Search Results - "Trempe, Jean‐Francois"

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  1. 1

    Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection by Trempe, Jean-François, Fon, Edward A

    Published in Frontiers in neurology (01-01-2013)
    “…Autosomal recessive forms of Parkinson's disease are caused by mutations in three genes: Parkin, PINK1, and DJ-1. These genes encode for proteins with distinct…”
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    SPTAN1 variants as a potential cause for autosomal recessive hereditary spastic paraplegia by Leveille, Etienne, Estiar, Mehrdad A, Krohn, Lynne, Spiegelman, Dan, Dionne-Laporte, Alexandre, Dupré, Nicolas, Trempe, Jean François, Rouleau, Guy A, Gan-Or, Ziv

    Published in Journal of human genetics (01-11-2019)
    “…More than 80 known or suspected genes/loci have been reported to be involved in hereditary spastic paraplegia (HSP). Genetic and clinical overlap have been…”
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  4. 4

    Self‐association studies of the bifunctional N‐acetylglucosamine‐1‐phosphate uridyltransferase from Escherichia coli by Trempe, JeanFrançois, Shenker, Solomon, Kozlov, Guennadi, Gehring, Kalle

    Published in Protein science (01-04-2011)
    “…The N‐acetylglucosamine‐1‐phosphate uridyltransferase (GlmU) is a key bifunctional enzyme in the biosynthesis of UDP‐GlcNAc, a precursor in the synthesis of…”
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  5. 5

    Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond by Bayne, Andrew N., Trempe, Jean-François

    “…Parkinson’s disease (PD) is a degenerative movement disorder resulting from the loss of specific neuron types in the midbrain. Early environmental and…”
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  6. 6

    PINK1 autophosphorylation is required for ubiquitin recognition by Rasool, Shafqat, Soya, Naoto, Truong, Luc, Croteau, Nathalie, Lukacs, Gergely L, Trempe, JeanFrançois

    Published in EMBO reports (01-04-2018)
    “…Mutations in PINK1 cause autosomal recessive Parkinson's disease (PD), a neurodegenerative movement disorder. PINK1 is a kinase that acts as a sensor of…”
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  7. 7

    Structural Mechanisms of Mitochondrial Quality Control Mediated by PINK1 and Parkin by Trempe, Jean-François, Gehring, Kalle

    Published in Journal of molecular biology (15-06-2023)
    “…[Display omitted] •PINK1 (a protein kinase) and parkin (a ubiquitin ligase) are neuroprotective proteins and frequently mutated in Parkinson's…”
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  8. 8

    A Ubl/ubiquitin switch in the activation of Parkin by Sauvé, Véronique, Lilov, Asparouh, Seirafi, Marjan, Vranas, Marta, Rasool, Shafqat, Kozlov, Guennadi, Sprules, Tara, Wang, Jimin, Trempe, Jean-François, Gehring, Kalle

    Published in The EMBO journal (14-10-2015)
    “…Mutations in Parkin and PINK1 cause an inherited early‐onset form of Parkinson's disease. The two proteins function together in a mitochondrial quality control…”
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  9. 9

    Mfn2 ubiquitination by PINK1/parkin gates the p97-dependent release of ER from mitochondria to drive mitophagy by McLelland, Gian-Luca, Goiran, Thomas, Yi, Wei, Dorval, Geneviève, Chen, Carol X, Lauinger, Nadine D, Krahn, Andrea I, Valimehr, Sepideh, Rakovic, Aleksandar, Rouiller, Isabelle, Durcan, Thomas M, Trempe, Jean-François, Fon, Edward A

    Published in eLife (20-04-2018)
    “…Despite their importance as signaling hubs, the function of mitochondria-ER contact sites in mitochondrial quality control pathways remains unexplored. Here we…”
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  10. 10

    Structure of the complex I-like molecule NDH of oxygenic photosynthesis by Laughlin, Thomas G., Bayne, Andrew N., Trempe, Jean-François, Savage, David F., Davies, Karen M.

    Published in Nature (London) (01-02-2019)
    “…Cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient…”
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  11. 11

    Mechanism of parkin activation by phosphorylation by Sauvé, Véronique, Sung, George, Soya, Naoto, Kozlov, Guennadi, Blaimschein, Nina, Miotto, Lis Schwartz, Trempe, Jean-François, Lukacs, Gergely L., Gehring, Kalle

    Published in Nature structural & molecular biology (01-07-2018)
    “…Mutations in the ubiquitin ligase parkin are responsible for a familial form of Parkinson’s disease. Parkin and the PINK1 kinase regulate a quality-control…”
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  12. 12

    Ubiquitin is phosphorylated by PINK1 to activate parkin by Koyano, Fumika, Okatsu, Kei, Kosako, Hidetaka, Tamura, Yasushi, Go, Etsu, Kimura, Mayumi, Kimura, Yoko, Tsuchiya, Hikaru, Yoshihara, Hidehito, Hirokawa, Takatsugu, Endo, Toshiya, Fon, Edward A., Trempe, Jean-François, Saeki, Yasushi, Tanaka, Keiji, Matsuda, Noriyuki

    Published in Nature (London) (05-06-2014)
    “…Ubiquitin, known for its role in post-translational modification of other proteins, undergoes post-translational modification itself; after a decrease in…”
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    Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation by Trempe, Jean-François, Sauvé, Véronique, Grenier, Karl, Seirafi, Marjan, Tang, Matthew Y., Ménade, Marie, Al-Abdul-Wahid, Sameer, Krett, Jonathan, Wong, Kathy, Kozlov, Guennadi, Nagar, Bhushan, Fon, Edward A., Gehring, Kalle

    “…Mutations in the PARK2 (parkin) gene are responsible for an autosomal recessive form of Parkinson's disease. The parkin protein is a RING-in-between-RING E3…”
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  14. 14

    Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation by Tang, Matthew Y., Vranas, Marta, Krahn, Andrea I., Pundlik, Shayal, Trempe, Jean- François, Fon, Edward A.

    Published in Nature communications (09-03-2017)
    “…Parkin and PINK1 function in a common pathway to clear damaged mitochondria. Parkin exists in an auto-inhibited conformation stabilized by multiple interdomain…”
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  15. 15

    Reading the ubiquitin postal code by Trempe, Jean-François

    Published in Current opinion in structural biology (01-12-2011)
    “…► Polyubiquitin chains linked through different linkages carry various specific functions in the cell. ► Polyubiquitin chains are flexible structures that can…”
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    Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex by Rasool, Shafqat, Veyron, Simon, Soya, Naoto, Eldeeb, Mohamed A., Lukacs, Gergely L., Fon, Edward A., Trempe, Jean-François

    Published in Molecular cell (06-01-2022)
    “…Mutations in PINK1 cause autosomal-recessive Parkinson’s disease. Mitochondrial damage results in PINK1 import arrest on the translocase of the outer…”
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    Structures of the Dsk2 UBL and UBA domains and their complex by Lowe, Edward D., Hasan, Na'il, Fonso, Laura, Trempe, Jean-Francois, Noble, Martin E. M., Endicott, Jane A., Johnson, Louise N., Brown, Nick R.

    “…The yeast proteins Dsk2 and Rad23 belong to a family of proteins that contain an N‐terminal ubiquitin‐like domain (UBL) and a C‐terminal ubiquitin‐associated…”
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    The landscape of Parkin variants reveals pathogenic mechanisms and therapeutic targets in Parkinson’s disease by Yi, Wei, MacDougall, Emma J, Tang, Matthew Y, Krahn, Andrea I, Gan-Or, Ziv, Trempe, Jean-François, Fon, Edward A

    Published in Human molecular genetics (01-09-2019)
    “…Abstract Mutations in Parkin (PARK2), which encodes an E3 ubiquitin ligase implicated in mitophagy, are the most common cause of early-onset Parkinson’s…”
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  19. 19

    The yeast proteases Ddi1 and Wss1 are both involved in the DNA replication stress response by Svoboda, Michal, Konvalinka, Jan, Trempe, Jean-François, Grantz Saskova, Klara

    Published in DNA repair (01-08-2019)
    “…Genome integrity and cell survival are dependent on proper replication stress response. Multiple repair pathways addressing obstacles generated by replication…”
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  20. 20

    The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications by Khalifa, Ahmad Abdelzaher Zaki, Ichikawa, Muneyoshi, Dai, Daniel, Kubo, Shintaroh, Black, Corbin Steven, Peri, Katya, McAlear, Thomas S, Veyron, Simon, Yang, Shun Kai, Vargas, Javier, Bechstedt, Susanne, Trempe, Jean-François, Bui, Khanh Huy

    Published in eLife (17-01-2020)
    “…Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers,…”
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