Imperial College London

DrMarufAli

Faculty of Natural SciencesDepartment of Life Sciences

CRUK Research Fellow
 
 
 
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Contact

 

+44 (0)20 7594 5733maruf.ali Website

 
 
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Location

 

505Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Summary

The aim of our research is to understand the molecular mechanisms that govern how cells maintain the quality of proteins during cellular stress, towards developing novel strategies for therapeutic intervention in cancer and neurodegenerative diseases.

Of particular interest, we seek to gain structural and mechanistic insights into how the Unfolded Protein Response, a key cell signaling system that maintains protein homeostasis within the ER, is activated and how the signal is subsequently propagated.

We utilize a multidisciplinary approach that encompasses structural biology, biochemistry, and cellular techniques, to characterize proteins and complexes involved in ER stress pathways. 

Selected Publications

Journal Articles

Cerezo M, Lehraiki A, Millet A, et al., 2016, Compounds Triggering ER Stress Exert Anti-Melanoma Effects and Overcome BRAF Inhibitor Resistance, Cancer Cell, Vol:29, ISSN:1535-6108, Pages:805-819

Carrara M, Prischi F, Nowak PR, et al., 2015, Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling, EMBO Journal, Vol:34, ISSN:0261-4189, Pages:1589-1600

Carrara M, Prischi F, Nowak PR, et al., 2015, Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein C(H)1 to initiate ER stress signaling, Elife, Vol:4, ISSN:2050-084X

Prischi F, Nowak PR, Carrara M, et al., 2014, Phosphoregulation of Ire1 RNase splicing activity., Nat Commun, Vol:5

Ali MMU, Bagratuni T, Davenport EL, et al., 2011, Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response, EMBO Journal, Vol:30, ISSN:0261-4189, Pages:894-905

Ali MMU, Roe SM, Vaughan CK, et al., 2006, Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex, Nature, Vol:440, ISSN:0028-0836, Pages:1013-1017

More Publications