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2023

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2023

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2022

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2022

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2022

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2022

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2021

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2021

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2021

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2021

Collaborators (11)

Carine Tisne

CNRS

FRANCE

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Anupriya Aggarwal

UNSW Sydney

AUSTRALIA

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Dan Yuan

Lecturer (Assistant Prof.)

University of Queensland

AUSTRALIA

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Assia Mouhand

Assistant professor (Biochemistry/Structural biology)

University of Montpellier

FRANCE

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John Thornhill

Imperial College London

UNITED KINGDOM

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Annette von Delft

University of Oxford

UNITED KINGDOM

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J C Kenyon

UNITED KINGDOM

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Hugues Berry

Inria, the French national research institute for the digital sciences

FRANCE

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Valérie Vivet-Boudou

University of Strasbourg

FRANCE

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Belinda de Villiers

Griffith University

AUSTRALIA

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Martin Jarrold

Indiana State University

UNITED STATES

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johnson mak

Research Interests

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About

Articles (14)

High-efficient white blood cell separation from whole blood using cascaded inertial microfluidics

Identifying the structures of individual RNA isoforms inside cells

Quantifying membrane binding and diffusion with fluorescence correlation spectroscopy diffusion laws

Protocol to quantify glycan-mediated binding between viral particles and human peripheral blood mononuclear cells using nanoluciferase

Protocol to visualize glycan-mediated binding between virus and human blood mononuclear cells using thin-section transmission electron microscopy

HIV-1 diverts cortical actin for particle assembly and release

Structural maturation of the HIV-1 RNA 5’ untranslated region by Pr55Gag and its maturation products

Calcium Contributes to Polarized Targeting of HIV Assembly Machinery by Regulating Complex Stability

Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry

Complement Receptor 3 Mediates HIV-1 Transcytosis across an Intact Cervical Epithelial Cell Barrier: New Insight into HIV Transmission in Women

Antibodies to neutralising epitopes synergistically block the interaction of the receptor‐binding domain of SARS‐CoV‐2 to ACE 2

Incoming HIV virion-derived Gag Spacer Peptide 2 (p1) is a target of effective CD8<sup>+</sup> T cell antiviral responses

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

Multidisciplinary approaches identify compounds that bind to human ace2 or sars-cov-2 spike protein as candidates to block sars-cov-2–ace2 receptor interactions

Collaborators (11)

Carine Tisne

Anupriya Aggarwal

Dan Yuan

Assia Mouhand

John Thornhill

Annette von Delft

J C Kenyon

Hugues Berry

Valérie Vivet-Boudou

Belinda de Villiers

Martin Jarrold

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