---
_id: '12275'
abstract:
- lang: eng
  text: N-glycans are molecularly diverse sugars borne by over 70% of proteins transiting
    the secretory pathway and have been implicated in protein folding, stability,
    and localization. Mutations in genes important for N-glycosylation result in congenital
    disorders of glycosylation that are often associated with intellectual disability.
    Here, we show that structurally distinct N-glycans regulate an extracellular protein
    complex involved in the patterning of somatosensory dendrites in Caenorhabditis
    elegans. Specifically, aman-2/Golgi alpha-mannosidase II, a conserved key enzyme
    in the biosynthesis of specific N-glycans, regulates the activity of the Menorin
    adhesion complex without obviously affecting the protein stability and localization
    of its components. AMAN-2 functions cell-autonomously to allow for decoration
    of the neuronal transmembrane receptor DMA-1/LRR-TM with the correct set of high-mannose/hybrid/paucimannose
    N-glycans. Moreover, distinct types of N-glycans on specific N-glycosylation sites
    regulate DMA-1/LRR-TM receptor function, which, together with three other extracellular
    proteins, forms the Menorin adhesion complex. In summary, specific N-glycan structures
    regulate dendrite patterning by coordinating the activity of an extracellular
    adhesion complex, suggesting that the molecular diversity of N-glycans can contribute
    to developmental specificity in the nervous system.
acknowledgement: 'We thank Scott Garforth, Sarah Garrett, Peri Kurshan, Yehuda Salzberg,
  PamelaStanley, Robert Townley, and members of the B€ulow laboratory for commentson
  the manuscript or helpful discussions during the course of this work. Wethank David
  Miller, Shohei Mitani, Kang Shen, and Iain Wilson for reagents,and Yuji Kohara for
  theyk11g705cDNA clone. We are grateful to MeeraTrivedi for sharing thedzIs117strain
  prior to publication. Some strains wereprovided by the Caenorhabditis Genome Center
  (funded by the NIH Office ofResearch Infrastructure Programs P40OD010440). This
  work was supportedby grants from the National Institute of Health (NIH): R01NS096672andR21NS111145to
  HEB; F31NS100370to MR; T32GM007288and F31HD066967to CADB; P30HD071593to Albert Einstein
  College of Medicine. We acknowl-edge support to MR by the Department of Neuroscience.
  NJRS was the recipi-ent of a Colciencias-Fulbright Fellowship and HEB of an Irma
  T. Hirschl/Monique Weill-Caulier research fellowship'
article_number: e54163
article_processing_charge: No
article_type: original
author:
- first_name: Maisha
  full_name: Rahman, Maisha
  last_name: Rahman
- first_name: Nelson
  full_name: Ramirez, Nelson
  id: 39831956-E4FE-11E9-85DE-0DC7E5697425
  last_name: Ramirez
- first_name: Carlos A
  full_name: Diaz‐Balzac, Carlos A
  last_name: Diaz‐Balzac
- first_name: Hannes E
  full_name: Bülow, Hannes E
  last_name: Bülow
citation:
  ama: Rahman M, Ramirez N, Diaz‐Balzac CA, Bülow HE. Specific N-glycans regulate
    an extracellular adhesion complex during somatosensory dendrite patterning. <i>EMBO
    Reports</i>. 2022;23(7). doi:<a href="https://doi.org/10.15252/embr.202154163">10.15252/embr.202154163</a>
  apa: Rahman, M., Ramirez, N., Diaz‐Balzac, C. A., &#38; Bülow, H. E. (2022). Specific
    N-glycans regulate an extracellular adhesion complex during somatosensory dendrite
    patterning. <i>EMBO Reports</i>. Embo Press. <a href="https://doi.org/10.15252/embr.202154163">https://doi.org/10.15252/embr.202154163</a>
  chicago: Rahman, Maisha, Nelson Ramirez, Carlos A Diaz‐Balzac, and Hannes E Bülow.
    “Specific N-Glycans Regulate an Extracellular Adhesion Complex during Somatosensory
    Dendrite Patterning.” <i>EMBO Reports</i>. Embo Press, 2022. <a href="https://doi.org/10.15252/embr.202154163">https://doi.org/10.15252/embr.202154163</a>.
  ieee: M. Rahman, N. Ramirez, C. A. Diaz‐Balzac, and H. E. Bülow, “Specific N-glycans
    regulate an extracellular adhesion complex during somatosensory dendrite patterning,”
    <i>EMBO Reports</i>, vol. 23, no. 7. Embo Press, 2022.
  ista: Rahman M, Ramirez N, Diaz‐Balzac CA, Bülow HE. 2022. Specific N-glycans regulate
    an extracellular adhesion complex during somatosensory dendrite patterning. EMBO
    Reports. 23(7), e54163.
  mla: Rahman, Maisha, et al. “Specific N-Glycans Regulate an Extracellular Adhesion
    Complex during Somatosensory Dendrite Patterning.” <i>EMBO Reports</i>, vol. 23,
    no. 7, e54163, Embo Press, 2022, doi:<a href="https://doi.org/10.15252/embr.202154163">10.15252/embr.202154163</a>.
  short: M. Rahman, N. Ramirez, C.A. Diaz‐Balzac, H.E. Bülow, EMBO Reports 23 (2022).
date_created: 2023-01-16T10:01:44Z
date_published: 2022-07-05T00:00:00Z
date_updated: 2023-10-03T11:25:54Z
day: '05'
department:
- _id: MaDe
doi: 10.15252/embr.202154163
external_id:
  isi:
  - '000797302700001'
  pmid:
  - '35586945'
has_accepted_license: '1'
intvolume: '        23'
isi: 1
issue: '7'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.15252/embr.202154163
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: EMBO Reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: Embo Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Specific N-glycans regulate an extracellular adhesion complex during somatosensory
  dendrite patterning
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2022'
...
---
_id: '10283'
abstract:
- lang: eng
  text: 'During the past decade, the scientific community and outside observers have
    noted a concerning lack of rigor and transparency in preclinical research that
    led to talk of a “reproducibility crisis” in the life sciences (Baker, 2016; Bespalov
    & Steckler, 2018; Heddleston et al, 2021). Various measures have been proposed
    to address the problem: from better training of scientists to more oversight to
    expanded publishing practices such as preregistration of studies. The recently
    published EQIPD (Enhancing Quality in Preclinical Data) System is, to date, the
    largest initiative that aims to establish a systematic approach for increasing
    the robustness and reliability of biomedical research (Bespalov et al, 2021).
    However, promoting a cultural change in research practices warrants a broad adoption
    of the Quality System and its underlying philosophy. It is here that academic
    Core Facilities (CF), research service providers at universities and research
    institutions, can make a difference. It is fair to assume that a significant fraction
    of published data originated from experiments that were designed, run, or analyzed
    in CFs. These academic services play an important role in the research ecosystem
    by offering access to cutting-edge equipment and by developing and testing novel
    techniques and methods that impact research in the academic and private sectors
    alike (Bikovski et al, 2020). Equipment and infrastructure are not the only value:
    CFs employ competent personnel with profound knowledge and practical experience
    of the specific field of interest: animal behavior, imaging, crystallography,
    genomics, and so on. Thus, CFs are optimally positioned to address concerns about
    the quality and robustness of preclinical research.'
acknowledgement: This EQIPD project has received funding from the Innovative Medicines
  Initiative 2 Joint Undertaking under grant agreement no. 777364. This Joint Undertaking
  receives support from the European Union’s Horizon 2020 research and innovation
  program and EFPIA. LR was supported by the Faculty of Biology and Medicine, University
  of Lausanne. VV was supported by Biocenter Finland and the Jane and Aatos Erkko
  Foundation. CP and IKB received funding from the Federal Ministry of Education and
  Research (BMBF, grant 01PW18001). SB from the Vienna BioCenter Core Facilities (VBCF)
  Preclinical Phenotyping Facility acknowledges funding from the Austrian Federal
  Ministry of Education, Science & Research; and the City of Vienna. MT is an incumbent
  of the Carolito Stiftung Research Fellow Chair in Neurodegenerative Diseases. We
  thank Dr. Katja Kivinen (Helsinki Institute of Life Science) for discussions and
  feedback.
article_number: e53824
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Leonardo
  full_name: Restivo, Leonardo
  last_name: Restivo
- first_name: Björn
  full_name: Gerlach, Björn
  last_name: Gerlach
- first_name: Michael
  full_name: Tsoory, Michael
  last_name: Tsoory
- first_name: Lior
  full_name: Bikovski, Lior
  last_name: Bikovski
- first_name: Sylvia
  full_name: Badurek, Sylvia
  last_name: Badurek
- first_name: Claudia
  full_name: Pitzer, Claudia
  last_name: Pitzer
- first_name: Isabelle C.
  full_name: Kos-Braun, Isabelle C.
  last_name: Kos-Braun
- first_name: Anne Laure Mj
  full_name: Mausset-Bonnefont, Anne Laure Mj
  last_name: Mausset-Bonnefont
- first_name: Jonathan
  full_name: Ward, Jonathan
  last_name: Ward
- first_name: Michael
  full_name: Schunn, Michael
  id: 4272DB4A-F248-11E8-B48F-1D18A9856A87
  last_name: Schunn
  orcid: 0000-0003-4326-5300
- first_name: Lucas P.J.J.
  full_name: Noldus, Lucas P.J.J.
  last_name: Noldus
- first_name: Anton
  full_name: Bespalov, Anton
  last_name: Bespalov
- first_name: Vootele
  full_name: Voikar, Vootele
  last_name: Voikar
citation:
  ama: 'Restivo L, Gerlach B, Tsoory M, et al. Towards best practices in research:
    Role of academic core facilities. <i>EMBO Reports</i>. 2021;22. doi:<a href="https://doi.org/10.15252/embr.202153824">10.15252/embr.202153824</a>'
  apa: 'Restivo, L., Gerlach, B., Tsoory, M., Bikovski, L., Badurek, S., Pitzer, C.,
    … Voikar, V. (2021). Towards best practices in research: Role of academic core
    facilities. <i>EMBO Reports</i>. EMBO Press. <a href="https://doi.org/10.15252/embr.202153824">https://doi.org/10.15252/embr.202153824</a>'
  chicago: 'Restivo, Leonardo, Björn Gerlach, Michael Tsoory, Lior Bikovski, Sylvia
    Badurek, Claudia Pitzer, Isabelle C. Kos-Braun, et al. “Towards Best Practices
    in Research: Role of Academic Core Facilities.” <i>EMBO Reports</i>. EMBO Press,
    2021. <a href="https://doi.org/10.15252/embr.202153824">https://doi.org/10.15252/embr.202153824</a>.'
  ieee: 'L. Restivo <i>et al.</i>, “Towards best practices in research: Role of academic
    core facilities,” <i>EMBO Reports</i>, vol. 22. EMBO Press, 2021.'
  ista: 'Restivo L, Gerlach B, Tsoory M, Bikovski L, Badurek S, Pitzer C, Kos-Braun
    IC, Mausset-Bonnefont ALM, Ward J, Schunn M, Noldus LPJJ, Bespalov A, Voikar V.
    2021. Towards best practices in research: Role of academic core facilities. EMBO
    Reports. 22, e53824.'
  mla: 'Restivo, Leonardo, et al. “Towards Best Practices in Research: Role of Academic
    Core Facilities.” <i>EMBO Reports</i>, vol. 22, e53824, EMBO Press, 2021, doi:<a
    href="https://doi.org/10.15252/embr.202153824">10.15252/embr.202153824</a>.'
  short: L. Restivo, B. Gerlach, M. Tsoory, L. Bikovski, S. Badurek, C. Pitzer, I.C.
    Kos-Braun, A.L.M. Mausset-Bonnefont, J. Ward, M. Schunn, L.P.J.J. Noldus, A. Bespalov,
    V. Voikar, EMBO Reports 22 (2021).
date_created: 2021-11-14T23:01:24Z
date_published: 2021-11-04T00:00:00Z
date_updated: 2023-08-14T11:47:35Z
day: '04'
ddc:
- '570'
department:
- _id: PreCl
doi: 10.15252/embr.202153824
external_id:
  isi:
  - '000714350000001'
file:
- access_level: open_access
  checksum: 74743baa6ef431ef60c3de3bc4da045a
  content_type: application/pdf
  creator: dernst
  date_created: 2022-05-16T07:07:41Z
  date_updated: 2022-05-16T07:07:41Z
  file_id: '11381'
  file_name: 2021_EmboReports_Restivo.pdf
  file_size: 488583
  relation: main_file
  success: 1
file_date_updated: 2022-05-16T07:07:41Z
has_accepted_license: '1'
intvolume: '        22'
isi: 1
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
publication: EMBO Reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: EMBO Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Towards best practices in research: Role of academic core facilities'
tmp:
  image: /images/cc_by_nc_nd.png
  legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
    (CC BY-NC-ND 4.0)
  short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 22
year: '2021'
...
---
_id: '9913'
abstract:
- lang: eng
  text: Nitrate commands genome-wide gene expression changes that impact metabolism,
    physiology, plant growth, and development. In an effort to identify new components
    involved in nitrate responses in plants, we analyze the Arabidopsis thaliana root
    phosphoproteome in response to nitrate treatments via liquid chromatography coupled
    to tandem mass spectrometry. 176 phosphoproteins show significant changes at 5
    or 20 min after nitrate treatments. Proteins identified by 5 min include signaling
    components such as kinases or transcription factors. In contrast, by 20 min, proteins
    identified were associated with transporter activity or hormone metabolism functions,
    among others. The phosphorylation profile of NITRATE TRANSPORTER 1.1 (NRT1.1)
    mutant plants was significantly altered as compared to wild-type plants, confirming
    its key role in nitrate signaling pathways that involves phosphorylation changes.
    Integrative bioinformatics analysis highlights auxin transport as an important
    mechanism modulated by nitrate signaling at the post-translational level. We validated
    a new phosphorylation site in PIN2 and provide evidence that it functions in primary
    and lateral root growth responses to nitrate.
acknowledgement: This work was supported by ANID—Millennium Science Initiative Program—ICN17_022,
  Fondo de Desarrollo de Areas Prioritarias (FONDAP) Center for Genome Regulation
  (15090007), ANID—Fondo Nacional de Desarrollo Científico y Tecnológico (FONDECYT)
  1180759 (to RAG) and 1171631 (to AV). We would like to thank Unidad de Microscopía
  Avanzada UC (UMA UC).
article_number: e51813
article_processing_charge: Yes
article_type: original
author:
- first_name: Andrea
  full_name: Vega, Andrea
  last_name: Vega
- first_name: Isabel
  full_name: Fredes, Isabel
  last_name: Fredes
- first_name: José
  full_name: O’Brien, José
  last_name: O’Brien
- first_name: Zhouxin
  full_name: Shen, Zhouxin
  last_name: Shen
- first_name: Krisztina
  full_name: Ötvös, Krisztina
  id: 29B901B0-F248-11E8-B48F-1D18A9856A87
  last_name: Ötvös
  orcid: 0000-0002-5503-4983
- first_name: Rashed
  full_name: Abualia, Rashed
  id: 4827E134-F248-11E8-B48F-1D18A9856A87
  last_name: Abualia
  orcid: 0000-0002-9357-9415
- first_name: Eva
  full_name: Benková, Eva
  id: 38F4F166-F248-11E8-B48F-1D18A9856A87
  last_name: Benková
  orcid: 0000-0002-8510-9739
- first_name: Steven P.
  full_name: Briggs, Steven P.
  last_name: Briggs
- first_name: Rodrigo A.
  full_name: Gutiérrez, Rodrigo A.
  last_name: Gutiérrez
citation:
  ama: Vega A, Fredes I, O’Brien J, et al. Nitrate triggered phosphoproteome changes
    and a PIN2 phosphosite modulating root system architecture. <i>EMBO Reports</i>.
    2021;22(9). doi:<a href="https://doi.org/10.15252/embr.202051813">10.15252/embr.202051813</a>
  apa: Vega, A., Fredes, I., O’Brien, J., Shen, Z., Ötvös, K., Abualia, R., … Gutiérrez,
    R. A. (2021). Nitrate triggered phosphoproteome changes and a PIN2 phosphosite
    modulating root system architecture. <i>EMBO Reports</i>. Wiley. <a href="https://doi.org/10.15252/embr.202051813">https://doi.org/10.15252/embr.202051813</a>
  chicago: Vega, Andrea, Isabel Fredes, José O’Brien, Zhouxin Shen, Krisztina Ötvös,
    Rashed Abualia, Eva Benková, Steven P. Briggs, and Rodrigo A. Gutiérrez. “Nitrate
    Triggered Phosphoproteome Changes and a PIN2 Phosphosite Modulating Root System
    Architecture.” <i>EMBO Reports</i>. Wiley, 2021. <a href="https://doi.org/10.15252/embr.202051813">https://doi.org/10.15252/embr.202051813</a>.
  ieee: A. Vega <i>et al.</i>, “Nitrate triggered phosphoproteome changes and a PIN2
    phosphosite modulating root system architecture,” <i>EMBO Reports</i>, vol. 22,
    no. 9. Wiley, 2021.
  ista: Vega A, Fredes I, O’Brien J, Shen Z, Ötvös K, Abualia R, Benková E, Briggs
    SP, Gutiérrez RA. 2021. Nitrate triggered phosphoproteome changes and a PIN2 phosphosite
    modulating root system architecture. EMBO Reports. 22(9), e51813.
  mla: Vega, Andrea, et al. “Nitrate Triggered Phosphoproteome Changes and a PIN2
    Phosphosite Modulating Root System Architecture.” <i>EMBO Reports</i>, vol. 22,
    no. 9, e51813, Wiley, 2021, doi:<a href="https://doi.org/10.15252/embr.202051813">10.15252/embr.202051813</a>.
  short: A. Vega, I. Fredes, J. O’Brien, Z. Shen, K. Ötvös, R. Abualia, E. Benková,
    S.P. Briggs, R.A. Gutiérrez, EMBO Reports 22 (2021).
date_created: 2021-08-15T22:01:30Z
date_published: 2021-09-06T00:00:00Z
date_updated: 2024-03-25T23:30:22Z
day: '06'
ddc:
- '580'
department:
- _id: EvBe
- _id: GradSch
doi: 10.15252/embr.202051813
external_id:
  isi:
  - '000681754200001'
  pmid:
  - '34357701 '
file:
- access_level: open_access
  checksum: 750de03dc3b715c37090126c1548ba13
  content_type: application/pdf
  creator: cchlebak
  date_created: 2021-10-05T13:36:42Z
  date_updated: 2021-10-05T13:36:42Z
  file_id: '10090'
  file_name: 2021_EmboR_Vega.pdf
  file_size: 3144854
  relation: main_file
  success: 1
file_date_updated: 2021-10-05T13:36:42Z
has_accepted_license: '1'
intvolume: '        22'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
publication: EMBO Reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: Wiley
quality_controlled: '1'
related_material:
  record:
  - id: '10303'
    relation: dissertation_contains
    status: public
scopus_import: '1'
status: public
title: Nitrate triggered phosphoproteome changes and a PIN2 phosphosite modulating
  root system architecture
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: 22
year: '2021'
...
---
_id: '6499'
abstract:
- lang: eng
  text: Expansion microscopy is a recently introduced imaging technique that achieves
    super‐resolution through physically expanding the specimen by ~4×, after embedding
    into a swellable gel. The resolution attained is, correspondingly, approximately
    fourfold better than the diffraction limit, or ~70 nm. This is a major improvement
    over conventional microscopy, but still lags behind modern STED or STORM setups,
    whose resolution can reach 20–30 nm. We addressed this issue here by introducing
    an improved gel recipe that enables an expansion factor of ~10× in each dimension,
    which corresponds to an expansion of the sample volume by more than 1,000‐fold.
    Our protocol, which we termed X10 microscopy, achieves a resolution of 25–30 nm
    on conventional epifluorescence microscopes. X10 provides multi‐color images similar
    or even superior to those produced with more challenging methods, such as STED,
    STORM, and iterative expansion microscopy (iExM). X10 is therefore the cheapest
    and easiest option for high‐quality super‐resolution imaging currently available.
    X10 should be usable in any laboratory, irrespective of the machinery owned or
    of the technical knowledge.
article_number: e45836
article_processing_charge: No
author:
- first_name: Sven M
  full_name: Truckenbrodt, Sven M
  id: 45812BD4-F248-11E8-B48F-1D18A9856A87
  last_name: Truckenbrodt
- first_name: Manuel
  full_name: Maidorn, Manuel
  last_name: Maidorn
- first_name: Dagmar
  full_name: Crzan, Dagmar
  last_name: Crzan
- first_name: Hanna
  full_name: Wildhagen, Hanna
  last_name: Wildhagen
- first_name: Selda
  full_name: Kabatas, Selda
  last_name: Kabatas
- first_name: Silvio O
  full_name: Rizzoli, Silvio O
  last_name: Rizzoli
citation:
  ama: Truckenbrodt SM, Maidorn M, Crzan D, Wildhagen H, Kabatas S, Rizzoli SO. X10
    expansion microscopy enables 25‐nm resolution on conventional microscopes. <i>EMBO
    reports</i>. 2018;19(9). doi:<a href="https://doi.org/10.15252/embr.201845836">10.15252/embr.201845836</a>
  apa: Truckenbrodt, S. M., Maidorn, M., Crzan, D., Wildhagen, H., Kabatas, S., &#38;
    Rizzoli, S. O. (2018). X10 expansion microscopy enables 25‐nm resolution on conventional
    microscopes. <i>EMBO Reports</i>. EMBO. <a href="https://doi.org/10.15252/embr.201845836">https://doi.org/10.15252/embr.201845836</a>
  chicago: Truckenbrodt, Sven M, Manuel Maidorn, Dagmar Crzan, Hanna Wildhagen, Selda
    Kabatas, and Silvio O Rizzoli. “X10 Expansion Microscopy Enables 25‐nm Resolution
    on Conventional Microscopes.” <i>EMBO Reports</i>. EMBO, 2018. <a href="https://doi.org/10.15252/embr.201845836">https://doi.org/10.15252/embr.201845836</a>.
  ieee: S. M. Truckenbrodt, M. Maidorn, D. Crzan, H. Wildhagen, S. Kabatas, and S.
    O. Rizzoli, “X10 expansion microscopy enables 25‐nm resolution on conventional
    microscopes,” <i>EMBO reports</i>, vol. 19, no. 9. EMBO, 2018.
  ista: Truckenbrodt SM, Maidorn M, Crzan D, Wildhagen H, Kabatas S, Rizzoli SO. 2018.
    X10 expansion microscopy enables 25‐nm resolution on conventional microscopes.
    EMBO reports. 19(9), e45836.
  mla: Truckenbrodt, Sven M., et al. “X10 Expansion Microscopy Enables 25‐nm Resolution
    on Conventional Microscopes.” <i>EMBO Reports</i>, vol. 19, no. 9, e45836, EMBO,
    2018, doi:<a href="https://doi.org/10.15252/embr.201845836">10.15252/embr.201845836</a>.
  short: S.M. Truckenbrodt, M. Maidorn, D. Crzan, H. Wildhagen, S. Kabatas, S.O. Rizzoli,
    EMBO Reports 19 (2018).
date_created: 2019-05-28T13:16:08Z
date_published: 2018-09-01T00:00:00Z
date_updated: 2023-09-19T14:52:32Z
day: '01'
ddc:
- '580'
department:
- _id: JoDa
doi: 10.15252/embr.201845836
external_id:
  isi:
  - '000443682200009'
file:
- access_level: open_access
  checksum: 6ec90abc637f09cca3a7b6424d7e7a26
  content_type: application/pdf
  creator: kschuh
  date_created: 2019-05-28T13:17:19Z
  date_updated: 2020-07-14T12:47:32Z
  file_id: '6500'
  file_name: 2018_embo_Truckenbrodt.pdf
  file_size: 2005572
  relation: main_file
file_date_updated: 2020-07-14T12:47:32Z
has_accepted_license: '1'
intvolume: '        19'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: EMBO reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
scopus_import: '1'
status: public
title: X10 expansion microscopy enables 25‐nm resolution on conventional microscopes
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: 19
year: '2018'
...
---
_id: '11105'
abstract:
- lang: eng
  text: Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear
    envelope (NE), which is a double membrane that encloses the nuclear genome of
    eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells
    is composed of multiple copies of 30 different proteins known as nucleoporins.
    The evolutionarily conserved NPC proteins have the well-characterized function
    of mediating the transport of molecules between the nucleoplasm and the cytoplasm.
    Mutations in nucleoporins are often linked to specific developmental defects and
    disease, and the resulting phenotypes are usually interpreted as the consequences
    of perturbed nuclear transport activity. However, recent evidence suggests that
    NPCs have additional functions in chromatin organization and gene regulation,
    some of which might be independent of nuclear transport. Here, we review the transport-dependent
    and transport-independent roles of NPCs in the regulation of nuclear function
    and gene expression.
article_processing_charge: No
article_type: original
author:
- first_name: Maya
  full_name: Capelson, Maya
  last_name: Capelson
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
citation:
  ama: Capelson M, Hetzer M. The role of nuclear pores in gene regulation, development
    and disease. <i>EMBO reports</i>. 2009;10(7):697-705. doi:<a href="https://doi.org/10.1038/embor.2009.147">10.1038/embor.2009.147</a>
  apa: Capelson, M., &#38; Hetzer, M. (2009). The role of nuclear pores in gene regulation,
    development and disease. <i>EMBO Reports</i>. EMBO. <a href="https://doi.org/10.1038/embor.2009.147">https://doi.org/10.1038/embor.2009.147</a>
  chicago: Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation,
    Development and Disease.” <i>EMBO Reports</i>. EMBO, 2009. <a href="https://doi.org/10.1038/embor.2009.147">https://doi.org/10.1038/embor.2009.147</a>.
  ieee: M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation,
    development and disease,” <i>EMBO reports</i>, vol. 10, no. 7. EMBO, pp. 697–705,
    2009.
  ista: Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation,
    development and disease. EMBO reports. 10(7), 697–705.
  mla: Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation,
    Development and Disease.” <i>EMBO Reports</i>, vol. 10, no. 7, EMBO, 2009, pp.
    697–705, doi:<a href="https://doi.org/10.1038/embor.2009.147">10.1038/embor.2009.147</a>.
  short: M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705.
date_created: 2022-04-07T07:54:06Z
date_published: 2009-07-01T00:00:00Z
date_updated: 2022-07-18T08:42:44Z
day: '01'
doi: 10.1038/embor.2009.147
extern: '1'
external_id:
  pmid:
  - '19543230'
intvolume: '        10'
issue: '7'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/embor.2009.147
month: '07'
oa: 1
oa_version: Published Version
page: 697-705
pmid: 1
publication: EMBO reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
related_material:
  link:
  - relation: erratum
    url: https://doi.org/10.1038/embor.2009.176
scopus_import: '1'
status: public
title: The role of nuclear pores in gene regulation, development and disease
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 10
year: '2009'
...
---
_id: '11116'
abstract:
- lang: eng
  text: The metazoan nuclear envelope (NE) breaks down and re-forms during each cell
    cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport
    during interphase, assemble into the re-forming NE at the end of mitosis. Using
    in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal
    effect lethal), a recently discovered NE component in Caenorhabditis elegans,
    functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex
    (Nup for nucleoporin), an important building block of the NPC, and is essential
    for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28
    acts as a seeding point for NPC assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Cerstin
  full_name: Franz, Cerstin
  last_name: Franz
- first_name: Rudolf
  full_name: Walczak, Rudolf
  last_name: Walczak
- first_name: Sevil
  full_name: Yavuz, Sevil
  last_name: Yavuz
- first_name: Rachel
  full_name: Santarella, Rachel
  last_name: Santarella
- first_name: Marc
  full_name: Gentzel, Marc
  last_name: Gentzel
- first_name: Peter
  full_name: Askjaer, Peter
  last_name: Askjaer
- first_name: Vincent
  full_name: Galy, Vincent
  last_name: Galy
- 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: Iain W
  full_name: Mattaj, Iain W
  last_name: Mattaj
- first_name: Wolfram
  full_name: Antonin, Wolfram
  last_name: Antonin
citation:
  ama: Franz C, Walczak R, Yavuz S, et al. MEL‐28/ELYS is required for the recruitment
    of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO
    reports</i>. 2007;8(2):165-172. doi:<a href="https://doi.org/10.1038/sj.embor.7400889">10.1038/sj.embor.7400889</a>
  apa: Franz, C., Walczak, R., Yavuz, S., Santarella, R., Gentzel, M., Askjaer, P.,
    … Antonin, W. (2007). MEL‐28/ELYS is required for the recruitment of nucleoporins
    to chromatin and postmitotic nuclear pore complex assembly. <i>EMBO Reports</i>.
    EMBO. <a href="https://doi.org/10.1038/sj.embor.7400889">https://doi.org/10.1038/sj.embor.7400889</a>
  chicago: Franz, Cerstin, Rudolf Walczak, Sevil Yavuz, Rachel Santarella, Marc Gentzel,
    Peter Askjaer, Vincent Galy, Martin Hetzer, Iain W Mattaj, and Wolfram Antonin.
    “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and
    Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>. EMBO, 2007. <a
    href="https://doi.org/10.1038/sj.embor.7400889">https://doi.org/10.1038/sj.embor.7400889</a>.
  ieee: C. Franz <i>et al.</i>, “MEL‐28/ELYS is required for the recruitment of nucleoporins
    to chromatin and postmitotic nuclear pore complex assembly,” <i>EMBO reports</i>,
    vol. 8, no. 2. EMBO, pp. 165–172, 2007.
  ista: Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, Galy V, Hetzer
    M, Mattaj IW, Antonin W. 2007. MEL‐28/ELYS is required for the recruitment of
    nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO
    reports. 8(2), 165–172.
  mla: Franz, Cerstin, et al. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins
    to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” <i>EMBO Reports</i>,
    vol. 8, no. 2, EMBO, 2007, pp. 165–72, doi:<a href="https://doi.org/10.1038/sj.embor.7400889">10.1038/sj.embor.7400889</a>.
  short: C. Franz, R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V.
    Galy, M. Hetzer, I.W. Mattaj, W. Antonin, EMBO Reports 8 (2007) 165–172.
date_created: 2022-04-07T07:56:13Z
date_published: 2007-01-19T00:00:00Z
date_updated: 2022-07-18T08:56:40Z
day: '19'
doi: 10.1038/sj.embor.7400889
extern: '1'
external_id:
  pmid:
  - '17235358'
intvolume: '         8'
issue: '2'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/sj.embor.7400889
month: '01'
oa: 1
oa_version: Published Version
page: 165-172
pmid: 1
publication: EMBO reports
publication_identifier:
  eissn:
  - 1469-3178
  issn:
  - 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
scopus_import: '1'
status: public
title: MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and
  postmitotic nuclear pore complex assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 8
year: '2007'
...
---
_id: '6151'
author:
- first_name: Iris
  full_name: Salecker, Iris
  last_name: Salecker
- first_name: Michael
  full_name: Häusser, Michael
  last_name: Häusser
- first_name: Mario
  full_name: de Bono, Mario
  id: 4E3FF80E-F248-11E8-B48F-1D18A9856A87
  last_name: de Bono
  orcid: 0000-0001-8347-0443
citation:
  ama: 'Salecker I, Häusser M, de Bono M. On the axonal road to circuit function and
    behaviour: Workshop on the assembly and function of neuronal circuits. <i>EMBO
    reports</i>. 2006;7(6):585-589. doi:<a href="https://doi.org/10.1038/sj.embor.7400713">10.1038/sj.embor.7400713</a>'
  apa: 'Salecker, I., Häusser, M., &#38; de Bono, M. (2006). On the axonal road to
    circuit function and behaviour: Workshop on the assembly and function of neuronal
    circuits. <i>EMBO Reports</i>. Wiley. <a href="https://doi.org/10.1038/sj.embor.7400713">https://doi.org/10.1038/sj.embor.7400713</a>'
  chicago: 'Salecker, Iris, Michael Häusser, and Mario de Bono. “On the Axonal Road
    to Circuit Function and Behaviour: Workshop on the Assembly and Function of Neuronal
    Circuits.” <i>EMBO Reports</i>. Wiley, 2006. <a href="https://doi.org/10.1038/sj.embor.7400713">https://doi.org/10.1038/sj.embor.7400713</a>.'
  ieee: 'I. Salecker, M. Häusser, and M. de Bono, “On the axonal road to circuit function
    and behaviour: Workshop on the assembly and function of neuronal circuits,” <i>EMBO
    reports</i>, vol. 7, no. 6. Wiley, pp. 585–589, 2006.'
  ista: 'Salecker I, Häusser M, de Bono M. 2006. On the axonal road to circuit function
    and behaviour: Workshop on the assembly and function of neuronal circuits. EMBO
    reports. 7(6), 585–589.'
  mla: 'Salecker, Iris, et al. “On the Axonal Road to Circuit Function and Behaviour:
    Workshop on the Assembly and Function of Neuronal Circuits.” <i>EMBO Reports</i>,
    vol. 7, no. 6, Wiley, 2006, pp. 585–89, doi:<a href="https://doi.org/10.1038/sj.embor.7400713">10.1038/sj.embor.7400713</a>.'
  short: I. Salecker, M. Häusser, M. de Bono, EMBO Reports 7 (2006) 585–589.
date_created: 2019-03-21T08:50:43Z
date_published: 2006-06-01T00:00:00Z
date_updated: 2021-01-12T08:06:23Z
day: '01'
doi: 10.1038/sj.embor.7400713
extern: '1'
external_id:
  pmid:
  - '16729018'
intvolume: '         7'
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://europepmc.org/articles/pmc1479602
month: '06'
oa: 1
oa_version: Published Version
page: 585-589
pmid: 1
publication: EMBO reports
publication_identifier:
  issn:
  - 1469-221X
  - 1469-3178
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: 'On the axonal road to circuit function and behaviour: Workshop on the assembly
  and function of neuronal circuits'
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 7
year: '2006'
...
