M
Martin J. Law
Researcher at John Radcliffe Hospital
Publications - 5
Citations - 1739
Martin J. Law is an academic researcher from John Radcliffe Hospital. The author has contributed to research in topics: ATRX & Gene. The author has an hindex of 4, co-authored 5 publications receiving 1553 citations. Previous affiliations of Martin J. Law include University of Oxford.
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Journal ArticleDOI
Distinct Factors Control Histone Variant H3.3 Localization at Specific Genomic Regions
Aaron D Goldberg,Laura A. Banaszynski,Kyung-Min Noh,Peter W. Lewis,Simon J. Elsaesser,Sonja C. Stadler,Scott Dewell,Martin J. Law,Xingyi Guo,Xuan Li,Duancheng Wen,Duancheng Wen,Ariane Chapgier,Russell Dekelver,Jeffrey C. Miller,Ya Li Lee,Elizabeth A. Boydston,Michael C. Holmes,Philip D. Gregory,John M. Greally,Shahin Rafii,Shahin Rafii,Chingwen Yang,Peter J. Scambler,David Garrick,Richard J. Gibbons,Douglas R. Higgs,Ileana M. Cristea,Fyodor D. Urnov,Deyou Zheng,C. David Allis +30 more
TL;DR: It is demonstrated that multiple and distinct factors are responsible for H3.3 localization at specific genomic locations in mammalian cells.
Journal ArticleDOI
ATR-X Syndrome Protein Targets Tandem Repeats and Influences Allele-Specific Expression in a Size-Dependent Manner
Martin J. Law,Karen M. Lower,Hsiao P.J. Voon,Jim R. Hughes,David Garrick,Vip Viprakasit,Matthew Mitson,Marco De Gobbi,Marco A. Marra,Andrew J. Morris,Aaron Abbott,Steven P. Wilder,Stephen Taylor,Guilherme Martins Santos,Joe Cross,Helena Ayyub,Steven J.M. Jones,Jiannis Ragoussis,Daniela Rhodes,Ian Dunham,Douglas R. Higgs,Richard J. Gibbons +21 more
TL;DR: It is shown that ATRX binds G-quadruplex structures in vitro, suggesting a mechanism by which ATRx may play a role in various nuclear processes and how this is perturbed when ATRZ is mutated.
Journal ArticleDOI
Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin
Sebastian Eustermann,Ji-Chun Yang,Martin J. Law,Rachel Amos,Lynda Chapman,Clare Jelinska,David Garrick,David Clynes,Richard J. Gibbons,Daniela Rhodes,Douglas R. Higgs,David Neuhaus +11 more
TL;DR: The ADD domain of ATRX, in which most syndrome-causing mutations occur, engages the N-terminal tail of histone H3 through two rigidly oriented binding pockets, one for unmodified Lys4 and the other for di- or trimethylated Lys9, and illustrates how the 'histone-code' is interpreted by a combination of multivalent effector-chromatin interactions.
Journal ArticleDOI
Understanding alpha-globin gene regulation: Aiming to improve the management of thalassemia.
Doug Higgs,David Garrick,Eduardo Anguita,M De Gobbi,Jim R. Hughes,M Muers,Douglas Vernimmen,Karen M. Lower,Martin J. Law,A Argentaro,Marie-Alice Deville,Richard J. Gibbons +11 more
TL;DR: Previously, nearly all mutations causing thalassemia have been found in or around the globin loci, but rare inherited and acquired trans‐acting mutations are being found more often and are revealing new pathways in the regulation of globin gene expression that may open up new avenues for improving the management of patients with common types of thalassesmia.