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Mitochondria shed their outer membrane in response to infection-induced stress.

Science (New York, N.Y.)

Li X, Straub J, Medeiros TC, Mehra C, den Brave F, Peker E, Atanassov I, Stillger K, Michaelis JB, Burbridge E, Adrain C, Münch C, Riemer J, Becker T, Pernas LF.
PMID: 35025629
Science. 2022 Jan 14;375(6577):eabi4343. doi: 10.1126/science.abi4343. Epub 2022 Jan 14.

[Figure: see text].

Cite
Li X, Straub J, Medeiros TC, et al. Mitochondria shed their outer membrane in response to infection-induced stress. Science. 2022;375(6577):eabi4343doi: 10.1126/science.abi4343.
Li, X., Straub, J., Medeiros, T. C., Mehra, C., den Brave, F., Peker, E., Atanassov, I., Stillger, K., Michaelis, J. B., Burbridge, E., Adrain, C., Münch, C., Riemer, J., Becker, T., & Pernas, L. F. (2022). Mitochondria shed their outer membrane in response to infection-induced stress. Science (New York, N.Y.), 375(6577), eabi4343. https://doi.org/10.1126/science.abi4343
Li, Xianhe, et al. "Mitochondria shed their outer membrane in response to infection-induced stress." Science (New York, N.Y.) vol. 375,6577 (2022): eabi4343. doi: https://doi.org/10.1126/science.abi4343
Li X, Straub J, Medeiros TC, Mehra C, den Brave F, Peker E, Atanassov I, Stillger K, Michaelis JB, Burbridge E, Adrain C, Münch C, Riemer J, Becker T, Pernas LF. Mitochondria shed their outer membrane in response to infection-induced stress. Science. 2022 Jan 14;375(6577):eabi4343. doi: 10.1126/science.abi4343. Epub 2022 Jan 14. PMID: 35025629.
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Mitochondria shed their outer membrane in response to infection-induced stress.

Science (New York, N.Y.)

Li X, Straub J, Medeiros TC, Mehra C, den Brave F, Peker E, Atanassov I, Stillger K, Michaelis JB, Burbridge E, Adrain C, Münch C, Riemer J, Becker T, Pernas LF.
PMID: 35025629
Science. 2022 Jan 14;375(6577):eabi4343. doi: 10.1126/science.abi4343. Epub 2022 Jan 14.

[Figure: see text].

Cite
Li X, Straub J, Medeiros TC, et al. Mitochondria shed their outer membrane in response to infection-induced stress. Science. 2022;375(6577):eabi4343doi: 10.1126/science.abi4343.
Li, X., Straub, J., Medeiros, T. C., Mehra, C., den Brave, F., Peker, E., Atanassov, I., Stillger, K., Michaelis, J. B., Burbridge, E., Adrain, C., Münch, C., Riemer, J., Becker, T., & Pernas, L. F. (2022). Mitochondria shed their outer membrane in response to infection-induced stress. Science (New York, N.Y.), 375(6577), eabi4343. https://doi.org/10.1126/science.abi4343
Li, Xianhe, et al. "Mitochondria shed their outer membrane in response to infection-induced stress." Science (New York, N.Y.) vol. 375,6577 (2022): eabi4343. doi: https://doi.org/10.1126/science.abi4343
Li X, Straub J, Medeiros TC, Mehra C, den Brave F, Peker E, Atanassov I, Stillger K, Michaelis JB, Burbridge E, Adrain C, Münch C, Riemer J, Becker T, Pernas LF. Mitochondria shed their outer membrane in response to infection-induced stress. Science. 2022 Jan 14;375(6577):eabi4343. doi: 10.1126/science.abi4343. Epub 2022 Jan 14. PMID: 35025629.
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Phyllomedusa bicolor skin secretion and the Kambô ritual.

The journal of venomous animals and toxins including tropical diseases

den Brave PS, Bruins E, Bronkhorst MW.
PMID: 26413084
J Venom Anim Toxins Incl Trop Dis. 2014 Sep 02;20:40. doi: 10.1186/1678-9199-20-40. eCollection 2014.

The ritual of Kambô or Sapo is a type of voluntary envenomation. During this purification ritual a shaman healer, from various South American countries, deliberately burns the right shoulder with a glowing stick from a fireplace. Excretions of Phyllomedusa...

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den Brave PS, Bruins E, Bronkhorst MW. Phyllomedusa bicolor skin secretion and the Kambô ritual. J Venom Anim Toxins Incl Trop Dis. 2014;20:40doi: 10.1186/1678-9199-20-40.
den Brave, P. S., Bruins, E., & Bronkhorst, M. W. (2014). Phyllomedusa bicolor skin secretion and the Kambô ritual. The journal of venomous animals and toxins including tropical diseases, 2040. https://doi.org/10.1186/1678-9199-20-40
den Brave, Paul S, et al. "Phyllomedusa bicolor skin secretion and the Kambô ritual." The journal of venomous animals and toxins including tropical diseases vol. 20 (2014): 40. doi: https://doi.org/10.1186/1678-9199-20-40
den Brave PS, Bruins E, Bronkhorst MW. Phyllomedusa bicolor skin secretion and the Kambô ritual. J Venom Anim Toxins Incl Trop Dis. 2014 Sep 02;20:40. doi: 10.1186/1678-9199-20-40. eCollection 2014. PMID: 26413084; PMCID: PMC4582952.
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Protein Quality Control at the Mitochondrial Surface.

Frontiers in cell and developmental biology

den Brave F, Gupta A, Becker T.
PMID: 34926473
Front Cell Dev Biol. 2021 Dec 03;9:795685. doi: 10.3389/fcell.2021.795685. eCollection 2021.

Mitochondria contain two membranes, the outer and inner membrane. The outer membrane fulfills crucial functions for the communication of mitochondria with the cellular environment like exchange of lipids via organelle contact sites, the transport of metabolites and the formation...

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den Brave F, Gupta A, Becker T. Protein Quality Control at the Mitochondrial Surface. Front Cell Dev Biol. 2021;9:795685doi: 10.3389/fcell.2021.795685.
den Brave, F., Gupta, A., & Becker, T. (2021). Protein Quality Control at the Mitochondrial Surface. Frontiers in cell and developmental biology, 9795685. https://doi.org/10.3389/fcell.2021.795685
den Brave, Fabian, et al. "Protein Quality Control at the Mitochondrial Surface." Frontiers in cell and developmental biology vol. 9 (2021): 795685. doi: https://doi.org/10.3389/fcell.2021.795685
den Brave F, Gupta A, Becker T. Protein Quality Control at the Mitochondrial Surface. Front Cell Dev Biol. 2021 Dec 03;9:795685. doi: 10.3389/fcell.2021.795685. eCollection 2021. PMID: 34926473; PMCID: PMC8678412.
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Protein Quality Control at the Mitochondrial Surface.

Frontiers in cell and developmental biology

den Brave F, Gupta A, Becker T.
PMID: 34926473
Front Cell Dev Biol. 2021 Dec 03;9:795685. doi: 10.3389/fcell.2021.795685. eCollection 2021.

Mitochondria contain two membranes, the outer and inner membrane. The outer membrane fulfills crucial functions for the communication of mitochondria with the cellular environment like exchange of lipids via organelle contact sites, the transport of metabolites and the formation...

Cite
den Brave F, Gupta A, Becker T. Protein Quality Control at the Mitochondrial Surface. Front Cell Dev Biol. 2021;9:795685doi: 10.3389/fcell.2021.795685.
den Brave, F., Gupta, A., & Becker, T. (2021). Protein Quality Control at the Mitochondrial Surface. Frontiers in cell and developmental biology, 9795685. https://doi.org/10.3389/fcell.2021.795685
den Brave, Fabian, et al. "Protein Quality Control at the Mitochondrial Surface." Frontiers in cell and developmental biology vol. 9 (2021): 795685. doi: https://doi.org/10.3389/fcell.2021.795685
den Brave F, Gupta A, Becker T. Protein Quality Control at the Mitochondrial Surface. Front Cell Dev Biol. 2021 Dec 03;9:795685. doi: 10.3389/fcell.2021.795685. eCollection 2021. PMID: 34926473; PMCID: PMC8678412.
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Mitochondrial Quality Control Governed by Ubiquitin.

Frontiers in cell and developmental biology

Ravanelli S, den Brave F, Hoppe T.
PMID: 32391359
Front Cell Dev Biol. 2020 Apr 24;8:270. doi: 10.3389/fcell.2020.00270. eCollection 2020.

Mitochondria are essential organelles important for energy production, proliferation, and cell death. Biogenesis, homeostasis, and degradation of this organelle are tightly controlled to match cellular needs and counteract chronic stress conditions. Despite providing their own DNA, the vast majority...

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Ravanelli S, den Brave F, Hoppe T. Mitochondrial Quality Control Governed by Ubiquitin. Front Cell Dev Biol. 2020;8:270doi: 10.3389/fcell.2020.00270.
Ravanelli, S., den Brave, F., & Hoppe, T. (2020). Mitochondrial Quality Control Governed by Ubiquitin. Frontiers in cell and developmental biology, 8270. https://doi.org/10.3389/fcell.2020.00270
Ravanelli, Sonia, et al. "Mitochondrial Quality Control Governed by Ubiquitin." Frontiers in cell and developmental biology vol. 8 (2020): 270. doi: https://doi.org/10.3389/fcell.2020.00270
Ravanelli S, den Brave F, Hoppe T. Mitochondrial Quality Control Governed by Ubiquitin. Front Cell Dev Biol. 2020 Apr 24;8:270. doi: 10.3389/fcell.2020.00270. eCollection 2020. PMID: 32391359; PMCID: PMC7193050.
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USP7 and VCP.

Cell reports

Franz A, Valledor P, Ubieto-Capella P, Pilger D, Galarreta A, Lafarga V, Fernández-Llorente A, de la Vega-Barranco G, den Brave F, Hoppe T, Fernandez-Capetillo O, Lecona E.
PMID: 34644576
Cell Rep. 2021 Oct 12;37(2):109819. doi: 10.1016/j.celrep.2021.109819.

The AAA

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Franz A, Valledor P, Ubieto-Capella P, et al. USP7 and VCP. Cell Rep. 2021;37(2):109819doi: 10.1016/j.celrep.2021.109819.
Franz, A., Valledor, P., Ubieto-Capella, P., Pilger, D., Galarreta, A., Lafarga, V., Fernández-Llorente, A., de la Vega-Barranco, G., den Brave, F., Hoppe, T., Fernandez-Capetillo, O., & Lecona, E. (2021). USP7 and VCP. Cell reports, 37(2), 109819. https://doi.org/10.1016/j.celrep.2021.109819
Franz, André, et al. "USP7 and VCP." Cell reports vol. 37,2 (2021): 109819. doi: https://doi.org/10.1016/j.celrep.2021.109819
Franz A, Valledor P, Ubieto-Capella P, Pilger D, Galarreta A, Lafarga V, Fernández-Llorente A, de la Vega-Barranco G, den Brave F, Hoppe T, Fernandez-Capetillo O, Lecona E. USP7 and VCP. Cell Rep. 2021 Oct 12;37(2):109819. doi: 10.1016/j.celrep.2021.109819. PMID: 34644576; PMCID: PMC8527565.
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