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  1. Article: Funding above and beyond scientific research. An interview with Thomas R. Cech, President of the Howard Hughes Medical Institute in Chevy Chase, MD. Interviewed by Holger Breithaupt.

    Cech, T

    EMBO reports

    2001  Volume 2, Issue 9, Page(s) 751–754

    MeSH term(s) Animals ; Ecology ; Europe ; Genetic Techniques ; Humans ; Organization and Administration ; Research/trends ; Research Support as Topic ; United States
    Language English
    Publishing date 2001-08-23
    Publishing country England
    Document type Interview
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.1093/embo-reports/kve192
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    Zs.A 5433: Show issues Location:
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  2. Article ; Online: Telomerase misbehaves after a breakup.

    Arnoult, Nausica / Cech, Thomas R

    Science (New York, N.Y.)

    2024  Volume 383, Issue 6684, Page(s) 702–703

    Abstract: Suppressing telomerase action at broken DNA preserves genome integrity. ...

    Abstract Suppressing telomerase action at broken DNA preserves genome integrity.
    MeSH term(s) DNA Repair ; Telomerase/genetics ; Telomerase/metabolism ; Telomere/genetics ; Telomere/metabolism ; DNA Breaks, Double-Stranded ; Humans
    Chemical Substances Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2024-02-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.adn7791
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: RNA in biological condensates.

    Cech, Thomas R

    RNA (New York, N.Y.)

    2021  Volume 28, Issue 1, Page(s) 1–2

    MeSH term(s) Animals ; Biomolecular Condensates/chemistry ; Biomolecular Condensates/metabolism ; Cell Compartmentation ; Humans ; Organelles/chemistry ; Organelles/genetics ; Organelles/metabolism ; RNA/chemistry ; RNA/classification ; RNA/genetics ; RNA/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances RNA-Binding Proteins ; RNA (63231-63-0)
    Language English
    Publishing date 2021-12-10
    Publishing country United States
    Document type Introductory Journal Article
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.079051.121
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  4. Article: Transcription factors ERα and Sox2 have differing multiphasic DNA and RNA binding mechanisms.

    Hemphill, Wayne O / Steiner, Halley R / Kominsky, Jackson R / Wuttke, Deborah S / Cech, Thomas R

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Many transcription factors (TFs) have been shown to bind RNA, leading to open questions regarding the mechanism(s) of this RNA binding and its role in regulating TF activities. Here we use biophysical assays to interrogate ... ...

    Abstract Many transcription factors (TFs) have been shown to bind RNA, leading to open questions regarding the mechanism(s) of this RNA binding and its role in regulating TF activities. Here we use biophysical assays to interrogate the
    Language English
    Publishing date 2024-03-19
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.18.585577
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  5. Article ; Online: Publisher Correction: Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization.

    Lim, Ci Ji / Cech, Thomas R

    Nature reviews. Molecular cell biology

    2021  Volume 22, Issue 4, Page(s) 299

    Language English
    Publishing date 2021-02-19
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-021-00353-x
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  6. Article ; Online: Transcription factors ERα and Sox2 have differing multiphasic DNA and RNA binding mechanisms.

    Hemphill, Wayne O / Steiner, Halley R / Kominsky, Jackson R / Wuttke, Deborah S / Cech, Thomas R

    RNA (New York, N.Y.)

    2024  

    Abstract: Many transcription factors (TFs) have been shown to bind RNA, leading to open questions regarding the mechanism(s) of this RNA binding and its role in regulating TF activities. Here we use biophysical assays to interrogate the kon, koff, and Kd for DNA ... ...

    Abstract Many transcription factors (TFs) have been shown to bind RNA, leading to open questions regarding the mechanism(s) of this RNA binding and its role in regulating TF activities. Here we use biophysical assays to interrogate the kon, koff, and Kd for DNA and RNA binding of two model human transcription factors, ERα and Sox2. Unexpectedly, we found that both proteins exhibited multiphasic nucleic acid binding kinetics. We propose that Sox2 RNA and DNA multiphasic binding kinetics could be explained by a conventional model for sequential Sox2 monomer association and dissociation. In contrast, ERα nucleic acid binding exhibited biphasic dissociation paired with novel triphasic association behavior, where two apparent binding transitions are separated by a 10-20 min "lag" phase depending on protein concentration. We considered several conventional models for the observed kinetic behavior, none of which adequately explained all the ERα nucleic acid binding data. Instead, simulations with a model incorporating sequential ERα monomer association, ERα nucleic acid complex isomerization, and product "feedback" on isomerization rate recapitulated the general kinetic trends for both ERα DNA and RNA binding. Collectively, our findings reveal that Sox2 and ERα bind RNA and DNA with previously unappreciated multiphasic binding kinetics, and that their reaction mechanisms differ with ERα binding nucleic acids via a novel reaction mechanism.
    Language English
    Publishing date 2024-05-17
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.080027.124
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  7. Article ; Online: A Lifelong Passion for All Things Ribonucleic.

    Cech, Thomas R

    Cell

    2018  Volume 175, Issue 1, Page(s) 14–17

    Abstract: This year's Lasker-Koshland Special Achievement Award is given to Joan Argetsinger Steitz for her RNA research discoveries and her exemplary international leadership. ...

    Abstract This year's Lasker-Koshland Special Achievement Award is given to Joan Argetsinger Steitz for her RNA research discoveries and her exemplary international leadership.
    MeSH term(s) Awards and Prizes ; Biomedical Research ; History, 21st Century ; Humans ; RNA/history ; RNA/metabolism ; RNA/physiology ; Ribonucleoproteins, Small Nuclear/metabolism ; Ribonucleoproteins, Small Nuclear/physiology
    Chemical Substances Ribonucleoproteins, Small Nuclear ; RNA (63231-63-0)
    Language English
    Publishing date 2018-09-11
    Publishing country United States
    Document type Autobiography ; Historical Article ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2018.08.037
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  8. Article ; Online: Targeted mutagenesis in human iPSCs using CRISPR genome-editing tools.

    Long, Yicheng / Cech, Thomas R

    Methods (San Diego, Calif.)

    2021  Volume 191, Page(s) 44–58

    Abstract: Mutagenesis studies have rapidly evolved in the era of CRISPR genome editing. Precise manipulation of genes in human induced pluripotent stem cells (iPSCs) allows biomedical researchers to study the physiological functions of individual genes during ... ...

    Abstract Mutagenesis studies have rapidly evolved in the era of CRISPR genome editing. Precise manipulation of genes in human induced pluripotent stem cells (iPSCs) allows biomedical researchers to study the physiological functions of individual genes during development. Furthermore, such genetic manipulation applied to patient-specific iPSCs allows disease modeling, drug screening and development of therapeutics. Although various genome-editing methods have been developed to introduce or remove mutations in human iPSCs, comprehensive strategic designs taking account of the potential side effects of CRISPR editing are needed. Here we present several novel and highly efficient strategies to introduce point mutations, insertions and deletions in human iPSCs, including step-by-step experimental protocols. These approaches involve the application of drug selection for effortless clone screening and the generation of a wild type control strain along with the mutant. We also present several examples of application of these strategies in human iPSCs and show that they are highly efficient and could be applied to other cell types.
    MeSH term(s) CRISPR-Cas Systems/genetics ; Clustered Regularly Interspaced Short Palindromic Repeats/genetics ; Gene Editing ; Humans ; Induced Pluripotent Stem Cells ; Mutagenesis
    Language English
    Publishing date 2021-01-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1066584-5
    ISSN 1095-9130 ; 1046-2023
    ISSN (online) 1095-9130
    ISSN 1046-2023
    DOI 10.1016/j.ymeth.2021.01.002
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    Zs.A 3239: Show issues Location:
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  9. Article ; Online: Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization.

    Lim, Ci Ji / Cech, Thomas R

    Nature reviews. Molecular cell biology

    2021  Volume 22, Issue 4, Page(s) 283–298

    Abstract: The regulation of telomere length in mammals is crucial for chromosome end-capping and thus for maintaining genome stability and cellular lifespan. This process requires coordination between telomeric protein complexes and the ribonucleoprotein ... ...

    Abstract The regulation of telomere length in mammals is crucial for chromosome end-capping and thus for maintaining genome stability and cellular lifespan. This process requires coordination between telomeric protein complexes and the ribonucleoprotein telomerase, which extends the telomeric DNA. Telomeric proteins modulate telomere architecture, recruit telomerase to accessible telomeres and orchestrate the conversion of the newly synthesized telomeric single-stranded DNA tail into double-stranded DNA. Dysfunctional telomere maintenance leads to telomere shortening, which causes human diseases including bone marrow failure, premature ageing and cancer. Recent studies provide new insights into telomerase-related interactions (the 'telomere replisome') and reveal new challenges for future telomere structural biology endeavours owing to the dynamic nature of telomere architecture and the great number of structures that telomeres form. In this Review, we discuss recently determined structures of the shelterin and CTC1-STN1-TEN1 (CST) complexes, how they may participate in the regulation of telomere replication and chromosome end-capping, and how disease-causing mutations in their encoding genes may affect specific functions. Major outstanding questions in the field include how all of the telomere components assemble relative to each other and how the switching between different telomere structures is achieved.
    MeSH term(s) Animals ; Chromatin/metabolism ; Chromosomes/metabolism ; DNA/metabolism ; Humans ; Telomerase/metabolism ; Telomere/metabolism ; Telomere-Binding Proteins/metabolism
    Chemical Substances Chromatin ; Telomere-Binding Proteins ; DNA (9007-49-2) ; Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2021-02-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-021-00328-y
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  10. Article ; Online: PRC2 direct transfer from G-quadruplex RNA to dsDNA has implications for RNA-binding chromatin modifiers.

    Hemphill, Wayne O / Fenske, Regan / Gooding, Anne R / Cech, Thomas R

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 23, Page(s) e2220528120

    Abstract: The chromatin-modifying enzyme, Polycomb Repressive Complex 2 (PRC2), deposits the H3K27me3 epigenetic mark to negatively regulate expression at numerous target genes, and this activity has been implicated in embryonic development, cell differentiation, ... ...

    Abstract The chromatin-modifying enzyme, Polycomb Repressive Complex 2 (PRC2), deposits the H3K27me3 epigenetic mark to negatively regulate expression at numerous target genes, and this activity has been implicated in embryonic development, cell differentiation, and various cancers. A biological role for RNA binding in regulating PRC2 histone methyltransferase activity is generally accepted, but the nature and mechanism of this relationship remains an area of active investigation. Notably, many in vitro studies demonstrate that RNA inhibits PRC2 activity on nucleosomes through mutually antagonistic binding, while some in vivo studies indicate that PRC2's RNA-binding activity is critical for facilitating its biological function(s). Here we use biochemical, biophysical, and computational approaches to interrogate PRC2's RNA and DNA-binding kinetics. Our findings demonstrate that PRC2-polynucleotide dissociation rates are dependent on the concentration of free ligand, indicating the potential for direct transfer between nucleic acid ligands without a free-enzyme intermediate. Direct transfer explains the variation in previously reported dissociation kinetics, allows reconciliation of prior in vitro and in vivo studies, and expands the potential mechanisms of RNA-mediated PRC2 regulation. Moreover, simulations indicate that such a direct transfer mechanism could be obligatory for RNA to recruit proteins to chromatin.
    MeSH term(s) Chromatin/genetics ; Polycomb Repressive Complex 2/genetics ; Polycomb Repressive Complex 2/metabolism ; RNA/genetics ; RNA/metabolism ; DNA/genetics ; DNA/metabolism ; Nucleosomes/genetics ; Protein Binding
    Chemical Substances Chromatin ; Polycomb Repressive Complex 2 (EC 2.1.1.43) ; RNA (63231-63-0) ; DNA (9007-49-2) ; Nucleosomes
    Language English
    Publishing date 2023-05-30
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2220528120
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