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Xiuju Jiang
Cornell University
Mycobacterium tuberculosisTuberculosisBiochemistryBiologyMicrobiology
19Publications
11H-index
644Citations
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Publications 21
Newest
#1Kangyun WuH-Index: 3
#2Jovanka KooH-Index: 2
Last. Carl NathanH-Index: 123
view all 6 authors...
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#1Shashirekha Mundhra (Cornell University)H-Index: 1
#2Ruslana Bryk (Cornell University)H-Index: 14
Last. Carl Nathan (Cornell University)H-Index: 123
view all 6 authors...
1 CitationsSource
#1A. Negri (Schrödinger)H-Index: 1
#2Prisca Elis Javidnia (Cornell University)H-Index: 2
Last. Selin Somersan-Karakaya (Cornell University)H-Index: 5
view all 24 authors...
The success of Mycobacterium tuberculosis (Mtb) as a pathogen depends on the redundant and complex mechanisms it has evolved for resisting nitrosative and oxidative stresses inflicted by host immunity. Improving our understanding of these defense pathways can reveal vulnerable points in Mtb pathogenesis. In this study, we combined genetic, structural, computational, biochemical, and biophysical approaches to identify a novel enzyme class represented by Rv2466c. We show that Rv2466c is a mycothio...
3 CitationsSource
#1Ruda de Luna Almeida Santos (Van Andel Institute)H-Index: 2
#2Lin Bai (Van Andel Institute)H-Index: 10
Last. Gang Lin (Cornell University)H-Index: 15
view all 14 authors...
Proteasome inhibitors benefit patients with multiple myeloma and B cell-dependent autoimmune disorders but exert toxicity from inhibition of proteasomes in other cells. Toxicity should be minimized by reversible inhibition of the immunoproteasome β5i subunit while sparing the constitutive β5c subunit. Here we report β5i-selective inhibition by asparagine-ethylenediamine (AsnEDA)-based compounds and present the high-resolution cryo-EM structural analysis of the human immunoproteasome. Despite inh...
10 CitationsSource
#1Kohta Saito (Cornell University)H-Index: 4
#2Thulasi Warrier (Cornell University)H-Index: 11
Last. Carl Nathan (Cornell University)H-Index: 123
view all 13 authors...
Mycobacterium tuberculosis (Mtb) encounters stresses during the pathogenesis and treatment of tuberculosis (TB) that can suppress replication of the bacteria and render them phenotypically tolerant to most available drugs. Where studied, the majority of Mtb in the sputum of most untreated subjects with active TB have been found to be nonreplicating by the criterion that they do not grow as colony-forming units (cfus) when plated on agar. However, these cells are viable because they grow when dil...
15 CitationsSource
#1Kyle A. TotaroH-Index: 5
#2Dominik BarthelmeH-Index: 6
Last. Jason K. SelloH-Index: 19
view all 8 authors...
The 20S core particle of the proteasome in Mycobacterium tuberculosis (Mtb) is a promising, yet unconventional, drug target. This multimeric peptidase is not essential, yet degrades proteins that have become damaged and toxic via reactions with nitric oxide (and/or the associated reactive nitrogen intermediates) produced during the host immune response. Proteasome inhibitors could render Mtb susceptible to the immune system, but they would only be therapeutically viable if they do not inhibit th...
6 CitationsSource
#1Pradeep K. Singh (Cornell University)H-Index: 44
#2Hao Fan (Cornell University)H-Index: 5
Last. Gang Lin (Cornell University)H-Index: 15
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N,C-capped dipeptides belong to a class of noncovalent proteasome inhibitors. Herein we report that the insertion of a β-amino acid into N,C-capped dipeptides markedly decreases their inhibitory potency against human constitutive proteasome β5c, while maintaining potent inhibitory activity against human immunoproteasome β5i, thereby achieving thousands-fold selectivity for β5i over β5c. Structure–activity relationship studies revealed that β5c does not tolerate the β-amino acid based dipeptidomi...
9 CitationsSource
#1Nan Zhao (Cornell University)H-Index: 4
#2Mingna Sun (THU: Tsinghua University)H-Index: 8
Last. Carl Nathan (Cornell University)H-Index: 123
view all 9 authors...
Mycobacterial tuberculosis (Mtb) is able to preserve its intrabacterial pH (pHIB) near neutrality in the acidic phagosomes of immunologically activated macrophages and to cause lethal pathology in immunocompetent mice. In contrast, when its ability to maintain pHIB homeostasis is genetically compromised, Mtb dies in acidic phagosomes and is attenuated in the mouse. Compounds that phenocopy the genetic disruption of Mtb’s pHIB homeostasis could serve as starting points for drug development in the...
4 CitationsSource
#1Nan ZhaoH-Index: 4
#2Crystal M. DarbyH-Index: 6
Last. Carl NathanH-Index: 123
view all 18 authors...
Mycobacterium tuberculosis (Mtb) maintains its intrabacterial pH (pHIB) near neutrality in the acidic environment of phagosomes within activated macrophages. A previously reported genetic screen revealed that Mtb loses this ability when the mycobacterial acid resistance protease (marP) gene is disrupted. In the present study, a high throughput screen (HTS) of compounds against the protease domain of MarP identified benzoxazinones as inhibitors of MarP. A potent benzoxazinone, BO43 (6-chloro-2-(2...
15 CitationsSource
#1Julien Vaubourgeix (Cornell University)H-Index: 10
#2Gang Lin (Cornell University)H-Index: 15
Last. Carl Nathan (Cornell University)H-Index: 123
view all 14 authors...
Summary Mycobacterium tuberculosis (Mtb) defends itself against host immunity and chemotherapy at several levels, including the repair or degradation of irreversibly oxidized proteins (IOPs). To investigate how Mtb deals with IOPs that can neither be repaired nor degraded, we used new chemical and biochemical probes and improved image analysis algorithms for time-lapse microscopy to reveal a defense against stationary phase stress, oxidants, and antibiotics—the sequestration of IOPs into aggrega...
41 CitationsSource
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