Asset Details
MbrlCatalogueTitleDetail
Do you wish to reserve the book?
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
by
Holsboer, Florian
, Zannas, Anthony S.
, Drosten, Christian
, Rein, Theo
, Corman, Victor M.
, Hafner, Kathrin
, Zellner, Andreas
, Niemeyer, Daniela
, Gassen, Alwine
, Mösbauer, Kirstin
, Muth, Doreen
, Müller, Marcel A.
, Gassen, Nils C.
, Papies, Jan
, Herrmann, Alexander
, Boshart, Michael
, Martinelli, Silvia
, Brack-Werner, Ruth
, Müller-Myhsok, Bertram
in
13
/ 13/1
/ 13/109
/ 13/31
/ 13/44
/ 13/89
/ 13/95
/ 14/34
/ 14/35
/ 14/63
/ 38/70
/ 38/77
/ 45/29
/ 45/88
/ 631/326/596/1296
/ 631/337/474/2073
/ 631/80/39/2346
/ 82/80
/ 96/95
/ Animals
/ Autophagy
/ Autophagy - drug effects
/ Autophagy - immunology
/ Beclin-1 - metabolism
/ Chlorocebus aethiops
/ Coronaviridae
/ Coronavirus Infections - immunology
/ Coronavirus Infections - virology
/ Coronaviruses
/ Gene Knockdown Techniques
/ HEK293 Cells
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Lysine
/ Middle East Respiratory Syndrome Coronavirus - immunology
/ Middle East Respiratory Syndrome Coronavirus - pathogenicity
/ multidisciplinary
/ Phagocytosis
/ Proteasomes
/ Proteolysis - drug effects
/ S-Phase Kinase-Associated Proteins - antagonists & inhibitors
/ S-Phase Kinase-Associated Proteins - genetics
/ S-Phase Kinase-Associated Proteins - metabolism
/ Science
/ Science (multidisciplinary)
/ Skp2 protein
/ Ubiquitination
/ Ubiquitination - drug effects
/ Ubiquitination - immunology
/ Vero Cells
2019
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
You are currently in the queue to collect this book. You will be notified once it is your turn to collect the book.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
by
Holsboer, Florian
, Zannas, Anthony S.
, Drosten, Christian
, Rein, Theo
, Corman, Victor M.
, Hafner, Kathrin
, Zellner, Andreas
, Niemeyer, Daniela
, Gassen, Alwine
, Mösbauer, Kirstin
, Muth, Doreen
, Müller, Marcel A.
, Gassen, Nils C.
, Papies, Jan
, Herrmann, Alexander
, Boshart, Michael
, Martinelli, Silvia
, Brack-Werner, Ruth
, Müller-Myhsok, Bertram
in
13
/ 13/1
/ 13/109
/ 13/31
/ 13/44
/ 13/89
/ 13/95
/ 14/34
/ 14/35
/ 14/63
/ 38/70
/ 38/77
/ 45/29
/ 45/88
/ 631/326/596/1296
/ 631/337/474/2073
/ 631/80/39/2346
/ 82/80
/ 96/95
/ Animals
/ Autophagy
/ Autophagy - drug effects
/ Autophagy - immunology
/ Beclin-1 - metabolism
/ Chlorocebus aethiops
/ Coronaviridae
/ Coronavirus Infections - immunology
/ Coronavirus Infections - virology
/ Coronaviruses
/ Gene Knockdown Techniques
/ HEK293 Cells
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Lysine
/ Middle East Respiratory Syndrome Coronavirus - immunology
/ Middle East Respiratory Syndrome Coronavirus - pathogenicity
/ multidisciplinary
/ Phagocytosis
/ Proteasomes
/ Proteolysis - drug effects
/ S-Phase Kinase-Associated Proteins - antagonists & inhibitors
/ S-Phase Kinase-Associated Proteins - genetics
/ S-Phase Kinase-Associated Proteins - metabolism
/ Science
/ Science (multidisciplinary)
/ Skp2 protein
/ Ubiquitination
/ Ubiquitination - drug effects
/ Ubiquitination - immunology
/ Vero Cells
2019
Oops! Something went wrong.
While trying to remove the title from your shelf something went wrong :( Kindly try again later!
Do you wish to request the book?
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
by
Holsboer, Florian
, Zannas, Anthony S.
, Drosten, Christian
, Rein, Theo
, Corman, Victor M.
, Hafner, Kathrin
, Zellner, Andreas
, Niemeyer, Daniela
, Gassen, Alwine
, Mösbauer, Kirstin
, Muth, Doreen
, Müller, Marcel A.
, Gassen, Nils C.
, Papies, Jan
, Herrmann, Alexander
, Boshart, Michael
, Martinelli, Silvia
, Brack-Werner, Ruth
, Müller-Myhsok, Bertram
in
13
/ 13/1
/ 13/109
/ 13/31
/ 13/44
/ 13/89
/ 13/95
/ 14/34
/ 14/35
/ 14/63
/ 38/70
/ 38/77
/ 45/29
/ 45/88
/ 631/326/596/1296
/ 631/337/474/2073
/ 631/80/39/2346
/ 82/80
/ 96/95
/ Animals
/ Autophagy
/ Autophagy - drug effects
/ Autophagy - immunology
/ Beclin-1 - metabolism
/ Chlorocebus aethiops
/ Coronaviridae
/ Coronavirus Infections - immunology
/ Coronavirus Infections - virology
/ Coronaviruses
/ Gene Knockdown Techniques
/ HEK293 Cells
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Lysine
/ Middle East Respiratory Syndrome Coronavirus - immunology
/ Middle East Respiratory Syndrome Coronavirus - pathogenicity
/ multidisciplinary
/ Phagocytosis
/ Proteasomes
/ Proteolysis - drug effects
/ S-Phase Kinase-Associated Proteins - antagonists & inhibitors
/ S-Phase Kinase-Associated Proteins - genetics
/ S-Phase Kinase-Associated Proteins - metabolism
/ Science
/ Science (multidisciplinary)
/ Skp2 protein
/ Ubiquitination
/ Ubiquitination - drug effects
/ Ubiquitination - immunology
/ Vero Cells
2019
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
Journal Article
SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
2019
Request Book From Autostore
and Choose the Collection Method
Overview
Autophagy is an essential cellular process affecting virus infections and other diseases and Beclin1 (BECN1) is one of its key regulators. Here, we identified S-phase kinase-associated protein 2 (SKP2) as E3 ligase that executes lysine-48-linked poly-ubiquitination of BECN1, thus promoting its proteasomal degradation. SKP2 activity is regulated by phosphorylation in a hetero-complex involving FKBP51, PHLPP, AKT1, and BECN1. Genetic or pharmacological inhibition of SKP2 decreases BECN1 ubiquitination, decreases BECN1 degradation and enhances autophagic flux. Middle East respiratory syndrome coronavirus (MERS-CoV) multiplication results in reduced BECN1 levels and blocks the fusion of autophagosomes and lysosomes. Inhibitors of SKP2 not only enhance autophagy but also reduce the replication of MERS-CoV up to 28,000-fold. The SKP2-BECN1 link constitutes a promising target for host-directed antiviral drugs and possibly other autophagy-sensitive conditions.
Here, Gassen
et al
. show that S-phase kinase-associated protein 2 (SKP2) is responsible for lysine-48-linked poly-ubiquitination of beclin 1, resulting in its proteasomal degradation, and that inhibition of SKP2 enhances autophagy and reduces replication of MERS coronavirus.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/1
/ 13/109
/ 13/31
/ 13/44
/ 13/89
/ 13/95
/ 14/34
/ 14/35
/ 14/63
/ 38/70
/ 38/77
/ 45/29
/ 45/88
/ 82/80
/ 96/95
/ Animals
/ Coronavirus Infections - immunology
/ Coronavirus Infections - virology
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Lysine
/ Middle East Respiratory Syndrome Coronavirus - immunology
/ Middle East Respiratory Syndrome Coronavirus - pathogenicity
/ S-Phase Kinase-Associated Proteins - antagonists & inhibitors
/ S-Phase Kinase-Associated Proteins - genetics
/ S-Phase Kinase-Associated Proteins - metabolism
/ Science
This website uses cookies to ensure you get the best experience on our website.