N. Sluis-Cremer

发表

Evidence for biphasic uncoating during HIV-1 infection from a novel imaging assay

Jeremy Luban, J. Luban, C. Aiken, 2013, Retrovirology.

The Emerging Profile of Cross-Resistance among the Nonnucleoside HIV-1 Reverse Transcriptase Inhibitors

N. Sluis-Cremer, 2014, Viruses.

Resistance to reverse transcriptase inhibitors used in the treatment and prevention of HIV-1 infection.

M. Wainberg, R. Schinazi, N. Sluis-Cremer, 2015, Future microbiology.

Future of nonnucleoside reverse transcriptase inhibitors

N. Sluis-Cremer, 2018, Proceedings of the National Academy of Sciences.

Proteolytic processing of an HIV-1 pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation.

N. Sluis-Cremer, M. Parniak, D. Arion, 2004, The international journal of biochemistry & cell biology.

HIV-1 Resistance to Reverse Transcriptase Inhibitors

N. Sluis-Cremer, G. Schauer, 2014 .

Molecular mechanism of HIV-1 resistance to 3'-azido-2',3'-dideoxyguanosine.

J. Mellors, R. Schinazi, N. Sluis-Cremer, 2014, Antiviral Research.

Molecular mechanisms of HIV-1 resistance to nucleoside and nucleotide reverse transcriptase inhibitors

N. Sluis-Cremer, 2007 .

Inhibitors of HIV- I reverse transcriptase

N. Sluis-Cremer, M. Parniak, 2000 .

Mechanism by Which Phosphonoformic Acid Resistance Mutations Restore 3′-Azido-3′-deoxythymidine (AZT) Sensitivity to AZT-resistant HIV-1 Reverse Transcriptase*

N. Sluis-Cremer, M. Parniak, D. Arion, 2000, The Journal of Biological Chemistry.

Mutations in the HIV-1 3′-Polypurine Tract and Integrase Strand Transfer Inhibitor Resistance

N. Sluis-Cremer, Yuliang Wei, 2021, Antimicrobial Agents and Chemotherapy.

Relative domain orientation of the L289K HIV‐1 reverse transcriptase monomer

Yun-Xing Wang, R. Ishima, N. Sluis-Cremer, 2022, Protein science : a publication of the Protein Society.

Peptides Mimicking the β7/β8 Loop of HIV-1 Reverse Transcriptase p51 as "Hotspot-Targeted" Dimerization Inhibitors.

F. Gago, L. Menéndez-Arias, S. de Castro, 2020, ACS medicinal chemistry letters.

Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[Spiro[4"-amino-2",2" -dioxo-1",2" -oxathiole-5",3'-[2', 5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]]]-3-ethylthy mine.

J. Balzarini, M. Camarasa, N. Sluis-Cremer, 2000, Biochemistry.

Dimerization of human immunodeficiency virus type 1 reverse transcriptase as an antiviral target.

N. Sluis-Cremer, S. Srivastava, G. Tachedjian, 2006, Current pharmaceutical design.

Mechanisms of inhibition of HIV replication by non-nucleoside reverse transcriptase inhibitors.

N. Sluis-Cremer, G. Tachedjian, 2008, Virus research.

Effect of reverse transcriptase inhibitors and mutations on the low-cost Cavidi reverse transcriptase viral load assay.

N. Sluis-Cremer, S. Crowe, M. Gouillou, 2009, Journal of acquired immune deficiency syndromes.

Structure–activity relationships in HIV‐1 reverse transcriptase revealed by radiation target analysis

N. Sluis-Cremer, E. Kempner, M. Parniak, 2003, Protein science : a publication of the Protein Society.

Inhibition of Fosfomycin Resistance Protein FosA by Phosphonoformate (Foscarnet) in Multidrug-Resistant Gram-Negative Pathogens

N. Sluis-Cremer, C. McElheny, R. Mettus, 2017, Antimicrobial Agents and Chemotherapy.

High-Level Fosfomycin Resistance in Vancomycin-Resistant Enterococcus faecium

L. Rice, V. Cooper, N. Sluis-Cremer, 2017, Emerging infectious diseases.

Frequent emergence of N348I in HIV-1 subtype C reverse transcriptase with failure of initial therapy reduces susceptibility to reverse-transcriptase inhibitors.

J. Mellors, K. Shutt, R. Wood, 2012, Clinical infectious diseases : an official publication of the Infectious Diseases Society of America.

The Base Component of 3′-Azido-2′,3′-Dideoxynucleosides Influences Resistance Mutations Selected in HIV-1 Reverse Transcriptase

J. Mellors, R. Schinazi, N. Sluis-Cremer, 2011, Antimicrobial Agents and Chemotherapy.

Anti-Human Immunodeficiency Virus Activity, Cross-Resistance, Cytotoxicity, and Intracellular Pharmacology of the 3′-Azido-2′,3′-Dideoxypurine Nucleosides

J. Mellors, R. Schinazi, N. Sluis-Cremer, 2009, Antimicrobial Agents and Chemotherapy.

Increasing prevalence of K65K and K66K in HIV-1 subtype B reverse transcriptase

P. Harrigan, N. Sluis-Cremer, C. Brumme, 2016, AIDS.

Conformational stability of Cys45‐alkylated and hydrogen peroxide‐oxidised glutathione S‐transferase

N. Sluis-Cremer, H. Dirr, 1995, FEBS letters.

Class-pi glutathione S-transferase is unable to regain its native conformation after oxidative inactivation by hydrogen peroxide.

N. Naidoo, N. Sluis-Cremer, H. Dirr, 1996, European journal of biochemistry.

Naive CD4+ T Cells Harbor a Large Inducible Reservoir of Latent, Replication-competent Human Immunodeficiency Virus Type 1

N. Sluis-Cremer, W. Mellors, K. McMahon, 2019 .

Mechanisms by Which the G333D Mutation in Human Immunodeficiency Virus Type 1 Reverse Transcriptase Facilitates Dual Resistance to Zidovudine and Lamivudine

J. Mellors, N. Sluis-Cremer, J. Radzio, 2007, Antimicrobial Agents and Chemotherapy.

Temporal transcriptional response to latency reversing agents identifies specific factors regulating HIV-1 viral transcriptional switch

Narasimhan J. Venkatachari, Z. Bar-Joseph, Siddhartha Jain, 2015, Retrovirology.

Small-Molecule Inhibitor of FosA Expands Fosfomycin Activity to Multidrug-Resistant Gram-Negative Pathogens

P. Wintrode, E. Sundberg, O. Weisz, 2019, Antimicrobial Agents and Chemotherapy.

The RNA binding protein HuR does not interact directly with HIV-1 reverse transcriptase and does not affect reverse transcription in vitro

A. Gronenborn, K. Huber, N. Sluis-Cremer, 2010, Retrovirology.

Subunit-specific mutational analysis of residue N348 in HIV-1 reverse transcriptase

N. Sluis-Cremer, J. Radzio, Jessica A. Radzio, 2011, Retrovirology.

In Vitro Cross-Resistance Profiles of Rilpivirine, Dapivirine, and MIV-150, Nonnucleoside Reverse Transcriptase Inhibitor Microbicides in Clinical Development for the Prevention of HIV-1 Infection

N. Sluis-Cremer, Nicholas S. Giacobbi, 2017, Antimicrobial Agents and Chemotherapy.

HIV-1 Resistance to the Nonnucleoside Reverse Transcriptase Inhibitors

N. Sluis-Cremer, 2017 .

Novel high-throughput screen identifies an HIV-1 reverse transcriptase inhibitor with a unique mechanism of action.

N. Sluis-Cremer, C. Sheen, Onur Alptürk, 2014, The Biochemical journal.

Probing nonnucleoside inhibitor‐induced active‐site distortion in HIV‐1 reverse transcriptase by transient kinetic analyses

N. Sluis-Cremer, K. Anderson, J. Radzio, 2007, Protein science : a publication of the Protein Society.

Characterization of novel non-nucleoside reverse transcriptase (RT) inhibitor resistance mutations at residues 132 and 135 in the 51 kDa subunit of HIV-1 RT.

N. Sluis-Cremer, Z. Ambrose, N. Hamamouch, 2007, The Biochemical journal.

Substrate mimicry: HIV-1 reverse transcriptase recognizes 6-modified-3′-azido-2′,3′-dideoxyguanosine-5′-triphosphates as adenosine analogs

Richard A. Stanton, J. Nettles, J. Mellors, 2011, Nucleic acids research.

The 3′-Azido Group Is Not the Primary Determinant of 3′-Azido-3′-deoxythymidine (AZT) Responsible for the Excision Phenotype of AZT-resistant HIV-1*

J. Mellors, R. Schinazi, N. Sluis-Cremer, 2005, Journal of Biological Chemistry.

The Human Immunodeficiency Virus Type 1 Nonnucleoside Reverse Transcriptase Inhibitor Resistance Mutation I132M Confers Hypersensitivity to Nucleoside Analogs

B. Herman, N. Sluis-Cremer, Z. Ambrose, 2009, Journal of Virology.

Macrophage-targeted nanocarriers for anti-HIV therapy

J. Ananworanich, M. Amiji, N. Sluis-Cremer, 2007 .

Frequent Emergence of N 348 I in HIV-1 Subtype C Reverse Transcriptase with Failure of Initial Therapy Reduces Susceptibility to Reverse-Transcriptase Inhibitors

J. Mellors, K. Shutt, R. Wood, 2012 .

The Base Component of 3 (cid:1) -Azido-2 (cid:1) ,3 (cid:1) -Dideoxynucleosides Inﬂuences Resistance Mutations Selected in HIV-1 Reverse Transcriptase (cid:1)

J. Mellors, R. Schinazi, N. Sluis-Cremer, 2011 .

Radiation target analyses of DNA template/primer complexes.

N. Sluis-Cremer, E. Kempner, 2006, Biophysical journal.

Establishment and Reversal of HIV-1 Latency in Naive and Central Memory CD4 (cid:2) T Cells In Vitro

Simon C Watkins, A. Engelman, Erik Serrao, 2016 .

Transient kinetic analyses of the ribonuclease H cleavage activity of HIV-1 reverse transcriptase in complex with efavirenz and/or a β-thujaplicinol analogue.

B. Herman, N. Sluis-Cremer, 2013, The Biochemical journal.

N348I in reverse transcriptase provides a genetic pathway for HIV-1 to select thymidine analogue mutations and mutations antagonistic to thymidine analogue mutations

N. Sluis-Cremer, J. Radzio, G. Tachedjian, 2010, AIDS.

Mutational analysis of Lys65 of HIV-1 reverse transcriptase.

N. Sluis-Cremer, M. Parniak, D. Arion, 2000, The Biochemical journal.

N348I in HIV-1 Reverse Transcriptase Counteracts the Synergy Between Zidovudine and Nevirapine

B. Herman, N. Sluis-Cremer, J. Radzio, 2012, Journal of acquired immune deficiency syndromes.

Efavirenz Accelerates HIV-1 Reverse Transcriptase Ribonuclease H Cleavage, Leading to Diminished Zidovudine Excision

N. Sluis-Cremer, J. Radzio, Jessica A. Radzio, 2008, Molecular Pharmacology.

Structure-activity relationships of [2',5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]- 3'-spiro-5' '-(4' '-amino-1' ',2' '-oxathiole-2' ',2' '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization.

J. Balzarini, M. Camarasa, S. Velázquez, 2006, Journal of medicinal chemistry.

Development of a Robust Cytopathic Effect-Based High-Throughput Screening Assay To Identify Novel Inhibitors of Dengue Virus

N. Sluis-Cremer, K. McCormick, Ernesto T. A. Marques, 2012, Antimicrobial Agents and Chemotherapy.

Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors.

N. Sluis-Cremer, M. Parniak, D. Arion, 2002, Molecular pharmacology.

Inhibitors of HIV-1 reverse transcriptase.

N. Sluis-Cremer, M. Parniak, 2000, Advances in pharmacology.

Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution

R. Ishima, N. Sluis-Cremer, Tatiana V. Ilina, 2020, International journal of molecular sciences.

Structural Basis of Reduced Susceptibility to Ceftazidime-Avibactam and Cefiderocol in Enterobacter cloacae Due to AmpC R2 Loop Deletion

N. Sluis-Cremer, C. McElheny, Y. Doi, 2020, Antimicrobial Agents and Chemotherapy.

Origin of the plasmid-mediated fosfomycin resistance gene fosA3

N. Sluis-Cremer, Marissa Pacey, R. Mettus, 2018, The Journal of antimicrobial chemotherapy.

Synthesis and Anti-HIV Evaluation of 3′-Triazolo Nucleosides

R. Schinazi, B. Herman, N. Sluis-Cremer, 2011, Nucleosides, nucleotides & nucleic acids.

Synthesis, antiviral activity, cytotoxicity and cellular pharmacology of l-3'-azido-2',3'-dideoxypurine nucleosides.

J. Nettles, J. Mellors, R. Schinazi, 2011, European journal of medicinal chemistry.

Synthesis and anti‐HIV Evaluation of 3′‐Triazolo Nucleosides.

R. Schinazi, B. Herman, N. Sluis-Cremer, 2012 .

Molecular mechanisms of bidirectional antagonism between K65R and thymidine analog mutations in HIV-1 reverse transcriptase

J. Mellors, N. Sluis-Cremer, U. Parikh, 2007, AIDS.

Molecular Mechanism by Which the K70E Mutation in Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confers Resistance to Nucleoside Reverse Transcriptase Inhibitors

J. Mellors, N. Sluis-Cremer, U. Parikh, 2006, Antimicrobial Agents and Chemotherapy.

Synthesis and evaluation of 3'-azido-2',3'-dideoxypurine nucleosides as inhibitors of human immunodeficiency virus.

Steven J Coats, J. Mellors, R. Schinazi, 2010, Bioorganic & Medicinal Chemistry Letters.

Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs)

N. Sluis-Cremer, M. Parniak, D. Arion, 2000, Cellular and Molecular Life Sciences (CMLS).

Mechanism of allosteric inhibition of HIV-1 reverse transcriptase revealed by single-molecule and ensemble fluorescence

K. Huber, N. Sluis-Cremer, S. Leuba, 2014, Nucleic acids research.

Synthesis and Anti-HIV-1 Activity of a Novel Series of Aminoimidazole Analogs.

B. Herman, S. Murugesan, N. Sluis-Cremer, 2010, Letters in drug design & discovery.

Mechanism by which a glutamine to leucine substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance.

J. Mellors, N. Sluis-Cremer, J. Brehm, 2008, Biochemistry.

Silent mutations are selected in HIV-1 reverse transcriptase and affect enzymatic efficiency

B. Wynhoven, A. Poon, N. Sluis-Cremer, 2008, AIDS.

Novel N-3 Substituted TSAO-T Derivatives: Synthesis and Anti-HIV-Evaluation

J. Balzarini, M. Camarasa, N. Sluis-Cremer, 2008, Nucleosides, nucleotides & nucleic acids.

N348I in the Connection Domain of HIV-1 Reverse Transcriptase Confers Zidovudine and Nevirapine Resistance

B. Wynhoven, Mark Zanin, N. Sluis-Cremer, 2007, PLoS medicine.

Stereo‐selectivity of HIV‐1 reverse transcriptase toward isomers of thymidine‐5′‐O‐1‐thiotriphosphate

N. Sluis-Cremer, J. Radzio, 2005, Protein science : a publication of the Protein Society.

Efavirenz enhances the proteolytic processing of an HIV‐1 pol polyprotein precursor and reverse transcriptase homodimer formation

S. Goff, N. Sluis-Cremer, G. Tachedjian, 2005, FEBS letters.

Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules.

N. Sluis-Cremer, G. Tachedjian, 2002, European journal of biochemistry.

Molecular Pharmacology of Nucleoside and Nucleotide HIV-1 Reverse Transcriptase Inhibitors

B. Herman, N. Sluis-Cremer, 2012 .

Conformational changes in HIV-1 reverse transcriptase induced by nonnucleoside reverse transcriptase inhibitor binding.

Ivet Bahar, I. Bahar, N. Sluis-Cremer, 2004, Current HIV research.

J. Balzarini, M. Camarasa, N. Sluis-Cremer, 2000, Biochemistry.

Nonnucleoside Reverse Transcriptase Inhibitors Reduce HIV-1 Production from Latently Infected Resting CD4+ T Cells following Latency Reversal

N. Sluis-Cremer, G. Tachedjian, J. Zerbato, 2016, Antimicrobial Agents and Chemotherapy.

The Acyclic 2,4-Diaminopyrimidine Nucleoside Phosphonate Acts as a Purine Mimetic in HIV-1 Reverse Transcriptase DNA Polymerization*

B. Herman, J. Balzarini, N. Sluis-Cremer, 2010, The Journal of Biological Chemistry.

Relationship between enzyme activity and dimeric structure of recombinant HIV‐1 reverse transcriptase

N. Sluis-Cremer, J. Radzio, G. Tachedjian, 2005, Proteins.

Role of RNase H Activity in NRTI/NNRTI Drug Resistance

N. Sluis-Cremer, G. Tachedjian, 2013 .

Zidovudine (AZT) Monotherapy Selects for the A360V Mutation in the Connection Domain of HIV-1 Reverse Transcriptase

S. Hammer, J. Mellors, N. Sluis-Cremer, 2012, PloS one.

Selection of Mutations in the Connection and RNase H Domains of Human Immunodeficiency Virus Type 1 Reverse Transcriptase That Increase Resistance to 3′-Azido-3′-Dideoxythymidine

V. Pathak, J. Mellors, N. Sluis-Cremer, 2007, Journal of Virology.

Novel N‐3 Substituted Tsao‐T Derivatives: Synthesis and anti‐HIV‐Evaluation.

J. Balzarini, M. Camarasa, N. Sluis-Cremer, 2008 .

E138A in HIV-1 reverse transcriptase is more common in subtype C than B: implications for rilpivirine use in resource-limited settings.

Michael I. Jordan, J. Mellors, N. Parkin, 2014, Antiviral research.

Establishment and Reversal of HIV-1 Latency in Naive and Central Memory CD4+ T Cells In Vitro

Simon C Watkins, A. Engelman, Erik Serrao, 2016, Journal of Virology.

HIV-1 reverse transcriptase decreases susceptibility to tenofovir and etravirine in combination with other resistance mutations

N. Sluis-Cremer, J. Radzio, S. Sonza, 2009 .

Silent mutations at codons 65 and 66 in reverse transcriptase alleviate indel formation and restore fitness in subtype B HIV-1 containing D67N and K70R drug resistance mutations

N. Sluis-Cremer, P. Harrigan, M. Tachedjian, 2015, Nucleic acids research.

Potent Nonnucleoside Reverse Transcriptase Inhibitors Target HIV-1 Gag-Pol

Johnson Mak, Gilda Tachedjian, J. Mak, 2006, PLoS pathogens.

Discovery of a Small Molecule Agonist of Phosphatidylinositol 3-Kinase p110α That Reactivates Latent HIV-1

J. Mellors, K. Huber, N. Sluis-Cremer, 2014, PloS one.

Biophysical Insights into the Inhibitory Mechanism of Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors

N. Sluis-Cremer, S. Leuba, G. Schauer, 2013, Biomolecules.

Inhibitors of Signaling Pathways That Block Reversal of HIV-1 Latency

Feng Qi Han, Narasimhan J. Venkatachari, Phalguni Gupta, 2018, Antimicrobial Agents and Chemotherapy.

HIV Infection of Naive CD4+ T Cells: An Important Reservoir of Persistent HIV Infection?

N. Sluis-Cremer, J. Zerbato, 2013 .

Naïve CD4+ T Cells Harbor a Large Inducible Reservoir of Latent, Replication-Competent HIV-1.

J. Mellors, N. Sluis-Cremer, D. McMahon, 2019, Clinical infectious diseases : an official publication of the Infectious Diseases Society of America.

Mechanism by Which PF-3758309, a Pan Isoform Inhibitor of p21-Activated Kinases, Blocks Reactivation of HIV-1 Latency

N. Yates, N. Sluis-Cremer, J. Boslett, 2022, bioRxiv.

Toward a Functional Cure for HIV-1 Infection: The Block and Lock Therapeutic Approach

N. Sluis-Cremer, B. Vargas, Benni Vargas, 2022, Frontiers in Virology.

Novel assay reveals a large inducible replication competent HIV-1 reservoir in resting CD4+ T cells

Narasimhan J. Venkatachari, Phalguni Gupta, C. Rinaldo, 2017, Nature Medicine.

Inhibitors of Histone Deacetylases

J. Mellors, K. Huber, N. Sluis-Cremer, 2011, The Journal of Biological Chemistry.

Efficient HIV-1 Trans Infection of CD4+ T Cells Occurs in the Presence of Antiretroviral Therapy

C. Rinaldo, N. Sluis-Cremer, G. Rappocciolo, 2019, Open forum infectious diseases.

Widespread Fosfomycin Resistance in Gram-Negative Bacteria Attributable to the Chromosomal fosA Gene

Yohei Doi, Ryota Ito, Mustapha M. Mustapha, 2017, mBio.

Glutathione-S-transferase FosA6 of Klebsiella pneumoniae origin conferring fosfomycin resistance in ESBL-producing Escherichia coli.

V. Cooper, N. Stoesser, N. Sluis-Cremer, 2016, The Journal of antimicrobial chemotherapy.

Mutational Analysis of Tyr-501 of HIV-1 Reverse Transcriptase

N. Sluis-Cremer, M. Parniak, D. Arion, 2002, The Journal of Biological Chemistry.

B Lymphocytes, but Not Dendritic Cells, Efficiently HIV-1 Trans Infect Naive CD4+ T Cells: Implications for the Viral Reservoir

C. Rinaldo, P. Piazza, N. Sluis-Cremer, 2021, mBio.

B LYMPHOCYTES, BUT NOT DENDRITIC CELLS, EFFICIENTLY HIV-1 TRANS-INFECT NAÏVE CD4+ T CELLS: IMPLICATIONS FOR THE VIRAL RESERVOIR

C. Rinaldo, P. Piazza, N. Sluis-Cremer, 2020, bioRxiv.

Type 1-programmed dendritic cells drive antigen-specific latency reversal and immune elimination of persistent HIV-1

Phalguni Gupta, C. Rinaldo, N. Sluis-Cremer, 2019, EBioMedicine.

Nonnucleoside Reverse Transcriptase Inhibitor Hypersusceptibility and Resistance by Mutation of Residue 181 in HIV-1 Reverse Transcriptase

K. Huber, N. Sluis-Cremer, J. Barnard, 2019, Antimicrobial Agents and Chemotherapy.

Replication Fitness of Multiple Nonnucleoside Reverse Transcriptase-Resistant HIV-1 Variants in the Presence of Etravirine Measured by 454 Deep Sequencing

P. Harrigan, A. Poon, K. Huber, 2013, Journal of Virology.

Conformational stability of pGEX‐expressed Schistosoma japonicum glutathione S‐transferase: A detoxification enzyme and fusion‐protein affinity tag

H. Klump, N. Sluis-Cremer, H. Dirr, 1997, Protein science : a publication of the Protein Society.

Disulfiram reactivates latent HIV-1 expression through depletion of the phosphatase and tensin homolog

J. Mellors, N. Sluis-Cremer, Geneviève Doyon, 2013, AIDS.

Temporal transcriptional response to latency reversing agents identifies specific factors regulating HIV-1 viral transcriptional switch

Narasimhan J. Venkatachari, Z. Bar-Joseph, Siddhartha Jain, 2015, Retrovirology.

Determination of a binding site for a non-substrate ligand in mammalian cytosolic glutathione S-transferases by means of fluorescence-resonance energy transfer.

N. Naidoo, T. Manoharan, N. Sluis-Cremer, 1996, European journal of biochemistry.

INHIBITORS OF HISTONE DEACETYLASES : CORRELATION BETWEEN ISOFORM SPECIFICITY AND REACTIVATION OF HIV-1 FROM LATENTLY INFECTED CELLS *

J. Mellors, K. Huber, N. Sluis-Cremer, 2011 .

Equilibrium and kinetic unfolding properties of dimeric human glutathione transferase A1-1.

L. Wallace, N. Sluis-Cremer, H. Dirr, 1998, Biochemistry.

Failure of Initial Therapy With Two Nucleosides and Efavirenz Is Not Associated With Early Emergence of Mutations in the C-Terminus of HIV-1 Reverse Transcriptase

M. Hughes, R. Haubrich, J. Mellors, 2011, Journal of acquired immune deficiency syndromes.

Targeting HIV-1 Reverse Transcriptase Using a Fragment-Based Approach

E. Arnold, M. Gunzburg, N. Sluis-Cremer, 2023, Molecules.

Structure and Dynamics of FosA-Mediated Fosfomycin Resistance in Klebsiella pneumoniae and Escherichia coli

Justin A. Lemkul, A. MacKerell, P. Wintrode, 2017, Antimicrobial Agents and Chemotherapy.

N348I in HIV-1 reverse transcriptase decreases susceptibility to tenofovir and etravirine in combination with other resistance mutations

N. Sluis-Cremer, S. Sonza, G. Tachedjian, 2010, AIDS.

Establishment and Reversal of HIV-1 Latency in Naive and Central Memory CD4+ T Cells In Vitro

Simon C Watkins, A. Engelman, Erik Serrao, 2016, Journal of Virology.

Identification of mechanistically distinct inhibitors of HIV-1 reverse transcriptase through fragment screening

K. Huber, N. Sluis-Cremer, D. Chalmers, 2015, Proceedings of the National Academy of Sciences.

Future of nonnucleoside reverse transcriptase inhibitors

N. Sluis-Cremer, 2018, Proceedings of the National Academy of Sciences.

Impact of residues in the nonnucleoside reverse transcriptase inhibitor binding pocket on HIV-1 reverse transcriptase heterodimer stability.

N. Sluis-Cremer, G. Tachedjian, A. Figueiredo, 2008, Current HIV research.