Search Results - "Frankel, Alan D"

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  1. 1

    Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions by Carlson, Christopher R., Asfaha, Jonathan B., Ghent, Chloe M., Howard, Conor J., Hartooni, Nairi, Safari, Maliheh, Frankel, Alan D., Morgan, David O.

    Published in Molecular cell (17-12-2020)
    “…The nucleocapsid (N) protein of coronaviruses serves two major functions: compaction of the RNA genome in the virion and regulation of viral gene…”
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  2. 2

    RNA-mediated displacement of an inhibitory snRNP complex activates transcription elongation by Frankel, Alan D, D'Orso, Iván

    Published in Nature structural & molecular biology (01-07-2010)
    “…The HIV-1 Tat protein relieves a block to transcription elongation by recruiting positive transcription elongation factor b (P-TEFb) to an RNA element (TAR) on…”
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  3. 3

    Structural basis for cooperative RNA binding and export complex assembly by HIV Rev by Frankel, Alan D, Daugherty, Matthew D, Liu, Bella

    Published in Nature structural & molecular biology (01-11-2010)
    “…Nuclear HIV-1 mRNA export is mediated by cooperative Rev protein binding to the Rev response element (RRE) RNA, forming a complex recognized by the Crm1 host…”
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  4. 4

    Host cell factors in HIV replication: meta-analysis of genome-wide studies by Bushman, Frederic D, Malani, Nirav, Fernandes, Jason, D'Orso, Iván, Cagney, Gerard, Diamond, Tracy L, Zhou, Honglin, Hazuda, Daria J, Espeseth, Amy S, König, Renate, Bandyopadhyay, Sourav, Ideker, Trey, Goff, Stephen P, Krogan, Nevan J, Frankel, Alan D, Young, John A T, Chanda, Sumit K

    Published in PLoS pathogens (01-05-2009)
    “…We have analyzed host cell genes linked to HIV replication that were identified in nine genome-wide studies, including three independent siRNA screens…”
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  5. 5

    The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA by Booth, David S, Cheng, Yifan, Frankel, Alan D

    Published in eLife (08-12-2014)
    “…The HIV Rev protein routes viral RNAs containing the Rev Response Element (RRE) through the Crm1 nuclear export pathway to the cytoplasm where viral proteins…”
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  6. 6

    Functional and structural segregation of overlapping helices in HIV-1 by Safari, Maliheh, Jayaraman, Bhargavi, Yang, Shumin, Smith, Cynthia, Fernandes, Jason D, Frankel, Alan D

    Published in eLife (05-05-2022)
    “…Overlapping coding regions balance selective forces between multiple genes. One possible division of nucleotide sequence is that the predominant selective…”
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  7. 7

    Highly Mutable Linker Regions Regulate HIV-1 Rev Function and Stability by Jayaraman, Bhargavi, Fernandes, Jason D., Yang, Shumin, Smith, Cynthia, Frankel, Alan D.

    Published in Scientific reports (26-03-2019)
    “…HIV-1 Rev is an essential viral regulatory protein that facilitates the nuclear export of intron-containing viral mRNAs. It is organized into structured,…”
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  8. 8

    A Solution to Limited Genomic Capacity: Using Adaptable Binding Surfaces to Assemble the Functional HIV Rev Oligomer on RNA by Daugherty, Matthew D., D'Orso, Iván, Frankel, Alan D.

    Published in Molecular cell (26-09-2008)
    “…Many ribonucleoprotein (RNP) complexes assemble into large, organized structures in which protein subunits are positioned by interactions with RNA and other…”
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  9. 9

    Thermodynamics of Rev–RNA Interactions in HIV‑1 Rev–RRE Assembly by Jayaraman, Bhargavi, Mavor, David, Gross, John D, Frankel, Alan D

    Published in Biochemistry (Easton) (27-10-2015)
    “…The HIV-1 protein Rev facilitates the nuclear export of intron-containing viral mRNAs by recognizing a structured RNA site, the Rev-response-element (RRE),…”
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  10. 10

    RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev-Rev response element complex by Jayaraman, Bhargavi, Crosby, David C, Homer, Christina, Ribeiro, Isabel, Mavor, David, Frankel, Alan D

    Published in eLife (08-12-2014)
    “…The HIV-1 protein Rev controls a critical step in viral replication by mediating the nuclear export of unspliced and singly-spliced viral mRNAs. Multiple Rev…”
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  11. 11

    Tat acetylation modulates assembly of a viral-host RNA-protein transcription complex by D'Orso, Iván, Frankel, Alan D

    “…HIV-1 Tat enhances viral transcription elongation by forming a ribonucleoprotein complex with transactivating responsive (TAR) RNA and P-TEFb, an elongation…”
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  12. 12

    The HIV-1 Tat protein recruits a ubiquitin ligase to reorganize the 7SK snRNP for transcriptional activation by Faust, Tyler B, Li, Yang, Bacon, Curtis W, Jang, Gwendolyn M, Weiss, Amit, Jayaraman, Bhargavi, Newton, Billy W, Krogan, Nevan J, D'Orso, Iván, Frankel, Alan D

    Published in eLife (30-05-2018)
    “…The HIV-1 Tat protein hijacks P-TEFb kinase to activate paused RNA polymerase II (RNAP II) at the viral promoter. Tat binds additional host factors, but it is…”
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  13. 13

    Oligomeric viral proteins: small in size, large in presence by Jayaraman, Bhargavi, Smith, Amber M, Fernandes, Jason D, Frankel, Alan D

    “…Viruses are obligate parasites that rely heavily on host cellular processes for replication. The small number of proteins typically encoded by a virus is faced…”
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  14. 14

    HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes by Daugherty, Matthew D., Booth, David S., Jayaraman, Bhargavi, Cheng, Yifan, Frankel, Alan D., Yamamoto, Keith R.

    “…RNA is a crucial structural component of many ribonucleoprotein (RNP) complexes, including the ribosome, spliceosome, and signal recognition particle, but the…”
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  15. 15

    A structurally plastic ribonucleoprotein complex mediates post-transcriptional gene regulation in HIV-1 by Fernandes, Jason D., Booth, David S., Frankel, Alan D.

    Published in Wiley interdisciplinary reviews. RNA (01-07-2016)
    “…HIV replication requires the nuclear export of essential, intron‐containing viral RNAs. To facilitate export, HIV encodes the viral accessory protein Rev which…”
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  16. 16

    Transition Step during Assembly of HIV Tat:P-TEFb Transcription Complexes and Transfer to TAR RNA by D'Orso, Iván, Jang, Gwendolyn M, Pastuszak, Alexander W, Faust, Tyler B, Quezada, Elizabeth, Booth, David S, Frankel, Alan D

    Published in Molecular and Cellular Biology (01-12-2012)
    “…Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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  17. 17

    Making Sense of Multifunctional Proteins: Human Immunodeficiency Virus Type 1 Accessory and Regulatory Proteins and Connections to Transcription by Faust, Tyler B, Binning, Jennifer M, Gross, John D, Frankel, Alan D

    Published in Annual review of virology (29-09-2017)
    “…Viruses are completely dependent upon cellular machinery to support replication and have therefore developed strategies to co-opt cellular processes to…”
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  18. 18

    GPS-Prot: a web-based visualization platform for integrating host-pathogen interaction data by Fahey, Marie E, Bennett, Melanie J, Mahon, Cathal, Jäger, Stefanie, Pache, Lars, Kumar, Dhiraj, Shapiro, Alex, Rao, Kanury, Chanda, Sumit K, Craik, Charles S, Frankel, Alan D, Krogan, Nevan J

    Published in BMC bioinformatics (22-07-2011)
    “…The increasing availability of HIV-host interaction datasets, including both physical and genetic interactions, has created a need for software tools to…”
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  19. 19

    HIV-1: Fifteen Proteins and an RNA by Frankel, Alan D, Young, John A. T

    Published in Annual review of biochemistry (01-01-1998)
    “…Human immunodeficiency virus type 1 is a complex retrovirus encoding 15 distinct proteins. Substantial progress has been made toward understanding the function…”
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  20. 20

    Recognition of Nucleic Acid Bases and Base-pairs by Hydrogen Bonding to Amino Acid Side-chains by Cheng, Alan C., Chen, William W., Fuhrmann, Cynthia N., Frankel, Alan D.

    Published in Journal of molecular biology (04-04-2003)
    “…Sequence-specific protein–nucleic acid recognition is determined, in part, by hydrogen bonding interactions between amino acid side-chains and nucleotide…”
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