Danny Huang

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Professor of Cancer Structural Biology

University of Glasgow

United Kingdom

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Professor Danny Huang is a leading researcher in Cancer Structural Biology at the University of Glasgow, UK. His recent work focuses on ubiquitination processes, including the role of RING E3 ubiquitin ligases and the implications of non-proteinaceous ubiquitination. Additionally, he has contributed to the understanding of oncogenic signaling pathways in leukemia and ovarian cancer, utilizing innovative techniques such as engineered peptides and computational modeling.

Recent Grants

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Mechanism and selective targeting of ubiquitin ligases

Open Date: 2020-04-01

Close Date: 2025-04-01

Grant: Close

Structural and mechanistic insights into RING E3-mediated ubiquitination

Open Date: 2015-05-01

Close Date: 2020-05-01

Grant: Close

Ubiquitin signalling

Open Date: 2015-01-01

Close Date: 2020-01-01

Grant: Close

Ubiquitin Signalling

Open Date: 2009-01-01

Close Date: 2015-01-01

Grant: Close

Ubiquitin Signalling

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Danny Huang

Research Interests

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About

Recent Grants

Articles (20)

Tuning ubiquitin transfer by RING E3 ubiquitin ligases through the linchpin residue

Insights into non-proteinaceous ubiquitination

Raman active diyne-girder conformationally constrained p53 stapled peptides bind to MDM2 for visualisation without fluorophores

Mitochondrial outer membrane integrity regulates a ubiquitin-dependent and NF-κB-mediated inflammatory response

AlphaFold Ensemble Competition Screens Enable Peptide Binder Design with Single-Residue Sensitivity

Autoinflammation in patients with leukocytic CBL loss of heterozygosity is caused by constitutive ERK-mediated monocyte activation

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids

An engineered ubiquitin binding coiled coil peptide

eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to activate localised eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation.

PRL2 phosphatase enhances oncogenic FLT3 signaling via dephosphorylation of the E3 ubiquitin ligase CBL at tyrosine 371.

PRL2 Phosphatase Promotes Oncogenic KIT Signaling in Leukemia Cells through Modulating CBL Phosphorylation

<scp>PTEN</scp> deficiency exposes a requirement for an <scp>ARF GTPase</scp> module for integrin‐dependent invasion in ovarian cancer

Hepatic glutamine synthetase controls N5-methylglutamine in homeostasis and cancer

Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function

Structure of UBE2K–Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension

E3 ligase-inactivation rewires CBL interactome to elicit oncogenesis by hijacking RTK–CBL–CIN85 axis

Identification of a Catalytic Active but Non-Aggregating MDM2 RING Domain Variant

Differential requirements for MDM2 E3 activity during embryogenesis and in adult mice

Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases

Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain

Collaborators (23)

Leo Carlin

VICTOR H. VILLAR

Yan Liu

Mads Gyrd-Hansen

David Lewis

Rosalie Heilig

Stephanie May

Andrew Thomson

David M Bryant

Huiping Liu

Yunpeng Bai

Daniel Murphy

Craig Steven

Thomas Bird

James Ropa

Andrew Jamieson

Chatrin Chatrin

Brian Smith

Alfredo Montes

Alison Hulme

Saverio Tardito

Timothy Humpton

Helge Magnus Magnussen

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