H
Hui-Chun Lu
Researcher at Randall Division of Cell and Molecular Biophysics
Publications - 12
Citations - 578
Hui-Chun Lu is an academic researcher from Randall Division of Cell and Molecular Biophysics. The author has contributed to research in topics: Gene & Medicine. The author has an hindex of 10, co-authored 10 publications receiving 483 citations. Previous affiliations of Hui-Chun Lu include University College London & King's College London.
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Journal ArticleDOI
AP1S3 mutations are associated with pustular psoriasis and impaired Toll-like receptor 3 trafficking
Niovi Setta-Kaffetzi,Michael A. Simpson,Alexander A. Navarini,Varsha M. Patel,Hui-Chun Lu,Michael H. Allen,Michael Duckworth,Hervé Bachelez,A. David Burden,Siew Eng Choon,Christopher E.M. Griffiths,Brian Kirby,Antonios G.A. Kolios,Marieke M B Seyger,Christa Prins,Asma Smahi,Richard C. Trembath,Richard C. Trembath,Franca Fraternali,Catherine H. Smith,Jonathan Barker,Francesca Capon +21 more
TL;DR: It is found that AP1S3 silencing disrupted the endosomal translocation of the innate pattern-recognition receptor TLR-3 (Toll-like receptor 3) and resulted in a marked inhibition of downstream signaling.
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B-RAF Mutant Alleles Associated with Langerhans Cell Histiocytosis, a Granulomatous Pediatric Disease
Takeshi Satoh,Alexander E. Smith,Aurelien Sarde,Hui-Chun Lu,Sophie Mian,Céline Trouillet,Ghulam J. Mufti,Jean-François Emile,Franca Fraternali,Jean Donadieu,Frederic Geissmann +10 more
TL;DR: It is indicated that V600EB-RAf and 600DLATB-RAF mutations are somatic mutants enriched in LCH CD1a+ cells and absent from the patient blood, and further studies are needed to assess the functional consequences of the germ-line T599AB-RAFs.
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The Protein 4.1 family: hub proteins in animals for organizing membrane proteins.
TL;DR: It is hypothesized that differential regulation of 4.1 proteins and ankyrins allows highly selective control of cell surface protein accumulation and, hence, function.
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Specialized Dynamical Properties of Promiscuous Residues Revealed by Simulated Conformational Ensembles
Arianna Fornili,Alessandro Pandini,Alessandro Pandini,Hui-Chun Lu,Franca Fraternali,Franca Fraternali +5 more
TL;DR: The study revealed that promiscuous residues tend to be more flexible than nonpromiscuous ones, and this additional flexibility has a higher degree of organization, and evolutionary conservation and binding promiscuity have opposite effects on intrinsic dynamics.
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Mapping disease-related missense mutations in the immunoglobulin-like fold domain of lamin A/C reveals novel genotype–phenotype associations for laminopathies
TL;DR: A subgroup of skeletal muscle laminopathies, dubbed the ‘Skeletal muscle cluster’, may have a distinct pathological mechanism and novel associations refine the ability to predict clinical features caused by certain LMNA missense mutations.