G. Lin

J. Azzi, M. Seelen, G. Lin, 2017, American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons.

Inhibitors Selective for Mycobacterial versus Human Proteasomes

Huilin Li, C. Nathan, J. Warren, 2009, Nature.

Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome

Tao Wang, Gang Lin, Huilin Li, 2010, The EMBO journal.

Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity

T. Parsons, Huilin Li, P. Zwickl, 2006, Molecular microbiology.

Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate

Huilin Li, L. Dick, C. Nathan, 2006, Molecular microbiology.

Stressed mycobacteria use the chaperone ClpB to sequester irreversibly oxidized proteins asymmetrically within and between cells.

Nicolas Chenouard, M. Unser, D. Schnappinger, 2015, Cell host & microbe.

Rational Design of Selective and Bioactive Inhibitors of the Mycobacterium tuberculosis Proteasome.

R. Sauer, J. Sello, C. Nathan, 2017, ACS infectious diseases.

Activity of epigenetic inhibitors against Plasmodium falciparum asexual and sexual blood stages

Björn F. C. Kafsack, G. Lin, Hao Zhang, 2019, bioRxiv.

Mitigating the risk of antimalarial resistance via covalent dual-subunit inhibition of the Plasmodium proteasome

H. Zhang, M. Bogyo, D. Fidock, 2023, Cell chemical biology.

A philosophy of anti-infectives as a guide in the search for new drugs for tuberculosis.

C. Nathan, R. Bryk, Aditya Venugopal, 2008, Tuberculosis.

Structure-Activity Relationship Studies of Antimalarial Plasmodium Proteasome Inhibitors─Part II.

M. Foley, J. Vendôme, N. Liverton, 2023, Journal of medicinal chemistry.

Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa.

Chunyan Tang, Huilin Li, C. Nathan, 2009, Structure.

High-Throughput/High Content Imaging Screen Identifies Novel Small Molecule Inhibitors and Immunoproteasomes as Therapeutic Targets for Chordoma

H. Zhang, L. Hsiao, J. Azzi, 2023, Pharmaceutics.

Structure-Activity Relationships of Noncovalent Immunoproteasome β5i-Selective Dipeptides.

Xiaojing Ma, C. Nathan, J. Salmon, 2020, Journal of medicinal chemistry.

Artemisinin-based hybrids produce intracellular proteasome inhibitors that overcome resistance in Plasmodium falciparum

C. Nathan, Changmei Yang, L. Kirkman, 2021, bioRxiv.

Selective killing of nonreplicating mycobacteria.

M. Gurney, C. Nathan, C. Popescu, 2008, Cell host & microbe.

Discovery of Highly Selective Inhibitors of the Human Constitutive Proteasome β5c Chymotryptic Subunit.

J. Azzi, G. Sukenick, Wenhu Zhan, 2023, Journal of medicinal chemistry.

Structure of human immunoproteasome with a reversible and noncompetitive inhibitor that selectively inhibits activated lymphocytes

Huilin Li, C. Nathan, Kaiming Zhang, 2017, Nature Communications.

Selective Phenylimidazole-based Inhibitors of the Mycobacterium tuberculosis Proteasome.

M. Foley, Huilin Li, M. Michino, 2019, Journal of medicinal chemistry.

Brief treatment with a highly selective immunoproteasome inhibitor promotes long-term cardiac allograft acceptance in mice

Lei Shi, C. Nathan, J. Azzi, 2016, Proceedings of the National Academy of Sciences.

Dual-pharmacophore artezomibs hijack the Plasmodium ubiquitin-proteasome system to kill malaria parasites while overcoming drug resistance.

H. Zhang, A. Waters, C. Nathan, 2023, Cell chemical biology.

Susceptibilities of Ugandan Plasmodium falciparum Isolates to Proteasome Inhibitors

J. Bailey, A. Gould, O. Aydemir, 2022, Antimicrobial agents and chemotherapy.

Development of a highly selective Plasmodium falciparum proteasome inhibitor with anti-malaria activity in humanized mice.

P. Rosenthal, J. Vendôme, M. Michino, 2021, Angewandte Chemie.

N,C-Capped dipeptides with selectivity for mycobacterial proteasome over human proteasomes: role of S3 and S1 binding pockets.

M. Sintchak, L. Dick, C. Nathan, 2013, Journal of the American Chemical Society.

Immunoproteasome β5i‐Selective Dipeptidomimetic Inhibitors

Lei Shi, C. Nathan, P. Singh, 2016, ChemMedChem.

Macrocyclic Peptides that Selectively Inhibit the Mycobacterium tuberculosis Proteasome.

M. Foley, Huilin Li, J. Vendôme, 2021, Journal of medicinal chemistry.

Structural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome.

Huilin Li, C. Nathan, H. Hsu, 2017, Biochemistry.

Activity of Epigenetic Inhibitors against Plasmodium falciparum Asexual and Sexual Blood Stages

Björn F. C. Kafsack, G. Lin, Hao Zhang, 2020, Antimicrobial Agents and Chemotherapy.

Rational Design of Selective and Bioactive Inhibitors of the Mycobacterium tuberculosis Proteasome.

R. Sauer, C. Nathan, Xiuju Jiang, 2017, ACS infectious diseases.

Structure of human immunoproteasome with a reversible and noncompetitive inhibitor that selectively inhibits activated lymphocytes

Huilin Li, C. Nathan, Kaiming Zhang, 2017, Nature Communications.

Structures revealing mechanisms of resistance and collateral sensitivity of Plasmodium falciparum to proteasome inhibitors

F. Gamo, Benigno Crespo, L. Kirkman, 2023, Nature communications.

Covalent macrocyclic proteasome inhibitors mitigate resistance in Plasmodium falciparum

H. Zhang, M. Bogyo, D. Fidock, 2023, bioRxiv.

Protocol for analysis of intracellular conversion of artezomib molecules into new proteasome inhibitors in Plasmodium falciparum parasites

L. Kirkman, Wenhu Zhan, G. Lin, 2024, STAR protocols.