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Cell chemical biology 14건

  1. [해외논문]   A Master Switch in Thiopeptide Biosynthesis   SCI SCIE

    Roessler, Claudia (Friedrich Schiller University, Institute of Organic and Macromolecular Chemistry, Humboldtstr. 10, D-07743 Jena, Germany ) , Arndt, Hans-Dieter (Friedrich Schiller University, Institute of Organic and Macromolecular Chemistry, Humboldtstr. 10, D-07743 Jena, Germany)
    Cell chemical biology v.25 no.2 ,pp. 121 - 123 , 2018 , 2451-9456 ,

    초록

    Although considerable knowledge of the biosynthetic machinery of thiopeptide antibiotics has been accumulated, the regulation of their production remains unclear. In this issue of Cell Chemical Biology , have now characterized a key transcription factor and suggest its feedback regulation by biosynthesis intermediates and the final product.

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  2. [해외논문]   Insights into an Ancient Atypical Kinase Essential for Biosynthesis of Coenzyme Q   SCI SCIE

    Clarke, Catherine F. (Department of Chemistry and Biochemistry, and the Molecular Biology Institute, UCLA, Los Angeles, CA 90095, USA)
    Cell chemical biology v.25 no.2 ,pp. 123 - 125 , 2018 , 2451-9456 ,

    초록

    COQ8 proteins are homologs of atypical protein kinases required for the biosynthesis of coenzyme Q (CoQ). In this issue of Cell Chemical Biology , show that COQ8 has an ATPase activity, required for CoQ biosynthesis, that is strongly activated by cardiolipin and small molecule mimics of early CoQ intermediates.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  3. [해외논문]   Screening Drugs for Kidney Disease: Targeting the Podocyte   SCI SCIE

    Bryer, Joshua S. (Renal-Electrolyte and Hypertension Division of Department of Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA ) , Susztak, Katalin (Renal-Electrolyte and Hypertension Division of Department of Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA)
    Cell chemical biology v.25 no.2 ,pp. 126 - 127 , 2018 , 2451-9456 ,

    초록

    Podocytes cover the kidney glomerular basement membrane and present the final barrier in the renal filtration system. Podocyte loss, observed in most kidney diseases, correlates with kidney function decline. In this issue of Cell Chemical Biology , , using a high-throughput chemical screen, identified the compound CDG-0876, which improved podocyte survival.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  4. [해외논문]   The Elements of Translational Chemical Biology   SCI SCIE

    Copeland, Robert A. (Epizyme, Inc., 400 Technology Square, Cambridge, MA 02139, USA ) , Boriack-Sjodin, P. Ann (Epizyme, Inc., 400 Technology Square, Cambridge, MA 02139, USA)
    Cell chemical biology v.25 no.2 ,pp. 128 - 134 , 2018 , 2451-9456 ,

    초록

    A causal relationship between target activity modulation by small molecules and phenotypic consequence is the cornerstone of chemical biology and drug discovery. Here we articulate elements of translational chemical biology, as guideposts to ensure the appropriate use of chemical probes and the conclusions drawn from cellular studies with these molecules.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  5. [해외논문]   Overcoming Resistance to the THZ Series of Covalent Transcriptional CDK Inhibitors   SCI SCIE

    Gao, Yang (Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Zhang, Tinghu (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Terai, Hideki (Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Ficarro, Scott B. (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Kwiatkowski, Nicholas (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Hao, Ming-Feng (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Sharma, Bandana (Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Christensen, Camilla L. (Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Chipumuro, Edmond (KSQ Therapeutics, Cambridge, MA 02139, USA ) , Wong, Kwok-kin (Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Marto, Jarrod A. (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Hammerman, Peter S. (Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA ) , Gray, Nathanael S. (Department of C) , George, Rani E.
    Cell chemical biology v.25 no.2 ,pp. 135 - 142.e5 , 2018 , 2451-9456 ,

    초록

    Summary Irreversible inhibition of transcriptional cyclin-dependent kinases (CDKs) provides a therapeutic strategy for cancers that rely on aberrant transcription; however, lack of understanding of resistance mechanisms to these agents will likely impede their clinical evolution. Here, we demonstrate upregulation of multidrug transporters ABCB1 and ABCG2 as a major mode of resistance to THZ1, a covalent inhibitor of CDKs 7, 12, and 13 in neuroblastoma and lung cancer. To counter this obstacle, we developed a CDK inhibitor, E9 , that is not a substrate for ABC transporters, and by selecting for resistance, determined that it exerts its cytotoxic effects through covalent modification of cysteine 1039 of CDK12. These results highlight the importance of considering this common mode of resistance in the development of clinical analogs of THZ1, identify a covalent CDK12 inhibitor that is not susceptible to ABC transporter-mediated drug efflux, and demonstrate that target deconvolution can be accomplished through selection for resistance. Highlights ABC transporters mediate resistance to THZ series of transcriptional CDK inhibitors E9 lacks substrate specificity for ABC transporters and thus overcomes THZ resistance E9 induces cytotoxicity through covalent modification of C1039 of CDK12 ABC transporter status should be considered in the development of clinical THZ analogs Graphical Abstract [DISPLAY OMISSION]

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  6. [해외논문]   NosP-Regulated Nosiheptide Production Responds to Both Peptidyl and Small-Molecule Ligands Derived from the Precursor Peptide   SCI SCIE

    Li, Jingjing (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China ) , Li, Yue (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China ) , Niu, Guoqing (State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China ) , Guo, Heng (State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China ) , Qiu, Yanping (State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China ) , Lin, Zhi (State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China ) , Liu, Wen (State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Sh) , Tan, Huarong
    Cell chemical biology v.25 no.2 ,pp. 143 - 153.e4 , 2018 , 2451-9456 ,

    초록

    Summary Nosiheptide, an archetypal member of thiopeptide antibiotics, arises from post-translational modifications of a ribosomally synthesized precursor peptide that contains an N-terminal leader peptide (LP) sequence and a C-terminal core peptide (CP) sequence. Despite extensive efforts concerning the biosynthesis of thiopeptide antibiotics, the regulatory mechanisms in this process remain poorly understood. Using the nosiheptide-producing Streptomyces actuosus strain as a model system, we report here that NosP, a Streptomyces antibiotic regulatory protein, serves as the only cluster-situated regulator and activates the transcription of all structural genes, which are organized into two divergently transcribed operons in the nos cluster, by binding to their intergenic region. NocP, the counterpart of NosP in Nocardia sp., regulates the production of structurally related nocathiacin I in a similar manner. NosP activity senses the nosiheptide biosynthetic process by interactions with both peptidyl and small-molecule ligands that result from the LP and CP parts of the precursor peptide, respectively. Highlights NosP serves as the only CSR related to NOS production NocP, a homolog of NosP, functions in a similar manner Thiopeptide-specific small-molecule ligands antagonize NosP activity NosP responds to the peptidyl ligand LP-carboxylate Graphical Abstract [DISPLAY OMISSION]

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  7. [해외논문]   Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family   SCI SCIE

    Reidenbach, Andrew G. (Morgridge Institute for Research, Madison, WI 53715, USA ) , Kemmerer, Zachary A. (Morgridge Institute for Research, Madison, WI 53715, USA ) , Aydin, Deniz (Institute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland ) , Jochem, Adam (Morgridge Institute for Research, Madison, WI 53715, USA ) , McDevitt, Molly T. (Morgridge Institute for Research, Madison, WI 53715, USA ) , Hutchins, Paul D. (Department of Chemistry, University of Wisconsin–Madison, Madison, WI 53706, USA ) , Stark, Jaime L. (Department of Biochemistry, University of Wisconsin–Madison, Madison, WI 53706, USA ) , Stefely, Jonathan A. (Morgridge Institute for Research, Madison, WI 53715, USA ) , Reddy, Thiru (Morgridge Institute for Research, Madison, WI 53715, USA ) , Hebert, Alex S. (Genome Center of Wisconsin, Madison, WI 53706, USA ) , Wilkerson, Emily M. (Department of Chemistry, University of Wisconsin–Madison, Madison, WI 53706, USA ) , Johnson, Isabel E. (Morgridge Institute for Research, Madison, WI 53715, USA ) , Bingman, Craig A. (Department of Biochemistry, University of Wisconsin–Madison, Madison, WI 53706, USA ) , Markley, John L. (Department of Biochemi) , Coon, Joshua J. , Dal Peraro, Matteo , Pagliarini, David J.
    Cell chemical biology v.25 no.2 ,pp. 154 - 165.e11 , 2018 , 2451-9456 ,

    초록

    Summary Human COQ8A (ADCK3) and Saccharomyces cerevisiae Coq8p (collectively COQ8) are UbiB family proteins essential for mitochondrial coenzyme Q (CoQ) biosynthesis. However, the biochemical activity of COQ8 and its direct role in CoQ production remain unclear, in part due to lack of known endogenous regulators of COQ8 function and of effective small molecules for probing its activity in vivo. Here, we demonstrate that COQ8 possesses evolutionarily conserved ATPase activity that is activated by binding to membranes containing cardiolipin and by phenolic compounds that resemble CoQ pathway intermediates. We further create an analog-sensitive version of Coq8p and reveal that acute chemical inhibition of its endogenous activity in yeast is sufficient to cause respiratory deficiency concomitant with CoQ depletion. Collectively, this work defines lipid and small-molecule modulators of an ancient family of atypical kinase-like proteins and establishes a chemical genetic system for further exploring the mechanistic role of COQ8 in CoQ biosynthesis. Highlights The UbiB family has a conserved ATPase activity that is activated by CoQ-like phenols Mature COQ8 binds specifically to cardiolipin-containing liposomes Cardiolipin significantly increases COQ8's ATPase activity Covalent inhibition of analog-sensitive COQ8 acutely disrupts CoQ biosynthesis Graphical Abstract [DISPLAY OMISSION]

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  8. [해외논문]   Site-Specific Installation of Succinyl Lysine Analog into Histones Reveals the Effect of H2BK34 Succinylation on Nucleosome Dynamics   SCI SCIE

    Jing, Yihang (Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China ) , Liu, Zheng (Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China ) , Tian, Gaofei (Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China ) , Bao, Xiucong (Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China ) , Ishibashi, Toyotaka (Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China ) , Li, Xiang David (Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China)
    Cell chemical biology v.25 no.2 ,pp. 166 - 174.e7 , 2018 , 2451-9456 ,

    초록

    Summary Posttranslational modifications of histones play key roles in the dynamic regulation of chromatin structure. Lysine succinylation is a new type of histone modification, but its biological significance in chromatin structure and dynamics remains unknown. Here we develop a chemical approach to site-specifically install a succinyl lysine analog into histones. This analog serves as an ideal structural and functional mimic to natural succinyl lysine. The incorporation of this succinylation mimic into histone H2B at lysine 34, a succinylation site at the nucleosomal DNA-histone interface, leads to significant decrease in nucleosome stability in vitro , which is consistent with the defects in chromatin structure of a budding yeast strain containing a lysine-to-glutamate mutation at the corresponding residue of yeast histone H2B. This study provides a simple method for the rapid generation of histones with site-specific succinylation mimics, and reveals novel regulatory mechanisms of histone succinylation in the dynamic organization of chromatin. Highlights Site-specific installation of a succinyl lysine (Ksucc) analog into histones H2BK34succ destabilizes nucleosomes by affecting histone-DNA interaction A K-to-E mutation mimicking H2BK34succ causes defects in yeast chromatin compaction Graphical Abstract [DISPLAY OMISSION]

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  9. [해외논문]   GDC-0879, a BRAFV600E Inhibitor, Protects Kidney Podocytes from Death   SCI SCIE

    Sieber, Jonas (Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA ) , Wieder, Nicolas (Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA ) , Clark, Abbe (Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA ) , Reitberger, Manuel (Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA ) , Matan, Sofia (Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA ) , Schoenfelder, Jeannine (Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA ) , Zhang, Jianming (Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA ) , Mandinova, Anna (Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA ) , Bittker, Joshua Adam (The Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA ) , Gutierrez, Juan (The Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA ) , Aygü (The Broad Inst) , n, Ozan , Udeshi, Namrata , Carr, Steven , Mundel, Peter , Jehle, Andreas Werner , Greka, Anna
    Cell chemical biology v.25 no.2 ,pp. 175 - 184.e4 , 2018 , 2451-9456 ,

    초록

    Summary Progressive kidney diseases affect approximately 500 million people worldwide. Podocytes are terminally differentiated cells of the kidney filter, the loss of which leads to disease progression and kidney failure. To date, there are no therapies to promote podocyte survival. Drug repurposing may therefore help accelerate the development of cures in an area of tremendous unmet need. In a newly developed high-throughput screening assay of podocyte viability, we identified the BRAF V600E inhibitor GDC-0879 and the adenylate cyclase agonist forskolin as podocyte-survival-promoting compounds. GDC-0879 protects podocytes from injury through paradoxical activation of the MEK/ERK pathway. Forskolin promotes podocyte survival by attenuating protein biosynthesis. Importantly, GDC-0879 and forskolin are shown to promote podocyte survival against an array of cellular stressors. This work reveals new therapeutic targets for much needed podocyte-protective therapies and provides insights into the use of GDC-0879-like molecules for the treatment of progressive kidney diseases. Highlights HTS identifies the BRAF V600E inhibitor GDC-0879 as a podocyte-protective drug GDC-0879 restores MAPK signaling in podocytes GDC-0879 protects podocytes from an array of cell death inducers The podocyte is the target of choice for the development of kidney therapeutics Graphical Abstract [DISPLAY OMISSION]

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  10. [해외논문]   Specific Inhibition of the Bifunctional Farnesyl/Geranylgeranyl Diphosphate Synthase in Malaria Parasites via a New Small-Molecule Binding Site   SCI SCIE

    Gisselberg, Jolyn E. (Department of Biochemistry, Stanford Medical School, Stanford University, Stanford, CA 94305, USA ) , Herrera, Zachary (Department of Biochemistry, Stanford Medical School, Stanford University, Stanford, CA 94305, USA ) , Orchard, Lindsey M. (Department of Biochemistry & Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA ) , Lliná (Department of Biochemistry & Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA ) , s, Manuel (Department of Biochemistry, Stanford Medical School, Stanford University, Stanford, CA 94305, USA) , Yeh, Ellen
    Cell chemical biology v.25 no.2 ,pp. 185 - 193.e5 , 2018 , 2451-9456 ,

    초록

    Summary The bifunctional farnesyl/geranylgeranyl diphosphate synthase (FPPS/GGPPS) is a key branchpoint enzyme in isoprenoid biosynthesis in Plasmodium falciparum (malaria) parasites. Pf FPPS/GGPPS is a validated, high-priority antimalarial drug target. Unfortunately, current bisphosphonate drugs that inhibit FPPS and GGPPS enzymes by acting as a diphosphate substrate analog show poor bioavailability and selectivity for Pf FPPS/GGPPS. We identified a new non-bisphosphonate compound, MMV019313, which is highly selective for Pf FPPS/GGPPS and showed no activity against human FPPS or GGPPS. Inhibition of Pf FPPS/GGPPS by MMV019313, but not bisphosphonates, was disrupted in an S228T variant, demonstrating that MMV019313 and bisphosphonates have distinct modes of inhibition. Molecular docking indicated that MMV019313 did not bind previously characterized substrate sites in Pf FPPS/GGPPS. Our finding uncovers a new, selective small-molecule binding site in this important antimalarial drug target with superior druggability compared with the known inhibitor site and sets the stage for the development of Plasmodium -specific FPPS/GGPPS inhibitors. Highlights A new non-bisphosphonate compound inhibits Pf FPPS/GGPPS, a validated drug target Unlike bisphosphonates, MMV019313 is specific for Pf FPPS/GGPPS over human homologs We reveal a novel mode of inhibition of this high-priority antimalarial drug target This study sets the stage for development of specific Pf FPPS/GGPPS inhibitors Graphical Abstract [DISPLAY OMISSION]

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