Nature Search

Translocation of an RNA duplex on a ribozyme

Scott A. Strobel
Thomas R. Cech
Research01 Jan 1994
Nature Structural Biology

Volume: 1, P: 13-17
DNA cleavage catalysed by the ribozyme from Tetrahymena

Daniel Herschlag
Thomas R. Cech
Research29 Mar 1990
Nature

Volume: 344, P: 405-409
Mechanism of recognition of the 5′ splice site in self-splicing group I introns

Gian Garriga
Alan M. Lambowitz
Thomas R. Cech
Research03 Jul 1986
Nature

Volume: 322, P: 86-89
Metal ion catalysis in the Tetrahymena ribozyme reaction

Joseph A. Piccirilli
Joseph S. Vyle
Thomas R. Cech
Research07 Jan 1993
Nature

Volume: 361, P: 85-88
Representation of the secondary and tertiary structure of group I introns

Thomas R. Cech
Simon H. Damberger
Robin R. Gutell
Research01 May 1994
Nature Structural Biology

Volume: 1, P: 273-280
RNA substrate binding site in the catalytic core of the Tetrahymena ribozyme

Anna Marie Pyle
Felicia L. Murphy
Thomas R. Cech
Research09 Jul 1992
Nature

Volume: 358, P: 123-128
The Tetrahymena ribozyme acts like an RNA restriction endonuclease

Arthur J. Zaug
Michael D. Been
Thomas R. Cech
Research04 Dec 1986
Nature

Volume: 324, P: 429-433
Solution structure of the cyclosporin A/cyclophilin complex by NMR

Yves Thériault
Timothy M. Logan
Stephen W. Fesik
Research07 Jan 1993
Nature

Volume: 361, P: 88-91
Group I Introns: New Molecular Mechanisms for mRNA Repair

Using ribozymes to repair transcripts may yield new therapeutic approaches to genetic disease

Thomas Cech
Research01 Apr 1995
Bio/Technology

Volume: 13, P: 323-326
Ribozyme recognition of RNA by tertiary interactions with specific ribose 2′-OH groups

Anna Marie Pyle
Thomas R. Cech
Research18 Apr 1991
Nature

Volume: 350, P: 628-631
Ribozyme-mediated repair of defective mRNA by targeted trans-splicing

Bruce A. Sullenger
Thomas R. Cech
Research13 Oct 1994
Nature

Volume: 371, P: 619-622
Autocatalytic cyclization of an excised intervening sequence RNA is a cleavage–ligation reaction

Arthur J. Zaug
Paula J. Grabowski
Thomas R. Cech
Research17 Feb 1983
Nature

Volume: 301, P: 578-583
Specific interaction between the self-splicing RNA of Tetrahymena and its guanosine substrate: implications for biological catalysis by RNA

Brenda L. Bass
Thomas R. Cech
Research26 Apr 1984
Nature

Volume: 308, P: 820-826
Ribozyme self-replication?

Thomas R. Cech
News & Views15 Jun 1989
Nature

Volume: 339, P: 507-508
erratum: Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle

Anita G. Seto
Arthur J. Zaug
Thomas R. Cech
Research23 Dec 1999
Nature

Volume: 402, P: 898
Regulation of telomere length and function by a Myb-___domain protein in fission yeast

Julia Promisel Cooper
Elaine R. Nimmo
Thomas R. Cech
Research20 Feb 1997
Nature

Volume: 385, P: 744-747
Fishing for fresh catalysts

Thomas R. Cech
News & Views16 Sept 1993
Nature

Volume: 365, P: 204-205
Inhibition of telomerase by G-quartet DMA structures

Alan M. Zahler
James R. Williamson
David M. Prescott
Research25 Apr 1991
Nature

Volume: 350, P: 718-720
G-strings at chromosome ends

Thomas R. Cech
News & Views28 Apr 1988
Nature

Volume: 332, P: 777-778
Hammerhead nailed down

Thomas R. Cech
Olke C. Uhlenbeck
News & Views03 Nov 1994
Nature

Volume: 372, P: 39-40
Leveraging family-specific signatures for AMP discovery and high-throughput annotation

Faiza Hanif Waghu
Ram Shankar Barai
Susan Idicula-Thomas
ResearchOpen Access19 Apr 2016
Scientific Reports

Volume: 6, P: 1-7
Erratum: DNA cleavage catalysed by the ribozyme from Tetrahymena

Daniel Herschlag
Thomas R. Cech
Amendments and Corrections19 Apr 1990
Nature

Volume: 344, P: 792
Erratum: The Tetrahymena ribozyme acts like an RNA restriction endonuclease

Arthur J. Zaug
Michael D. Been
Thomas R. Cech
Amendments and Corrections18 Feb 1987
Nature

Volume: 325, P: 646
Phosphorylation of two small GTP-binding proteins of the Rab family by p34^cdc2

Eric Bailly
Mary McCaffrey
Michel Bornens
Research25 Apr 1991
Nature

Volume: 350, P: 715-718
The POT1–TPP1 telomere complex is a telomerase processivity factor

The structure of TPP1's oligonucleotide binding fold contains features that are particularly characteristic of TEBPβ. When the POT1–TPP1 complex is bound to telomeric DNA, it does not inhibit telomerase activity, as other telomere binding proteins do. Instead, the presence of POT1–TPP1 unexpectedly stimulates telomerase activity and processivity.

Feng Wang
Elaine R. Podell
Ming Lei
Research21 Jan 2007
Nature

Volume: 445, P: 506-510
Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against C-raf kinase

Brett P. Monia
Joseph F. Johnston
Doriano Fabbro
Research01 Jun 1996
Nature Medicine

Volume: 2, P: 668-675
Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq

Telomerase assembles on a multi-___domain RNA scaffold that must adopt a specific structure to function. Here, the authors reveal an alternative RNA conformation in living cells that disrupts telomerase activity, suggesting RNA misfolding may challenge proper telomerase assembly.

Nicholas M. Forino
Jia Zheng Woo
Michael D. Stone
ResearchOpen Access22 Jan 2025
Nature Communications

Volume: 16, P: 1-15
The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity

Using separation-of-function mutations of TPP1 that inhibit telomerase binding while maintaining telomere capping, a region on the surface of TPP1, the TEL patch, is identified and found to be required for both binding telomerase and enhancing its processivity.

Jayakrishnan Nandakumar
Caitlin F. Bell
Thomas R. Cech
Research24 Oct 2012
Nature

Volume: 492, P: 285-289
Telomeric localization of TRF2, a novel human telobox protein

Thomas Bilaud
Christine Brun
Eric Gilson
Research01 Oct 1997
Nature Genetics

Volume: 17, P: 236-239
Academia and industry: Companies on campus

Housing industry labs in academic settings benefits all parties, say Jana J. Watson-Capps and Thomas R. Cech.

Jana J. Watson-Capps
Thomas R. Cech
Comments & Opinion15 Oct 2014
Nature

Volume: 514, P: 297-298
Evolution of Tetrahymena ribozyme mutants with increased structural stability

Feng Guo
Thomas R. Cech
Research30 Sept 2002
Nature Structural Biology

Volume: 9, P: 855-861
Reconstitution of a telomeric replicon organized by CST

The Polα–primase-associated CST complex organizes telomeric C-strand DNA synthesis, and, in combination with telomerase, it carries out complete replication of the single-stranded DNA overhang found at human telomeres.

Arthur J. Zaug
Karen J. Goodrich
Thomas R. Cech
ResearchOpen Access13 Jul 2022
Nature

Volume: 608, P: 819-825
Publisher Correction: Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization

Ci Ji Lim
Thomas R. Cech
Amendments and Corrections19 Feb 2021
Nature Reviews Molecular Cell Biology

Volume: 22, P: 299
RNA is essential for PRC2 chromatin occupancy and function in human pluripotent stem cells

Perturbation of RNA–PRC2 interaction in human pluripotent stem cells disrupts PRC2 chromatin occupancy and localization genome wide. PRC2–RNA interactions contribute to cardiomyocyte differentiation.

Yicheng Long
Taeyoung Hwang
Thomas R. Cech
Research06 Jul 2020
Nature Genetics

Volume: 52, P: 931-938
Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection

Ming Lei
Elaine R Podell
Thomas R Cech
Research21 Nov 2004
Nature Structural & Molecular Biology

Volume: 11, P: 1223-1229
Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity

The human shelterin complex protects telomere ends from being recognized as damaged DNA sites and regulates telomere length in conjunction with telomerase. Here the authors establish the stoichiometries of human shelterin complexes of various compositions and show shelterin provides dual pathways to stimulate telomerase processivity.

Ci Ji Lim
Arthur J. Zaug
Thomas R. Cech
ResearchOpen Access20 Oct 2017
Nature Communications

Volume: 8, P: 1-14
Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA

Biochemical reconstitution of PRC2 interactions with chromatinized templates demonstrates that protein-free linker DNA dominates the PRC2-nucleosome interaction, while RNA inhibits binding.

Xueyin Wang
Richard D Paucek
Thomas R Cech
Research23 Oct 2017
Nature Structural & Molecular Biology

Volume: 24, P: 1028-1038
The role of APOBEC3B in lung tumor evolution and targeted cancer therapy resistance

Analyses of in vivo models, cell lines and patient-derived samples show that apolipoprotein B mRNA-editing catalytic subunit 3B (APOBEC3B) not only restrains lung tumor initiation but also that its upregulation is associated with resistance to targeted therapies. This study highlights the complex and context-dependent role of APOBEC3B in lung cancer.

Deborah R. Caswell
Philippe Gui
Charles Swanton
ResearchOpen Access04 Dec 2023
Nature Genetics

Volume: 56, P: 60-73
A second catalytic metal ion in a group I ribozyme

Lara B. Weinstein
B. C. N. M. Jones
Thomas R. Cech
Research21 Aug 1997
Nature

Volume: 388, P: 805-808
Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle

Anita G. Seto
Arthur J. Zaug
Thomas R. Cech
Research09 Sept 1999
Nature

Volume: 401, P: 177-180
Correction: Corrigendum: A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro

David C Zappulla
Karen Goodrich
Thomas R Cech
Amendments and Corrections01 May 2006
Nature Structural & Molecular Biology

Volume: 13, P: 465
Addendum: Crystal structure of the essential N-terminal ___domain of telomerase reverse transcriptase

Steven A Jacobs
Elaine R Podell
Thomas R Cech
Amendments and Corrections01 Oct 2007
Nature Structural & Molecular Biology

Volume: 14, P: 984
A natural ribozyme with 3′,5′ RNA ligase activity

Quentin Vicens
Thomas R Cech
Research04 Jan 2009
Nature Chemical Biology

Volume: 5, P: 97-99
Promiscuous RNA binding by Polycomb repressive complex 2

Polycomb repressive complex 2 (PRC2) is a histone methyltransferase required for epigenetic silencing during development and cancer, and it can be recruited to chromatin by long noncoding RNAs. In vitro binding studies and comparative analysis of genome-wide in vivo data now suggest a model for the maintenance of the repressed chromatin state by PRC2, directed by PRC2's promiscuous binding to nascent RNA transcripts.

Chen Davidovich
Leon Zheng
Thomas R Cech
Research29 Sept 2013
Nature Structural & Molecular Biology

Volume: 20, P: 1250-1257
Publisher Correction: Nuclear compartmentalization of TERT mRNA and TUG1 lncRNA is driven by intron retention

Gabrijela Dumbović
Ulrich Braunschweig
John L. Rinn
Amendments and CorrectionsOpen Access21 Oct 2021
Nature Communications

Volume: 12, P: 1
Inhibition of telomerase RNA decay rescues telomerase deficiency caused by dyskerin or PARN defects

New evidence that human telomerase RNA (hTR) degradation by EXOSC10 or DCP2 and XRN1 reduces telomerase activity when dyskerin is compromised suggests that RNA decay pathways may provide future therapeutic targets for telomere biology disorders.

Siddharth Shukla
Jens C Schmidt
Roy Parker
Research07 Mar 2016
Nature Structural & Molecular Biology

Volume: 23, P: 286-292
DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA

Ming Lei
Elaine R. Podell
Thomas R. Cech
Research13 Nov 2003
Nature

Volume: 426, P: 198-203
The RNA accordion model for template positioning by telomerase RNA during telomeric DNA synthesis

Telomerase uses its associated RNA as a template for processive addition of telomeric DNA repeats. Biochemistry and smFRET analysis are now used to investigate how the RNA template moves along the active site, revealing an accordion mechanism whereby the regions flanking the template alternate between extended and compacted forms.

Andrea J Berman
Benjamin M Akiyama
Thomas R Cech
Research20 Nov 2011
Nature Structural & Molecular Biology

Volume: 18, P: 1371-1375
Crystal structure of the essential N-terminal ___domain of telomerase reverse transcriptase

Steven A Jacobs
Elaine R Podell
Thomas R Cech
Research05 Feb 2006
Nature Structural & Molecular Biology

Volume: 13, P: 218-225
Nuclear compartmentalization of TERT mRNA and TUG1 lncRNA is driven by intron retention

RNA localization plays an important role in transcriptome regulation. The majority of TERT transcripts are detected in the nucleus and TUG1 lncRNAs in both the nucleus and cytoplasm. Here, the authors combine single-cell RNA imaging, antisense oligonucleotides and splicing analyses to show that retention of specific introns drives stable compartmentalization of TERT and TUG1 transcripts in the nucleus, and that splicing of TERT retained introns is mitotically regulated.

Gabrijela Dumbović
Ulrich Braunschweig
John L. Rinn
ResearchOpen Access03 Jun 2021
Nature Communications

Volume: 12, P: 1-19

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