Nicolas Sluis-Cremer, PhD

  • Professor, Department of Medicine, Division of Infectious Diseases
  • Professor, Department of Microbiology and Molecular Genetics
  • Professor, Department of Infectious Diseases and Microbiology, School of Public Health

Education & Training

  • Postdoctoral, McGill University AIDS Center (Canada), 2001
  • PhD, University of the Witwatersrand (South Africa), 1997
  • BSc (Hons), University of the Witwatersrand (South Africa), 1995
  • BSc, University of the Witwatersrand (South Africa), 1994

Research Interests

Dr Sluis-Cremer's research focuses on antiretroviral drugs, drug resistance and HIV latency. Projects include understanding the biochemistry and cellular biology of HIV reverse transcription, elucidating the mechanisms of action and resistance to HIV antiviral drugs, and the discovery of novel inhibitors active against drug resistant HIV-1. New initiatives include understanding the mechanisms involved in HIV latency and pharmacological approaches to eradicate latent HIV infection.


Schauer GD, Huber K, Leuba S, Sluis-Cremer N. Mechanism of allosteric inhibition of HIV-1 reverse transcriptase revealed by single-molecule and ensemble fluorescence. Nucleic Acids Res. 2015; 42(18): 11687-96.

Doyon G, Zerbato J, Mellors JW, Sluis-Cremer N. Disulfiram reactivates latent HIV-1 expression through depletion of the phosphatase and tensin homolog (PTEN). AIDS. 2013; 27(2): F7-F11.

Brumme CJ, Huber KD, Dong W, Poon AF, Harrigan PR, Sluis-Cremer N. Replication fitness of multiple NNRTI-resistant HIV-1 variants in the presence of etravirine measured by 454 deep sequencing. J Virol. 2013; 87(15): 8805-7.

Herman BD, Schinazi RF, Zhang HW, Nettles JH, Stanton R, Detorio M, Obikhod A, Pradère U, Coats SJ, Mellors JW, Sluis-Cremer N. Substrate mimicry: HIV-1 reverse transcriptase recognizes 6-modified-3'-azido-2',3'-dideoxyguanosine-5'-triphosphates as adenosine analogs. Nucleic Acids Res. 2012; 40: 381-90.

Huber K, Doyon G, Plaks J, Fyne E, Mellors JW, Sluis-Cremer N. Inhibitors of histone deacetylases: correlation between isoform specificity and reactivation of HIV-1 from latently infected cells. J. Biol Chem. 2011; 286(25): 22211-8.

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