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Article ; Online: Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.

Lopez, Kyle E / Rizo, Alexandrea N / Tse, Eric / Lin, JiaBei / Scull, Nathaniel W / Thwin, Aye C / Lucius, Aaron L / Shorter, James / Southworth, Daniel R

Nature structural & molecular biology

2020 Volume 27, Issue 5, Page(s) 406–416

Abstract: The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high- ... ...

Abstract	The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high-resolution structures of wild-type Escherichia coli ClpAP undergoing active substrate unfolding and proteolysis. A spiral of pore loop-substrate contacts spans both ClpA AAA+ domains. Protomers at the spiral seam undergo nucleotide-specific rearrangements, supporting substrate translocation. IGL loops extend flexibly to bind the planar, heptameric ClpP surface with the empty, symmetry-mismatched IGL pocket maintained at the seam. Three different structures identify a binding-pocket switch by the IGL loop of the lowest positioned protomer, involving release and re-engagement with the clockwise pocket. This switch is coupled to a ClpA rotation and a network of conformational changes across the seam, suggesting that ClpA can rotate around the ClpP apical surface during processive steps of translocation and proteolysis.
MeSH term(s)	Adenosine Triphosphate/analogs & derivatives ; Adenosine Triphosphate/metabolism ; Cryoelectron Microscopy ; DNA Helicases/metabolism ; Endopeptidase Clp/chemistry ; Endopeptidase Clp/genetics ; Endopeptidase Clp/metabolism ; Escherichia coli/chemistry ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Models, Molecular ; Multiprotein Complexes ; Protein Conformation ; Protein Unfolding ; Trans-Activators/metabolism
Chemical Substances	Escherichia coli Proteins ; Multiprotein Complexes ; Trans-Activators ; replication initiator protein ; adenosine 5'-O-(3-thiotriphosphate) (35094-46-3) ; Adenosine Triphosphate (8L70Q75FXE) ; ClpA protease, E coli (EC 3.4.21.53) ; ClpP protease, E coli (EC 3.4.21.92) ; Endopeptidase Clp (EC 3.4.21.92) ; DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2020-04-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Video-Audio Media
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-020-0409-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Robust Sequence Determinants of α-Synuclein Toxicity in Yeast Implicate Membrane Binding.

Newberry, Robert W / Arhar, Taylor / Costello, Jean / Hartoularos, George C / Maxwell, Alison M / Naing, Zun Zar Chi / Pittman, Maureen / Reddy, Nishith R / Schwarz, Daniel M C / Wassarman, Douglas R / Wu, Taia S / Barrero, Daniel / Caggiano, Christa / Catching, Adam / Cavazos, Taylor B / Estes, Laurel S / Faust, Bryan / Fink, Elissa A / Goldman, Miriam A /

Gomez, Yessica K / Gordon, M Grace / Gunsalus, Laura M / Hoppe, Nick / Jaime-Garza, Maru / Johnson, Matthew C / Jones, Matthew G / Kung, Andrew F / Lopez, Kyle E / Lumpe, Jared / Martyn, Calla / McCarthy, Elizabeth E / Miller-Vedam, Lakshmi E / Navarro, Erik J / Palar, Aji / Pellegrino, Jenna / Saylor, Wren / Stephens, Christina A / Strickland, Jack / Torosyan, Hayarpi / Wankowicz, Stephanie A / Wong, Daniel R / Wong, Garrett / Redding, Sy / Chow, Eric D / DeGrado, William F / Kampmann, Martin

ACS chemical biology

2020 Volume 15, Issue 8, Page(s) 2137–2153

Abstract: Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific ... ...

Abstract	Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins
MeSH term(s)	Amino Acid Sequence ; Humans ; Mutation ; Parkinson Disease/metabolism ; Protein Conformation ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/metabolism ; alpha-Synuclein/chemistry ; alpha-Synuclein/genetics ; alpha-Synuclein/toxicity
Chemical Substances	alpha-Synuclein
Language	English
Publishing date	2020-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.0c00339
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

Gupta, Meghna / Azumaya, Caleigh M / Moritz, Michelle / Pourmal, Sergei / Diallo, Amy / Merz, Gregory E / Jang, Gwendolyn / Bouhaddou, Mehdi / Fossati, Andrea / Brilot, Axel F / Diwanji, Devan / Hernandez, Evelyn / Herrera, Nadia / Kratochvil, Huong T / Lam, Victor L / Li, Fei / Li, Yang / Nguyen, Henry C / Nowotny, Carlos /

Owens, Tristan W / Peters, Jessica K / Rizo, Alexandrea N / Schulze-Gahmen, Ursula / Smith, Amber M / Young, Iris D / Yu, Zanlin / Asarnow, Daniel / Billesbølle, Christian / Campbell, Melody G / Chen, Jen / Chen, Kuei-Ho / Chio, Un Seng / Dickinson, Miles Sasha / Doan, Loan / Jin, Mingliang / Kim, Kate / Li, Junrui / Li, Yen-Li / Linossi, Edmond / Liu, Yanxin / Lo, Megan / Lopez, Jocelyne / Lopez, Kyle E / Mancino, Adamo / Moss, Frank R / Paul, Michael D / Pawar, Komal Ishwar / Pelin, Adrian / Pospiech, Thomas H / Puchades, Cristina / Remesh, Soumya Govinda / Safari, Maliheh / Schaefer, Kaitlin / Sun, Ming / Tabios, Mariano C / Thwin, Aye C / Titus, Erron W / Trenker, Raphael / Tse, Eric / Tsui, Tsz Kin Martin / Wang, Feng / Zhang, Kaihua / Zhang, Yang / Zhao, Jianhua / Zhou, Fengbo / Zhou, Yuan / Zuliani-Alvarez, Lorena / Agard, David A / Cheng, Yifan / Fraser, James S / Jura, Natalia / Kortemme, Tanja / Manglik, Aashish / Southworth, Daniel R / Stroud, Robert M / Swaney, Danielle L / Krogan, Nevan J / Frost, Adam / Rosenberg, Oren S / Verba, Kliment A

Research square

2021

Abstract: The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo- ... ...

Abstract	The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIGYF2, an inhibitor of translation initiation and modulator of ribosome-associated quality control. Our work suggests a potential role of Nsp2 in linking viral transcription within the viral replication-transcription complexes (RTC) to the translation initiation of the viral message. Collectively, the structure reported here, combined with mutant interaction mapping, provides a foundation for functional studies of this evolutionary conserved coronavirus protein and may assist future drug design.
Language	English
Publishing date	2021-05-19
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-515215/v1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

bioRxiv : the preprint server for biology

2021

Abstract	The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIGYF2, an inhibitor of translation initiation and modulator of ribosome-associated quality control. Our work suggests a potential role of Nsp2 in linking viral transcription within the viral replication-transcription complexes (RTC) to the translation initiation of the viral message. Collectively, the structure reported here, combined with mutant interaction mapping, provides a foundation for functional studies of this evolutionary conserved coronavirus protein and may assist future drug design.
Language	English
Publishing date	2021-05-11
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.05.10.443524
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes

Gupta, Meghna / Azumaya, Caleigh M. / Moritz, Michelle / Pourmal, Sergei / Diallo, Amy / Merz, Gregory E. / Jang, Gwendolyn / Bouhaddou, Mehdi / Fossati, Andrea / Brilot, Axel F. / Diwanji, Devan / Hernandez, Evelyn / Herrera, Nadia / Kratochvil, Huong T. / Lam, Victor L. / Li, Fei / Li, Yang / Nguyen, Henry C. / Nowotny, Carlos /

Owens, Tristan W. / Peters, Jessica K. / Rizo, Alexandrea N. / Schulze-Gahmen, Ursula / Smith, Amber M. / Young, Iris D. / Yu, Zanlin / Asarnow, Daniel / Billesbølle, Christian / Campbell, Melody G. / Chen, Jen / Chen, Kuei-Ho / Chio, Un Seng / Dickinson, Miles Sasha / Doan, Loan / Jin, Mingliang / Kim, Kate / Li, Junrui / Li, Yen-Li / Linossi, Edmond / Liu, Yanxin / Lo, Megan / Lopez, Jocelyne / Lopez, Kyle E. / Mancino, Adamo / Moss, Frank R. / Paul, Michael D. / Pawar, Komal Ishwar / Pelin, Adrian / Pospiech, Thomas H. / Puchades, Cristina / Remesh, Soumya Govinda / Safari, Maliheh / Schaefer, Kaitlin / Sun, Ming / Tabios, Mariano C / Thwin, Aye C. / Titus, Erron W. / Trenker, Raphael / Tse, Eric / Tsui, Tsz Kin Martin / Wang, Feng / Zhang, Kaihua / Zhang, Yang / Zhao, Jianhua / Zhou, Fengbo / Zhou, Yuan / Zuliani-Alvarez, Lorena / QCRG Structural Biology Consortium / Agard, David A / Cheng, Yifan / Fraser, James S / Jura, Natalia / Kortemme, Tanja / Manglik, Aashish / Southworth, Daniel R. / Stroud, Robert M / Swaney, Danielle L / Krogan, Nevan J / Frost, Adam / Rosenberg, Oren S / Verba, Kliment A

bioRxiv

Abstract	The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIGYF2, an inhibitor of translation initiation and modulator of ribosome-associated quality control. Our work suggests a potential role of Nsp2 in linking viral transcription within the viral replication-transcription complexes (RTC) to the translation initiation of the viral message. Collectively, the structure reported here, combined with mutant interaction mapping, provides a foundation for functional studies of this evolutionary conserved coronavirus protein and may assist future drug design.
Keywords	covid19
Language	English
Publishing date	2021-05-12
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.05.10.443524
Database	COVID19

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Article ; Online: Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.

Gordon, David E / Hiatt, Joseph / Bouhaddou, Mehdi / Rezelj, Veronica V / Ulferts, Svenja / Braberg, Hannes / Jureka, Alexander S / Obernier, Kirsten / Guo, Jeffrey Z / Batra, Jyoti / Kaake, Robyn M / Weckstein, Andrew R / Owens, Tristan W / Gupta, Meghna / Pourmal, Sergei / Titus, Erron W / Cakir, Merve / Soucheray, Margaret / McGregor, Michael /

2020

Abstract: The COVID-19 (Coronavirus disease-2019) pandemic, caused by the SARS-CoV-2 coronavirus, is a significant threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and ... ...

Abstract	The COVID-19 (Coronavirus disease-2019) pandemic, caused by the SARS-CoV-2 coronavirus, is a significant threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and MERS-CoV. Here, we have carried out comparative viral-human protein-protein interaction and viral protein localization analysis for all three viruses. Subsequent functional genetic screening identified host factors that functionally impinge on coronavirus proliferation, including Tom70, a mitochondrial chaperone protein that interacts with both SARS-CoV-1 and SARS-CoV-2 Orf9b, an interaction we structurally characterized using cryo-EM. Combining genetically-validated host factors with both COVID-19 patient genetic data and medical billing records identified important molecular mechanisms and potential drug treatments that merit further molecular and clinical study.
Keywords	QCRG Structural Biology Consortium ; Zoonomia Consortium ; General Science & Technology ; covid19
Subject code	572
Publishing date	2020-10-15
Publisher	eScholarship, University of California
Publishing country	us
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.

Cakir, Zeynep / Jang, Gwendolyn / O'Meara, Matthew J / Tummino, Tia A / Zhang, Ziyang / Foussard, Helene / Rojc, Ajda / Zhou, Yuan / Kuchenov, Dmitry / Hüttenhain, Ruth / Xu, Jiewei / Eckhardt, Manon / Swaney, Danielle L / Fabius, Jacqueline M / Ummadi, Manisha / Tutuncuoglu, Beril / Rathore, Ujjwal / Modak, Maya / Haas, Paige / Haas, Kelsey M / Naing, Zun Zar Chi / Pulido, Ernst H / Shi, Ying / Barrio-Hernandez, Inigo / Memon, Danish / Petsalaki, Eirini / Dunham, Alistair / Marrero, Miguel Correa / Burke, David / Koh, Cassandra / Vallet, Thomas / Silvas, Jesus A / Azumaya, Caleigh M / Billesbølle, Christian / Brilot, Axel F / Campbell, Melody G / Diallo, Amy / Dickinson, Miles Sasha / Diwanji, Devan / Herrera, Nadia / Hoppe, Nick / Kratochvil, Huong T / Liu, Yanxin / Merz, Gregory E / Moritz, Michelle / Nguyen, Henry C / Nowotny, Carlos / Puchades, Cristina / Rizo, Alexandrea N / Schulze-Gahmen, Ursula / Smith, Amber M / Sun, Ming / Young, Iris D / Zhao, Jianhua / Asarnow, Daniel / Biel, Justin / Bowen, Alisa / Braxton, Julian R / Chen, Jen / Chio, Cynthia M / Chio, Un Seng / Deshpande, Ishan / Doan, Loan / Faust, Bryan / Flores, Sebastian / Jin, Mingliang / Kim, Kate / Lam, Victor L / Li, Fei / Li, Junrui / Li, Yen-Li / Li, Yang / Liu, Xi / Lo, Megan / Lopez, Kyle E / Melo, Arthur A / Moss, Frank R / Nguyen, Phuong / Paulino, Joana / Pawar, Komal Ishwar / Peters, Jessica K / Pospiech, Thomas H / Safari, Maliheh / Sangwan, Smriti / Schaefer, Kaitlin / Thomas, Paul V / Thwin, Aye C / Trenker, Raphael / Tse, Eric / Tsui, Tsz Kin Martin / Wang, Feng / Whitis, Natalie / Yu, Zanlin / Zhang, Kaihua / Zhang, Yang / Zhou, Fengbo / Saltzberg, Daniel / Hodder, Anthony J / Shun-Shion, Amber S / Williams, Daniel M / White, Kris M / Rosales, Romel / Kehrer, Thomas / Miorin, Lisa / Moreno, Elena / Patel, Arvind H / Rihn, Suzannah / Khalid, Mir M / Vallejo-Gracia, Albert / Fozouni, Parinaz / Simoneau, Camille R / Roth, Theodore L / Wu, David / Karim, Mohd Anisul / Ghoussaini, Maya / Dunham, Ian / Berardi, Francesco / Weigang, Sebastian / Chazal, Maxime / Park, Jisoo / Logue, James / McGrath, Marisa / Weston, Stuart / Haupt, Robert / Hastie, C James / Elliott, Matthew / Brown, Fiona / Burness, Kerry A / Reid, Elaine / Dorward, Mark / Johnson, Clare / Wilkinson, Stuart G / Geyer, Anna / Giesel, Daniel M / Baillie, Carla / Raggett, Samantha / Leech, Hannah / Toth, Rachel / Goodman, Nicola / Keough, Kathleen C / Lind, Abigail L / Klesh, Reyna J / Hemphill, Kafi R / Carlson-Stevermer, Jared / Oki, Jennifer / Holden, Kevin / Maures, Travis / Pollard, Katherine S / Sali, Andrej / Agard, David A / Cheng, Yifan / Fraser, James S / Frost, Adam / Jura, Natalia / Kortemme, Tanja / Manglik, Aashish / Southworth, Daniel R / Stroud, Robert M / Alessi, Dario R / Davies, Paul / Frieman, Matthew B / Ideker, Trey / Abate, Carmen / Jouvenet, Nolwenn / Kochs, Georg / Shoichet, Brian / Ott, Melanie / Palmarini, Massimo / Shokat, Kevan M / García-Sastre, Adolfo / Rassen, Jeremy A / Grosse, Robert / Rosenberg, Oren S / Verba, Kliment A / Basler, Christopher F / Vignuzzi, Marco / Peden, Andrew A / Beltrao, Pedro / Krogan, Nevan J

Science (New York, N.Y.)

2020 Volume 370, Issue 6521

Abstract: The COVID-19 pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), is a grave threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and ...

Abstract	The COVID-19 pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), is a grave threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and Middle East respiratory syndrome coronavirus (MERS-CoV). Here, we have carried out comparative viral-human protein-protein interaction and viral protein localization analyses for all three viruses. Subsequent functional genetic screening identified host factors that functionally impinge on coronavirus proliferation, including Tom70, a mitochondrial chaperone protein that interacts with both SARS-CoV-1 and SARS-CoV-2 ORF9b, an interaction we structurally characterized using cryo-electron microscopy. Combining genetically validated host factors with both COVID-19 patient genetic data and medical billing records identified molecular mechanisms and potential drug treatments that merit further molecular and clinical study.
MeSH term(s)	COVID-19/metabolism ; Conserved Sequence ; Coronavirus Nucleocapsid Proteins/genetics ; Coronavirus Nucleocapsid Proteins/metabolism ; Cryoelectron Microscopy ; Host Microbial Interactions ; Humans ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Precursor Protein Import Complex Proteins ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Conformation ; Protein Interaction Maps ; Severe acute respiratory syndrome-related coronavirus/metabolism ; SARS-CoV-2/metabolism ; Severe Acute Respiratory Syndrome/metabolism
Chemical Substances	Coronavirus Nucleocapsid Proteins ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Precursor Protein Import Complex Proteins ; Phosphoproteins ; TOMM70 protein, human ; nucleocapsid phosphoprotein, SARS-CoV-2
Keywords	covid19
Language	English
Publishing date	2020-10-15
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abe9403
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms

Gordon, David E. / Hiatt, Joseph / Bouhaddou, Mehdi / Rezelj, Veronica V. / Ulferts, Svenja / Braberg, Hannes / Jureka, Alexander S. / Obernier, Kirsten / Guo, Jeffrey Z. / Batra, Jyoti / Kaake, Robyn M. / Weckstein, Andrew R. / Owens, Tristan W. / Gupta, Meghna / Pourmal, Sergei / Titus, Erron W. / Cakir, Merve / Soucheray, Margaret / McGregor, Michael /

Cakir, Zeynep / Jang, Gwendolyn / O’Meara, Matthew J. / Tummino, Tia A. / Zhang, Ziyang / Foussard, Helene / Rojc, Ajda / Zhou, Yuan / Kuchenov, Dmitry / Hüttenhain, Ruth / Xu, Jiewei / Eckhardt, Manon / Swaney, Danielle L. / Fabius, Jacqueline M. / Ummadi, Manisha / Tutuncuoglu, Beril / Rathore, Ujjwal / Modak, Maya / Haas, Paige / Haas, Kelsey M. / Naing, Zun Zar Chi / Pulido, Ernst H. / Shi, Ying / Barrio-Hernandez, Inigo / Memon, Danish / Petsalaki, Eirini / Dunham, Alistair / Marrero, Miguel Correa / Burke, David / Koh, Cassandra / Vallet, Thomas / Silvas, Jesus A. / Azumaya, Caleigh M. / Billesbølle, Christian / Brilot, Axel F. / Campbell, Melody G. / Diallo, Amy / Dickinson, Miles Sasha / Diwanji, Devan / Herrera, Nadia / Hoppe, Nick / Kratochvil, Huong T. / Liu, Yanxin / Merz, Gregory E. / Moritz, Michelle / Nguyen, Henry C. / Nowotny, Carlos / Puchades, Cristina / Rizo, Alexandrea N. / Schulze-Gahmen, Ursula / Smith, Amber M. / Sun, Ming / Young, Iris D. / Zhao, Jianhua / Asarnow, Daniel / Biel, Justin / Bowen, Alisa / Braxton, Julian R. / Chen, Jen / Chio, Cynthia M. / Chio, Un Seng / Deshpande, Ishan / Doan, Loan / Faust, Bryan / Flores, Sebastian / Jin, Mingliang / Kim, Kate / Lam, Victor L. / Li, Fei / Li, Junrui / Li, Yen-Li / Li, Yang / Liu, Xi / Lo, Megan / Lopez, Kyle E. / Melo, Arthur A. / Moss, Frank R. / Nguyen, Phuong / Paulino, Joana / Pawar, Komal Ishwar / Peters, Jessica K. / Pospiech, Thomas H. / Safari, Maliheh / Sangwan, Smriti / Schaefer, Kaitlin / Thomas, Paul V. / Thwin, Aye C. / Trenker, Raphael / Tse, Eric / Tsui, Tsz Kin Martin / Wang, Feng / Whitis, Natalie / Yu, Zanlin / Zhang, Kaihua / Zhang, Yang / Zhou, Fengbo / Saltzberg, Daniel / Hodder, Anthony J. / Shun-Shion, Amber S. / Williams, Daniel M. / White, Kris M. / Rosales, Romel / Kehrer, Thomas / Miorin, Lisa / Moreno, Elena / Patel, Arvind H. / Rihn, Suzannah / Khalid, Mir M. / Vallejo-Gracia, Albert / Fozouni, Parinaz / Simoneau, Camille R. / Roth, Theodore L. / Wu, David / Karim, Mohd Anisul / Ghoussaini, Maya / Dunham, Ian / Berardi, Francesco / Weigang, Sebastian / Chazal, Maxime / Park, Jisoo / Logue, James / McGrath, Marisa / Weston, Stuart / Haupt, Robert / Hastie, C. James / Elliott, Matthew / Brown, Fiona / Burness, Kerry A. / Reid, Elaine / Dorward, Mark / Johnson, Clare / Wilkinson, Stuart G. / Geyer, Anna / Giesel, Daniel M. / Baillie, Carla / Raggett, Samantha / Leech, Hannah / Toth, Rachel / Goodman, Nicola / Keough, Kathleen C. / Lind, Abigail L. / Klesh, Reyna J. / Hemphill, Kafi R. / Carlson-Stevermer, Jared / Oki, Jennifer / Holden, Kevin / Maures, Travis / Pollard, Katherine S. / Sali, Andrej / Agard, David A. / Cheng, Yifan / Fraser, James S. / Frost, Adam / Jura, Natalia / Kortemme, Tanja / Manglik, Aashish / Southworth, Daniel R. / Stroud, Robert M. / Alessi, Dario R. / Davies, Paul / Frieman, Matthew B. / Ideker, Trey / Abate, Carmen / Jouvenet, Nolwenn / Kochs, Georg / Shoichet, Brian / Ott, Melanie / Palmarini, Massimo / Shokat, Kevan M. / García-Sastre, Adolfo / Rassen, Jeremy A. / Grosse, Robert / Rosenberg, Oren S. / Verba, Kliment A. / Basler, Christopher F. / Vignuzzi, Marco / Peden, Andrew A. / Beltrao, Pedro / Krogan, Nevan J.

Science

2020 , Page(s) eabe9403

Abstract	The COVID-19 (Coronavirus disease-2019) pandemic, caused by the SARS-CoV-2 coronavirus, is a significant threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and MERS-CoV. Here, we have carried out comparative viral-human protein-protein interaction and viral protein localization analysis for all three viruses. Subsequent functional genetic screening identified host factors that functionally impinge on coronavirus proliferation, including Tom70, a mitochondrial chaperone protein that interacts with both SARS-CoV-1 and SARS-CoV-2 Orf9b, an interaction we structurally characterized using cryo-EM. Combining genetically-validated host factors with both COVID-19 patient genetic data and medical billing records identified important molecular mechanisms and potential drug treatments that merit further molecular and clinical study.
Keywords	Multidisciplinary ; covid19
Language	English
Publisher	American Association for the Advancement of Science (AAAS)
Publishing country	us
Document type	Article ; Online
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abe9403
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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