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  • 1
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    Global landscape of HIV-human protein complexes (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-12-23
    Description: Human immunodeficiency virus (HIV) has a small genome and therefore relies heavily on the host cellular machinery to replicate. Identifying which host proteins and complexes come into physical contact with the viral proteins is crucial for a comprehensive understanding of how HIV rewires the host's cellular machinery during the course of infection. Here we report the use of affinity tagging and purification mass spectrometry to determine systematically the physical interactions of all 18 HIV-1 proteins and polyproteins with host proteins in two different human cell lines (HEK293 and Jurkat). Using a quantitative scoring system that we call MiST, we identified with high confidence 497 HIV-human protein-protein interactions involving 435 individual human proteins, with approximately 40% of the interactions being identified in both cell types. We found that the host proteins hijacked by HIV, especially those found interacting in both cell types, are highly conserved across primates. We uncovered a number of host complexes targeted by viral proteins, including the finding that HIV protease cleaves eIF3d, a subunit of eukaryotic translation initiation factor 3. This host protein is one of eleven identified in this analysis that act to inhibit HIV replication. This data set facilitates a more comprehensive and detailed understanding of how the host machinery is manipulated during the course of HIV infection.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3310911/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3310911/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jager, Stefanie -- Cimermancic, Peter -- Gulbahce, Natali -- Johnson, Jeffrey R -- McGovern, Kathryn E -- Clarke, Starlynn C -- Shales, Michael -- Mercenne, Gaelle -- Pache, Lars -- Li, Kathy -- Hernandez, Hilda -- Jang, Gwendolyn M -- Roth, Shoshannah L -- Akiva, Eyal -- Marlett, John -- Stephens, Melanie -- D'Orso, Ivan -- Fernandes, Jason -- Fahey, Marie -- Mahon, Cathal -- O'Donoghue, Anthony J -- Todorovic, Aleksandar -- Morris, John H -- Maltby, David A -- Alber, Tom -- Cagney, Gerard -- Bushman, Frederic D -- Young, John A -- Chanda, Sumit K -- Sundquist, Wesley I -- Kortemme, Tanja -- Hernandez, Ryan D -- Craik, Charles S -- Burlingame, Alma -- Sali, Andrej -- Frankel, Alan D -- Krogan, Nevan J -- P01 AI090935/AI/NIAID NIH HHS/ -- P01 AI090935-02/AI/NIAID NIH HHS/ -- P01 GM073732-05/GM/NIGMS NIH HHS/ -- P41 GM103481/GM/NIGMS NIH HHS/ -- P41 RR001081/RR/NCRR NIH HHS/ -- P41RR001614/RR/NCRR NIH HHS/ -- P50 GM081879/GM/NIGMS NIH HHS/ -- P50 GM081879-02/GM/NIGMS NIH HHS/ -- P50 GM082250/GM/NIGMS NIH HHS/ -- P50 GM082250-05/GM/NIGMS NIH HHS/ -- P50GM081879/GM/NIGMS NIH HHS/ -- P50GM082545/GM/NIGMS NIH HHS/ -- U54 RR022220/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Dec 21;481(7381):365-70. doi: 10.1038/nature10719.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22190034" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Amino Acid Sequence ; Conserved Sequence ; Eukaryotic Initiation Factor-3/chemistry/metabolism ; HEK293 Cells ; HIV Infections/metabolism/virology ; HIV Protease/metabolism ; HIV-1/*chemistry/*metabolism/physiology ; *Host-Pathogen Interactions ; Human Immunodeficiency Virus Proteins/analysis/chemistry/isolation & ; purification/*metabolism ; Humans ; Immunoprecipitation ; Jurkat Cells ; Mass Spectrometry ; Protein Binding ; Protein Interaction Mapping/*methods ; Protein Interaction Maps/*physiology ; Reproducibility of Results ; Virus Replication
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    CRL4AMBRA1 targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling (2018)
    Springer Nature
    Details
    Publication Date: 2018
    Description: 〈p〉Multi-subunit cullin-RING ligases (CRLs) are the largest family of ubiquitin E3 ligases in humans. CRL activity is tightly regulated to prevent unintended substrate degradation or autocatalytic degradation of CRL subunits. Using a proteomics strategy, we discovered that CRL4〈sup〉AMBRA〈/sup〉〈sup〉1〈/sup〉 (CRL substrate receptor denoted in superscript) targets Elongin C (ELOC), the essential adapter protein of CRL5 complexes, for polyubiquitination and degradation. We showed that the ubiquitin ligase function of CRL4〈sup〉AMBRA〈/sup〉〈sup〉1〈/sup〉 is required to disrupt the assembly and attenuate the ligase activity of human CRL5〈sup〉SOCS〈/sup〉〈sup〉3〈/sup〉 and HIV-1 CRL5〈sup〉VIF〈/sup〉 complexes as AMBRA1 depletion leads to hyperactivation of both CRL5 complexes. Moreover, CRL4〈sup〉AMBRA〈/sup〉〈sup〉1〈/sup〉 modulates interleukin-6/STAT3 signaling and HIV-1 infectivity that are regulated by CRL5〈sup〉SOCS〈/sup〉〈sup〉3〈/sup〉 and CRL5〈sup〉VIF〈/sup〉, respectively. Thus, by discovering a substrate of CRL4〈sup〉AMBRA〈/sup〉〈sup〉1〈/sup〉, ELOC, the shared adapter of CRL5 ubiquitin ligases, we uncovered a novel CRL cross-regulation pathway.〈/p〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
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  • 3
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    Springtail-inspired superomniphobic surface with extreme pressure resistance (2018)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2018-08-25
    Description: Both high static repellency and pressure resistance are critical to achieving a high-performance omniphobic surface. The cuticles of springtails have both of these features, which result from their hierarchical structure composed of primary doubly reentrant nanostructures on secondary microgrooves. Despite intensive efforts, none of the previous studies that were inspired by the springtail were able to simultaneously achieve both high static repellency and pressure resistance because of a general trade-off between these characteristics. We demonstrate for the first time a springtail-inspired superomniphobic surface displaying both features by fabricating a hierarchical system consisting of serif-T–shaped nanostructures on microscale wrinkles, overcoming previous limitations. Our biomimetic strategy yielded a surface showing high repellency to diverse liquids, from water to ethanol, with a contact angle above 150°. Simultaneously, the surface was able to endure extreme pressure resulting from the impacts of drops of water and of ethylene glycol with We 〉〉 200, and of ethanol with We ~ 53, which is the highest pressure resistance ever reported. Overall, the omniphobicity of our springtail-inspired fabricated system was found to be superior to that of the natural springtail cuticle itself.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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