---
_id: '12143'
abstract:
- lang: eng
  text: MicroRNA (miRNA) and RNA interference (RNAi) pathways rely on small RNAs produced
    by Dicer endonucleases. Mammalian Dicer primarily supports the essential gene-regulating
    miRNA pathway, but how it is specifically adapted to miRNA biogenesis is unknown.
    We show that the adaptation entails a unique structural role of Dicer’s DExD/H
    helicase domain. Although mice tolerate loss of its putative ATPase function,
    the complete absence of the domain is lethal because it assures high-fidelity
    miRNA biogenesis. Structures of murine Dicer⋅miRNA precursor complexes revealed
    that the DExD/H domain has a helicase-unrelated structural function. It locks
    Dicer in a closed state, which facilitates miRNA precursor selection. Transition
    to a cleavage-competent open state is stimulated by Dicer-binding protein TARBP2.
    Absence of the DExD/H domain or its mutations unlocks the closed state, reduces
    substrate selectivity, and activates RNAi. Thus, the DExD/H domain structurally
    contributes to mammalian miRNA biogenesis and underlies mechanistical partitioning
    of miRNA and RNAi pathways.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: We thank Kristian Vlahovicek (University of Zagreb) for support of
  bioinformatics analyses and Vladimir Benes (EMBL Sequencing Facility) and Genomics
  and Bioinformatics Core Facility at the Institute of Molecular Genetics for help
  with RNA sequencing. The main funding was provided by the Czech Science Foundation
  (EXPRO grant 20-03950X to P.S. and 22-19896S to R. Stefl). Early stages of the work
  were supported by European Research Council grants under the European Union’s Horizon
  2020 Research and Innovation Programme (grants 647403 to P.S. and 649030 to R. Stefl).
  V.B., D.F.J., and F.H. were in part supported by PhD student fellowships from the
  Charles University; this work will be in part fulfilling requirements for a PhD
  degree as “school work.” Funding of D.Z. included the OP RDE project “Internal Grant
  Agency of Masaryk University” no. CZ.02.2.69/0.0/0.0/19_073/0016943. The Ministry
  of Education, Youth, and Sports of the Czech Republic (MEYS CR) provided institutional
  support for CEITEC 2020 project LQ1601. For technical support, we acknowledge EMBL
  Monterotondo’s genome engineering and transgenic core facilities, the Czech Centre
  for Phenogenomics at the Institute of Molecular Genetics (supported by RVO 68378050
  from the Czech Academy of Sciences and LM2018126 and CZ.02.1.01/0.0/0.0/18_046/0015861
  CCP Infrastructure Upgrade II from MEYS CR), the Cryo-EM and Proteomics Core Facilities
  (CEITEC, Masaryk University) supported by the CIISB research infrastructure (LM2018127
  from MEYS CR), and support from the Scientific Service Units of ISTA through resources
  from the Electron Microscopy Facility. Computational resources included e-Infrastruktura
  CZ (LM2018140) and ELIXIR-CZ (LM2018131) projects by MEYS CR and the Croatian National
  Centres of Research Excellence in Personalized Healthcare (#KK.01.1.1.01.0010) and
  Data Science and Advanced Cooperative Systems (#KK.01.1.1.01.0009) projects funded
  by the European Structural and Investment Funds grants.
article_processing_charge: No
article_type: original
author:
- first_name: David
  full_name: Zapletal, David
  last_name: Zapletal
- first_name: Eliska
  full_name: Taborska, Eliska
  last_name: Taborska
- first_name: Josef
  full_name: Pasulka, Josef
  last_name: Pasulka
- first_name: Radek
  full_name: Malik, Radek
  last_name: Malik
- first_name: Karel
  full_name: Kubicek, Karel
  last_name: Kubicek
- first_name: Martina
  full_name: Zanova, Martina
  last_name: Zanova
- first_name: Christian
  full_name: Much, Christian
  last_name: Much
- first_name: Marek
  full_name: Sebesta, Marek
  last_name: Sebesta
- first_name: Valeria
  full_name: Buccheri, Valeria
  last_name: Buccheri
- first_name: Filip
  full_name: Horvat, Filip
  last_name: Horvat
- first_name: Irena
  full_name: Jenickova, Irena
  last_name: Jenickova
- first_name: Michaela
  full_name: Prochazkova, Michaela
  last_name: Prochazkova
- first_name: Jan
  full_name: Prochazka, Jan
  last_name: Prochazka
- first_name: Matyas
  full_name: Pinkas, Matyas
  last_name: Pinkas
- first_name: Jiri
  full_name: Novacek, Jiri
  last_name: Novacek
- first_name: Diego F.
  full_name: Joseph, Diego F.
  last_name: Joseph
- first_name: Radislav
  full_name: Sedlacek, Radislav
  last_name: Sedlacek
- first_name: Carrie A
  full_name: Bernecky, Carrie A
  id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
  last_name: Bernecky
  orcid: 0000-0003-0893-7036
- first_name: Dónal
  full_name: O’Carroll, Dónal
  last_name: O’Carroll
- first_name: Richard
  full_name: Stefl, Richard
  last_name: Stefl
- first_name: Petr
  full_name: Svoboda, Petr
  last_name: Svoboda
citation:
  ama: Zapletal D, Taborska E, Pasulka J, et al. Structural and functional basis of
    mammalian microRNA biogenesis by Dicer. <i>Molecular Cell</i>. 2022;82(21):4064-4079.e13.
    doi:<a href="https://doi.org/10.1016/j.molcel.2022.10.010">10.1016/j.molcel.2022.10.010</a>
  apa: Zapletal, D., Taborska, E., Pasulka, J., Malik, R., Kubicek, K., Zanova, M.,
    … Svoboda, P. (2022). Structural and functional basis of mammalian microRNA biogenesis
    by Dicer. <i>Molecular Cell</i>. Elsevier. <a href="https://doi.org/10.1016/j.molcel.2022.10.010">https://doi.org/10.1016/j.molcel.2022.10.010</a>
  chicago: Zapletal, David, Eliska Taborska, Josef Pasulka, Radek Malik, Karel Kubicek,
    Martina Zanova, Christian Much, et al. “Structural and Functional Basis of Mammalian
    MicroRNA Biogenesis by Dicer.” <i>Molecular Cell</i>. Elsevier, 2022. <a href="https://doi.org/10.1016/j.molcel.2022.10.010">https://doi.org/10.1016/j.molcel.2022.10.010</a>.
  ieee: D. Zapletal <i>et al.</i>, “Structural and functional basis of mammalian microRNA
    biogenesis by Dicer,” <i>Molecular Cell</i>, vol. 82, no. 21. Elsevier, p. 4064–4079.e13,
    2022.
  ista: Zapletal D, Taborska E, Pasulka J, Malik R, Kubicek K, Zanova M, Much C, Sebesta
    M, Buccheri V, Horvat F, Jenickova I, Prochazkova M, Prochazka J, Pinkas M, Novacek
    J, Joseph DF, Sedlacek R, Bernecky C, O’Carroll D, Stefl R, Svoboda P. 2022. Structural
    and functional basis of mammalian microRNA biogenesis by Dicer. Molecular Cell.
    82(21), 4064–4079.e13.
  mla: Zapletal, David, et al. “Structural and Functional Basis of Mammalian MicroRNA
    Biogenesis by Dicer.” <i>Molecular Cell</i>, vol. 82, no. 21, Elsevier, 2022,
    p. 4064–4079.e13, doi:<a href="https://doi.org/10.1016/j.molcel.2022.10.010">10.1016/j.molcel.2022.10.010</a>.
  short: D. Zapletal, E. Taborska, J. Pasulka, R. Malik, K. Kubicek, M. Zanova, C.
    Much, M. Sebesta, V. Buccheri, F. Horvat, I. Jenickova, M. Prochazkova, J. Prochazka,
    M. Pinkas, J. Novacek, D.F. Joseph, R. Sedlacek, C. Bernecky, D. O’Carroll, R.
    Stefl, P. Svoboda, Molecular Cell 82 (2022) 4064–4079.e13.
date_created: 2023-01-12T12:05:36Z
date_published: 2022-11-03T00:00:00Z
date_updated: 2023-08-04T08:57:17Z
day: '03'
ddc:
- '570'
department:
- _id: CaBe
doi: 10.1016/j.molcel.2022.10.010
external_id:
  isi:
  - '000898565300011'
  pmid:
  - '36332606'
file:
- access_level: open_access
  checksum: 999e443b54e4fdaa2542ca5a97619731
  content_type: application/pdf
  creator: dernst
  date_created: 2023-01-24T09:29:02Z
  date_updated: 2023-01-24T09:29:02Z
  file_id: '12354'
  file_name: 2022_MolecularCell_Zapletal.pdf
  file_size: 7368534
  relation: main_file
  success: 1
file_date_updated: 2023-01-24T09:29:02Z
has_accepted_license: '1'
intvolume: '        82'
isi: 1
issue: '21'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
page: 4064-4079.e13
pmid: 1
publication: Molecular Cell
publication_identifier:
  issn:
  - 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural and functional basis of mammalian microRNA biogenesis by Dicer
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 82
year: '2022'
...
---
_id: '9526'
abstract:
- lang: eng
  text: DNA methylation and histone H1 mediate transcriptional silencing of genes
    and transposable elements, but how they interact is unclear. In plants and animals
    with mosaic genomic methylation, functionally mysterious methylation is also common
    within constitutively active housekeeping genes. Here, we show that H1 is enriched
    in methylated sequences, including genes, of Arabidopsis thaliana, yet this enrichment
    is independent of DNA methylation. Loss of H1 disperses heterochromatin, globally
    alters nucleosome organization, and activates H1-bound genes, but only weakly
    de-represses transposable elements. However, H1 loss strongly activates transposable
    elements hypomethylated through mutation of DNA methyltransferase MET1. Hypomethylation
    of genes also activates antisense transcription, which is modestly enhanced by
    H1 loss. Our results demonstrate that H1 and DNA methylation jointly maintain
    transcriptional homeostasis by silencing transposable elements and aberrant intragenic
    transcripts. Such functionality plausibly explains why DNA methylation, a well-known
    mutagen, has been maintained within coding sequences of crucial plant and animal
    genes.
article_processing_charge: No
article_type: original
author:
- first_name: Jaemyung
  full_name: Choi, Jaemyung
  last_name: Choi
- first_name: David B.
  full_name: Lyons, David B.
  last_name: Lyons
- first_name: M. Yvonne
  full_name: Kim, M. Yvonne
  last_name: Kim
- first_name: Jonathan D.
  full_name: Moore, Jonathan D.
  last_name: Moore
- first_name: Daniel
  full_name: Zilberman, Daniel
  id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
  last_name: Zilberman
  orcid: 0000-0002-0123-8649
citation:
  ama: Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. DNA methylation and histone
    H1 jointly repress transposable elements and aberrant intragenic transcripts.
    <i>Molecular Cell</i>. 2020;77(2):310-323.e7. doi:<a href="https://doi.org/10.1016/j.molcel.2019.10.011">10.1016/j.molcel.2019.10.011</a>
  apa: Choi, J., Lyons, D. B., Kim, M. Y., Moore, J. D., &#38; Zilberman, D. (2020).
    DNA methylation and histone H1 jointly repress transposable elements and aberrant
    intragenic transcripts. <i>Molecular Cell</i>. Elsevier. <a href="https://doi.org/10.1016/j.molcel.2019.10.011">https://doi.org/10.1016/j.molcel.2019.10.011</a>
  chicago: Choi, Jaemyung, David B. Lyons, M. Yvonne Kim, Jonathan D. Moore, and Daniel
    Zilberman. “DNA Methylation and Histone H1 Jointly Repress Transposable Elements
    and Aberrant Intragenic Transcripts.” <i>Molecular Cell</i>. Elsevier, 2020. <a
    href="https://doi.org/10.1016/j.molcel.2019.10.011">https://doi.org/10.1016/j.molcel.2019.10.011</a>.
  ieee: J. Choi, D. B. Lyons, M. Y. Kim, J. D. Moore, and D. Zilberman, “DNA methylation
    and histone H1 jointly repress transposable elements and aberrant intragenic transcripts,”
    <i>Molecular Cell</i>, vol. 77, no. 2. Elsevier, p. 310–323.e7, 2020.
  ista: Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. 2020. DNA methylation and
    histone H1 jointly repress transposable elements and aberrant intragenic transcripts.
    Molecular Cell. 77(2), 310–323.e7.
  mla: Choi, Jaemyung, et al. “DNA Methylation and Histone H1 Jointly Repress Transposable
    Elements and Aberrant Intragenic Transcripts.” <i>Molecular Cell</i>, vol. 77,
    no. 2, Elsevier, 2020, p. 310–323.e7, doi:<a href="https://doi.org/10.1016/j.molcel.2019.10.011">10.1016/j.molcel.2019.10.011</a>.
  short: J. Choi, D.B. Lyons, M.Y. Kim, J.D. Moore, D. Zilberman, Molecular Cell 77
    (2020) 310–323.e7.
date_created: 2021-06-08T06:37:09Z
date_published: 2020-01-16T00:00:00Z
date_updated: 2021-12-14T07:51:15Z
day: '16'
department:
- _id: DaZi
doi: 10.1016/j.molcel.2019.10.011
extern: '1'
external_id:
  pmid:
  - '31732458'
intvolume: '        77'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.molcel.2019.10.011
month: '01'
oa: 1
oa_version: Published Version
page: 310-323.e7
pmid: 1
publication: Molecular Cell
publication_identifier:
  eissn:
  - 1097-4164
  issn:
  - 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: DNA methylation and histone H1 jointly repress transposable elements and aberrant
  intragenic transcripts
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 77
year: '2020'
...
---
_id: '7395'
abstract:
- lang: eng
  text: The mitochondrial electron transport chain complexes are organized into supercomplexes
    (SCs) of defined stoichiometry, which have been proposed to regulate electron
    flux via substrate channeling. We demonstrate that CoQ trapping in the isolated
    SC I+III2 limits complex (C)I turnover, arguing against channeling. The SC structure,
    resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may
    be rate limiting because of unequal access of CoQ to the active sites of CIII2.
    CI shows a transition between “closed” and “open” conformations, accompanied by
    the striking rotation of a key transmembrane helix. Furthermore, the state of
    CI affects the conformational flexibility within CIII2, demonstrating crosstalk
    between the enzymes. CoQ was identified at only three of the four binding sites
    in CIII2, suggesting that interaction with CI disrupts CIII2 symmetry in a functionally
    relevant manner. Together, these observations indicate a more nuanced functional
    role for the SCs.
article_processing_charge: No
article_type: original
author:
- first_name: James A
  full_name: Letts, James A
  id: 322DA418-F248-11E8-B48F-1D18A9856A87
  last_name: Letts
  orcid: 0000-0002-9864-3586
- first_name: Karol
  full_name: Fiedorczuk, Karol
  id: 5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0
  last_name: Fiedorczuk
- first_name: Gianluca
  full_name: Degliesposti, Gianluca
  last_name: Degliesposti
- first_name: Mark
  full_name: Skehel, Mark
  last_name: Skehel
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. Structures of
    respiratory supercomplex I+III2 reveal functional and conformational crosstalk.
    <i>Molecular Cell</i>. 2019;75(6):1131-1146.e6. doi:<a href="https://doi.org/10.1016/j.molcel.2019.07.022">10.1016/j.molcel.2019.07.022</a>
  apa: Letts, J. A., Fiedorczuk, K., Degliesposti, G., Skehel, M., &#38; Sazanov,
    L. A. (2019). Structures of respiratory supercomplex I+III2 reveal functional
    and conformational crosstalk. <i>Molecular Cell</i>. Cell Press. <a href="https://doi.org/10.1016/j.molcel.2019.07.022">https://doi.org/10.1016/j.molcel.2019.07.022</a>
  chicago: Letts, James A, Karol Fiedorczuk, Gianluca Degliesposti, Mark Skehel, and
    Leonid A Sazanov. “Structures of Respiratory Supercomplex I+III2 Reveal Functional
    and Conformational Crosstalk.” <i>Molecular Cell</i>. Cell Press, 2019. <a href="https://doi.org/10.1016/j.molcel.2019.07.022">https://doi.org/10.1016/j.molcel.2019.07.022</a>.
  ieee: J. A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, and L. A. Sazanov,
    “Structures of respiratory supercomplex I+III2 reveal functional and conformational
    crosstalk,” <i>Molecular Cell</i>, vol. 75, no. 6. Cell Press, p. 1131–1146.e6,
    2019.
  ista: Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. 2019. Structures
    of respiratory supercomplex I+III2 reveal functional and conformational crosstalk.
    Molecular Cell. 75(6), 1131–1146.e6.
  mla: Letts, James A., et al. “Structures of Respiratory Supercomplex I+III2 Reveal
    Functional and Conformational Crosstalk.” <i>Molecular Cell</i>, vol. 75, no.
    6, Cell Press, 2019, p. 1131–1146.e6, doi:<a href="https://doi.org/10.1016/j.molcel.2019.07.022">10.1016/j.molcel.2019.07.022</a>.
  short: J.A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, L.A. Sazanov, Molecular
    Cell 75 (2019) 1131–1146.e6.
date_created: 2020-01-29T16:02:33Z
date_published: 2019-09-19T00:00:00Z
date_updated: 2023-09-07T14:53:06Z
day: '19'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1016/j.molcel.2019.07.022
ec_funded: 1
external_id:
  isi:
  - '000486614200006'
  pmid:
  - '31492636'
file:
- access_level: open_access
  checksum: 5202f53a237d6650ece038fbf13bdcea
  content_type: application/pdf
  creator: dernst
  date_created: 2020-02-04T10:37:28Z
  date_updated: 2020-07-14T12:47:57Z
  file_id: '7447'
  file_name: 2019_MolecularCell_Letts.pdf
  file_size: 9654895
  relation: main_file
file_date_updated: 2020-07-14T12:47:57Z
has_accepted_license: '1'
intvolume: '        75'
isi: 1
issue: '6'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: 1131-1146.e6
pmid: 1
project:
- _id: 2590DB08-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '701309'
  name: Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
publication: Molecular Cell
publication_identifier:
  issn:
  - 1097-2765
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structures of respiratory supercomplex I+III2 reveal functional and conformational
  crosstalk
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 75
year: '2019'
...
---
_id: '11127'
abstract:
- lang: eng
  text: Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited
    by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE)
    vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran
    GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for
    Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion
    can be complemented by the addition of Ran loaded with either GTP or GDP but not
    with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus,
    generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the
    extensive membrane fusion events that lead to NE formation.
article_processing_charge: No
article_type: original
author:
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
- first_name: Daniel
  full_name: Bilbao-Cortés, Daniel
  last_name: Bilbao-Cortés
- first_name: Tobias C
  full_name: Walther, Tobias C
  last_name: Walther
- first_name: Oliver J
  full_name: Gruss, Oliver J
  last_name: Gruss
- first_name: Iain W
  full_name: Mattaj, Iain W
  last_name: Mattaj
citation:
  ama: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis
    by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. 2000;5(6):1013-1024.
    doi:<a href="https://doi.org/10.1016/s1097-2765(00)80266-x">10.1016/s1097-2765(00)80266-x</a>
  apa: Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., &#38; Mattaj,
    I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly.
    <i>Molecular Cell</i>. Elsevier. <a href="https://doi.org/10.1016/s1097-2765(00)80266-x">https://doi.org/10.1016/s1097-2765(00)80266-x</a>
  chicago: Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss,
    and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.”
    <i>Molecular Cell</i>. Elsevier, 2000. <a href="https://doi.org/10.1016/s1097-2765(00)80266-x">https://doi.org/10.1016/s1097-2765(00)80266-x</a>.
  ieee: M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj,
    “GTP hydrolysis by Ran is required for nuclear envelope assembly,” <i>Molecular
    Cell</i>, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.
  ista: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis
    by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.
  mla: Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope
    Assembly.” <i>Molecular Cell</i>, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24,
    doi:<a href="https://doi.org/10.1016/s1097-2765(00)80266-x">10.1016/s1097-2765(00)80266-x</a>.
  short: M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular
    Cell 5 (2000) 1013–1024.
date_created: 2022-04-07T07:57:59Z
date_published: 2000-06-01T00:00:00Z
date_updated: 2022-07-18T08:58:31Z
day: '01'
doi: 10.1016/s1097-2765(00)80266-x
extern: '1'
external_id:
  pmid:
  - '10911995'
intvolume: '         5'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/S1097-2765(00)80266-X
month: '06'
oa: 1
oa_version: Published Version
page: 1013-1024
pmid: 1
publication: Molecular Cell
publication_identifier:
  issn:
  - 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: GTP hydrolysis by Ran is required for nuclear envelope assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 5
year: '2000'
...