---
OA_place: publisher
OA_type: hybrid
_id: '18621'
abstract:
- lang: eng
  text: During neural development, cellular adhesion is crucial for interactions among
    and between neurons and surrounding tissues. This function is mediated by conserved
    cell adhesion molecules, which are tightly regulated to allow for coordinated
    neuronal outgrowth. Here, we show that the proprotein convertase KPC-1 (homolog
    of mammalian furin) regulates the Menorin adhesion complex during development
    of PVD dendritic arbors in Caenorhabditis elegans. We found a finely regulated
    antagonistic balance between PVD-expressed KPC-1 and the epidermally expressed
    putative cell adhesion molecule MNR-1 (Menorin). Genetically, partial loss of
    mnr-1 suppressed partial loss of kpc-1, and both loss of kpc-1 and transgenic
    overexpression of mnr-1 resulted in indistinguishable phenotypes in PVD dendrites.
    This balance regulated cell-surface localization of the DMA-1 leucine-rich transmembrane
    receptor in PVD neurons. Lastly, kpc-1 mutants showed increased amounts of MNR-1
    and decreased amounts of muscle-derived LECT-2 (Chondromodulin II), which is also
    part of the Menorin adhesion complex. These observations suggest that KPC-1 in
    PVD neurons directly or indirectly controls the abundance of proteins of the Menorin
    adhesion complex from adjacent tissues, thereby providing negative feedback from
    the dendrite to the instructive cues of surrounding tissues.
acknowledgement: "We thank members of the Bülow laboratory for comments on the manuscript
  and discussions throughout the course of this work; and Ryan Peer and William Corman
  for their initial help with the modifier genetic screen. We acknowledge the Genomics
  Core facility and the Advanced Imaging Facility at Albert Einstein College of Medicine
  for help during these studies. We are grateful to Kang Shen, David Miller and the
  Caenorhabditis Genetics Center (which is funded by National Institutes of Health
  Office of Research Infrastructure Programs P40OD0104400) for some of the strains
  used in this study, and Lhisia Chen for the anti-SAX-7 antibody.\r\nThis work was
  supported by grants from the National Institutes of Health (F31NS100370 to M.R.;
  T32GM007288 and F31NS111939 to M.T.; R01NS096672, R21NS081505 and R01NS129992 to
  H.E.B.; and P30HD071593 to Albert Einstein College of Medicine). N.J.R.-S. was the
  recipient of a Colciencias-Fulbright Fellowship [funded by Departamento Administrativo
  de Ciencia, Tecnología e Innovación (COLCIENCIAS) and Fulbright Colombia], L.T.H.T.
  of a Croucher Foundation Fellowship, and H.E.B. of an Irma T. Hirschl Trust/Monique
  Weill-Caulier Trust research fellowship. Open Access funding provided by Albert
  Einstein College of Medicine, Yeshiva University. Deposited in PMC for immediate
  release."
article_processing_charge: No
article_type: original
author:
- first_name: Nelson
  full_name: Ramirez, Nelson
  id: 39831956-E4FE-11E9-85DE-0DC7E5697425
  last_name: Ramirez
- first_name: Helen M.
  full_name: Belalcazar, Helen M.
  last_name: Belalcazar
- first_name: Maisha
  full_name: Rahman, Maisha
  last_name: Rahman
- first_name: Meera
  full_name: Trivedi, Meera
  last_name: Trivedi
- first_name: Leo T. H.
  full_name: Tang, Leo T. H.
  last_name: Tang
- first_name: Hannes E.
  full_name: Bülow, Hannes E.
  last_name: Bülow
citation:
  ama: Ramirez N, Belalcazar HM, Rahman M, Trivedi M, Tang LTH, Bülow HE. Convertase-dependent
    regulation of membrane-tethered and secreted ligands tunes dendrite adhesion.
    <i>Development</i>. 2023;150(18). doi:<a href="https://doi.org/10.1242/dev.201208">10.1242/dev.201208</a>
  apa: Ramirez, N., Belalcazar, H. M., Rahman, M., Trivedi, M., Tang, L. T. H., &#38;
    Bülow, H. E. (2023). Convertase-dependent regulation of membrane-tethered and
    secreted ligands tunes dendrite adhesion. <i>Development</i>. The Company of Biologists.
    <a href="https://doi.org/10.1242/dev.201208">https://doi.org/10.1242/dev.201208</a>
  chicago: Ramirez, Nelson, Helen M. Belalcazar, Maisha Rahman, Meera Trivedi, Leo
    T. H. Tang, and Hannes E. Bülow. “Convertase-Dependent Regulation of Membrane-Tethered
    and Secreted Ligands Tunes Dendrite Adhesion.” <i>Development</i>. The Company
    of Biologists, 2023. <a href="https://doi.org/10.1242/dev.201208">https://doi.org/10.1242/dev.201208</a>.
  ieee: N. Ramirez, H. M. Belalcazar, M. Rahman, M. Trivedi, L. T. H. Tang, and H.
    E. Bülow, “Convertase-dependent regulation of membrane-tethered and secreted ligands
    tunes dendrite adhesion,” <i>Development</i>, vol. 150, no. 18. The Company of
    Biologists, 2023.
  ista: Ramirez N, Belalcazar HM, Rahman M, Trivedi M, Tang LTH, Bülow HE. 2023. Convertase-dependent
    regulation of membrane-tethered and secreted ligands tunes dendrite adhesion.
    Development. 150(18).
  mla: Ramirez, Nelson, et al. “Convertase-Dependent Regulation of Membrane-Tethered
    and Secreted Ligands Tunes Dendrite Adhesion.” <i>Development</i>, vol. 150, no.
    18, The Company of Biologists, 2023, doi:<a href="https://doi.org/10.1242/dev.201208">10.1242/dev.201208</a>.
  short: N. Ramirez, H.M. Belalcazar, M. Rahman, M. Trivedi, L.T.H. Tang, H.E. Bülow,
    Development 150 (2023).
date_created: 2024-12-04T22:02:52Z
date_published: 2023-09-18T00:00:00Z
date_updated: 2024-12-09T11:43:40Z
day: '18'
ddc:
- '570'
doi: 10.1242/dev.201208
extern: '1'
external_id:
  pmid:
  - '37721334'
file:
- access_level: open_access
  checksum: d2158dc56db50457e6404c4afec4401c
  content_type: application/pdf
  creator: nramirez
  date_created: 2024-12-04T22:12:04Z
  date_updated: 2024-12-04T22:12:04Z
  file_id: '18624'
  file_name: dev201208.pdf
  file_size: 9559527
  relation: main_file
  success: 1
file_date_updated: 2024-12-04T22:12:04Z
fulldoi: https://doi.org/10.1242/dev.201208
has_accepted_license: '1'
intvolume: '       150'
issue: '18'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
publication: Development
publication_identifier:
  eissn:
  - 1477-9129
  issn:
  - 0950-1991
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
scopus_import: '1'
status: public
title: Convertase-dependent regulation of membrane-tethered and secreted ligands tunes
  dendrite adhesion
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 150
year: '2023'
...
---
_id: '11637'
abstract:
- lang: eng
  text: The ability to detect and respond to acute oxygen (O2) shortages is indispensable
    to aerobic life. The molecular mechanisms and circuits underlying this capacity
    are poorly understood. Here, we characterize the behavioral responses of feeding
    Caenorhabditis elegans to approximately 1% O2. Acute hypoxia triggers a bout of
    turning maneuvers followed by a persistent switch to rapid forward movement as
    animals seek to avoid and escape hypoxia. While the behavioral responses to 1%
    O2 closely resemble those evoked by 21% O2, they have distinct molecular and circuit
    underpinnings. Disrupting phosphodiesterases (PDEs), specific G proteins, or BBSome
    function inhibits escape from 1% O2 due to increased cGMP signaling. A primary
    source of cGMP is GCY-28, the ortholog of the atrial natriuretic peptide (ANP)
    receptor. cGMP activates the protein kinase G EGL-4 and enhances neuroendocrine
    secretion to inhibit acute responses to 1% O2. Triggering a rise in cGMP optogenetically
    in multiple neurons, including AIA interneurons, rapidly and reversibly inhibits
    escape from 1% O2. Ca2+ imaging reveals that a 7% to 1% O2 stimulus evokes a Ca2+
    decrease in several neurons. Defects in mitochondrial complex I (MCI) and mitochondrial
    complex I (MCIII), which lead to persistently high reactive oxygen species (ROS),
    abrogate acute hypoxia responses. In particular, repressing the expression of
    isp-1, which encodes the iron sulfur protein of MCIII, inhibits escape from 1%
    O2 without affecting responses to 21% O2. Both genetic and pharmacological up-regulation
    of mitochondrial ROS increase cGMP levels, which contribute to the reduced hypoxia
    responses. Our results implicate ROS and precise regulation of intracellular cGMP
    in the modulation of acute responses to hypoxia by C. elegans.
acknowledgement: ' This work was funded by H2020 European Research Council (ERC Advanced
  grant, 269058 ACMO, https://erc.europa.eu/funding/advanced-grants) and Wellcome
  Trust UK (Wellcome Investigator Award, 209504/Z/17/Z, https://wellcome.org/grant-funding/people-and-projects/grants-awarded/molecular-mechanisms-neural-circuit-function-0)
  to M.d.B, and by H2020 European Research Council (ERC starting grant, 802653 OXYGEN
  SENSING, https://erc.europa.eu/funding/starting-grants) and Vetenskapsrådet (VR
  starting grant, 2018-02216, https://www.vr.se/english.html) to C.C. The funders
  had no role in study design, data collection and analysis, decision to publish,
  or preparation of the manuscript.'
article_number: e3001684
article_processing_charge: No
article_type: original
author:
- first_name: Lina
  full_name: Zhao, Lina
  last_name: Zhao
- first_name: Lorenz A.
  full_name: Fenk, Lorenz A.
  last_name: Fenk
- first_name: Lars
  full_name: Nilsson, Lars
  last_name: Nilsson
- first_name: Niko Paresh
  full_name: Amin-Wetzel, Niko Paresh
  id: E95D3014-9D8C-11E9-9C80-D2F8E5697425
  last_name: Amin-Wetzel
- first_name: Nelson
  full_name: Ramirez, Nelson
  id: 39831956-E4FE-11E9-85DE-0DC7E5697425
  last_name: Ramirez
- first_name: Mario
  full_name: De Bono, Mario
  id: 4E3FF80E-F248-11E8-B48F-1D18A9856A87
  last_name: De Bono
  orcid: 0000-0001-8347-0443
- first_name: Changchun
  full_name: Chen, Changchun
  last_name: Chen
citation:
  ama: Zhao L, Fenk LA, Nilsson L, et al. ROS and cGMP signaling modulate persistent
    escape from hypoxia in Caenorhabditis elegans. <i>PLoS Biology</i>. 2022;20(6).
    doi:<a href="https://doi.org/10.1371/journal.pbio.3001684">10.1371/journal.pbio.3001684</a>
  apa: Zhao, L., Fenk, L. A., Nilsson, L., Amin-Wetzel, N. P., Ramirez, N., de Bono,
    M., &#38; Chen, C. (2022). ROS and cGMP signaling modulate persistent escape from
    hypoxia in Caenorhabditis elegans. <i>PLoS Biology</i>. Public Library of Science.
    <a href="https://doi.org/10.1371/journal.pbio.3001684">https://doi.org/10.1371/journal.pbio.3001684</a>
  chicago: Zhao, Lina, Lorenz A. Fenk, Lars Nilsson, Niko Paresh Amin-Wetzel, Nelson
    Ramirez, Mario de Bono, and Changchun Chen. “ROS and CGMP Signaling Modulate Persistent
    Escape from Hypoxia in Caenorhabditis Elegans.” <i>PLoS Biology</i>. Public Library
    of Science, 2022. <a href="https://doi.org/10.1371/journal.pbio.3001684">https://doi.org/10.1371/journal.pbio.3001684</a>.
  ieee: L. Zhao <i>et al.</i>, “ROS and cGMP signaling modulate persistent escape
    from hypoxia in Caenorhabditis elegans,” <i>PLoS Biology</i>, vol. 20, no. 6.
    Public Library of Science, 2022.
  ista: Zhao L, Fenk LA, Nilsson L, Amin-Wetzel NP, Ramirez N, de Bono M, Chen C.
    2022. ROS and cGMP signaling modulate persistent escape from hypoxia in Caenorhabditis
    elegans. PLoS Biology. 20(6), e3001684.
  mla: Zhao, Lina, et al. “ROS and CGMP Signaling Modulate Persistent Escape from
    Hypoxia in Caenorhabditis Elegans.” <i>PLoS Biology</i>, vol. 20, no. 6, e3001684,
    Public Library of Science, 2022, doi:<a href="https://doi.org/10.1371/journal.pbio.3001684">10.1371/journal.pbio.3001684</a>.
  short: L. Zhao, L.A. Fenk, L. Nilsson, N.P. Amin-Wetzel, N. Ramirez, M. de Bono,
    C. Chen, PLoS Biology 20 (2022).
corr_author: '1'
date_created: 2022-07-24T22:01:42Z
date_published: 2022-06-21T00:00:00Z
date_updated: 2025-04-15T07:32:21Z
day: '21'
ddc:
- '570'
department:
- _id: MaDe
doi: 10.1371/journal.pbio.3001684
external_id:
  isi:
  - '000828679600001'
  pmid:
  - '35727855'
file:
- access_level: open_access
  checksum: df4902f854ad76769d3203bfdc69f16c
  content_type: application/pdf
  creator: dernst
  date_created: 2022-07-25T07:38:49Z
  date_updated: 2022-07-25T07:38:49Z
  file_id: '11643'
  file_name: 2022_PLoSBiology_Zhao.pdf
  file_size: 3721585
  relation: main_file
  success: 1
file_date_updated: 2022-07-25T07:38:49Z
fulldoi: https://doi.org/10.1371/journal.pbio.3001684
has_accepted_license: '1'
intvolume: '        20'
isi: 1
issue: '6'
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 23870BE8-32DE-11EA-91FC-C7463DDC885E
  grant_number: 209504/A/17/Z
  name: Molecular mechanisms of neural circuit function
publication: PLoS Biology
publication_identifier:
  eissn:
  - 1545-7885
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: ROS and cGMP signaling modulate persistent escape from hypoxia in Caenorhabditis
  elegans
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: 20
year: '2022'
...
---
_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: 2026-06-18T17:26:25Z
day: '05'
ddc:
- '570'
department:
- _id: MaDe
doi: 10.15252/embr.202154163
external_id:
  isi:
  - '000797302700001'
  pmid:
  - '35586945'
fulldoi: https://doi.org/10.15252/embr.202154163
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: '15272'
abstract:
- lang: eng
  text: The assembly of neuronal circuits involves the migrations of neurons from
    their place of birth to their final location in the nervous system, as well as
    the coordinated growth and patterning of axons and dendrites. In screens for genes
    required for patterning of the nervous system, we identified the <jats:italic>catp-8/P5A-ATPase</jats:italic>
    as an important regulator of neural patterning. P5A-ATPases are part of the P-type
    ATPases, a family of proteins known to serve a conserved function as transporters
    of ions, lipids and polyamines in unicellular eukaryotes, plants, and humans.
    While the function of many P-type ATPases is relatively well understood, the function
    of P5A-ATPases in metazoans remained elusive. We show here, that the <jats:italic>Caenorhabditis
    elegans</jats:italic> ortholog <jats:italic>catp-8/P5A-ATPase</jats:italic> is
    required for defined aspects of nervous system development. Specifically, the
    <jats:italic>catp-8/P5A-ATPase</jats:italic> serves functions in shaping the elaborately
    sculpted dendritic trees of somatosensory PVD neurons. Moreover, <jats:italic>catp-8/P5A-ATPase</jats:italic>
    is required for axonal guidance and repulsion at the midline, as well as embryonic
    and postembryonic neuronal migrations. Interestingly, not all axons at the midline
    require <jats:italic>catp-8/P5A-ATPase</jats:italic>, although the axons run in
    the same fascicles and navigate the same space. Similarly, not all neuronal migrations
    require <jats:italic>catp-8/P5A-ATPase</jats:italic>. A CATP-8/P5A-ATPase reporter
    is localized to the ER in most, if not all, tissues and <jats:italic>catp-8/P5A-ATPase</jats:italic>
    can function both cell-autonomously and non-autonomously to regulate neuronal
    development. Genetic analyses establish that <jats:italic>catp-8/P5A-ATPase</jats:italic>
    can function in multiple pathways, including the Menorin pathway, previously shown
    to control dendritic patterning in PVD, and Wnt signaling, which functions to
    control neuronal migrations. Lastly, we show that <jats:italic>catp-8/P5A-ATPase</jats:italic>
    is required for localizing select transmembrane proteins necessary for dendrite
    morphogenesis. Collectively, our studies suggest that <jats:italic>catp-8/P5A-ATPase</jats:italic>
    serves diverse, yet specific, roles in different genetic pathways and may be involved
    in the regulation or localization of transmembrane and secreted proteins to specific
    subcellular compartments.
article_number: e1009475
article_processing_charge: No
article_type: original
author:
- first_name: Leo T. H.
  full_name: Tang, Leo T. H.
  last_name: Tang
- first_name: Meera
  full_name: Trivedi, Meera
  last_name: Trivedi
- first_name: Jenna
  full_name: Freund, Jenna
  last_name: Freund
- first_name: Christopher J.
  full_name: Salazar, Christopher J.
  last_name: Salazar
- 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: Garrett
  full_name: Lee, Garrett
  last_name: Lee
- first_name: Yu
  full_name: Wang, Yu
  last_name: Wang
- first_name: Barth D.
  full_name: Grant, Barth D.
  last_name: Grant
- first_name: Hannes E.
  full_name: Bülow, Hannes E.
  last_name: Bülow
citation:
  ama: Tang LTH, Trivedi M, Freund J, et al. The CATP-8/P5A-type ATPase functions
    in multiple pathways during neuronal patterning. <i>PLOS Genetics</i>. 2021;17(7).
    doi:<a href="https://doi.org/10.1371/journal.pgen.1009475">10.1371/journal.pgen.1009475</a>
  apa: Tang, L. T. H., Trivedi, M., Freund, J., Salazar, C. J., Rahman, M., Ramirez,
    N., … Bülow, H. E. (2021). The CATP-8/P5A-type ATPase functions in multiple pathways
    during neuronal patterning. <i>PLOS Genetics</i>. Public Library of Science. <a
    href="https://doi.org/10.1371/journal.pgen.1009475">https://doi.org/10.1371/journal.pgen.1009475</a>
  chicago: Tang, Leo T. H., Meera Trivedi, Jenna Freund, Christopher J. Salazar, Maisha
    Rahman, Nelson Ramirez, Garrett Lee, Yu Wang, Barth D. Grant, and Hannes E. Bülow.
    “The CATP-8/P5A-Type ATPase Functions in Multiple Pathways during Neuronal Patterning.”
    <i>PLOS Genetics</i>. Public Library of Science, 2021. <a href="https://doi.org/10.1371/journal.pgen.1009475">https://doi.org/10.1371/journal.pgen.1009475</a>.
  ieee: L. T. H. Tang <i>et al.</i>, “The CATP-8/P5A-type ATPase functions in multiple
    pathways during neuronal patterning,” <i>PLOS Genetics</i>, vol. 17, no. 7. Public
    Library of Science, 2021.
  ista: Tang LTH, Trivedi M, Freund J, Salazar CJ, Rahman M, Ramirez N, Lee G, Wang
    Y, Grant BD, Bülow HE. 2021. The CATP-8/P5A-type ATPase functions in multiple
    pathways during neuronal patterning. PLOS Genetics. 17(7), e1009475.
  mla: Tang, Leo T. H., et al. “The CATP-8/P5A-Type ATPase Functions in Multiple Pathways
    during Neuronal Patterning.” <i>PLOS Genetics</i>, vol. 17, no. 7, e1009475, Public
    Library of Science, 2021, doi:<a href="https://doi.org/10.1371/journal.pgen.1009475">10.1371/journal.pgen.1009475</a>.
  short: L.T.H. Tang, M. Trivedi, J. Freund, C.J. Salazar, M. Rahman, N. Ramirez,
    G. Lee, Y. Wang, B.D. Grant, H.E. Bülow, PLOS Genetics 17 (2021).
date_created: 2024-04-03T07:57:12Z
date_published: 2021-07-01T00:00:00Z
date_updated: 2024-04-10T08:57:16Z
day: '01'
ddc:
- '570'
department:
- _id: MaDe
doi: 10.1371/journal.pgen.1009475
external_id:
  pmid:
  - '34197450'
file:
- access_level: open_access
  checksum: 7352b195e4db6d404f702fe6ad8b55ad
  content_type: application/pdf
  creator: dernst
  date_created: 2024-04-10T08:53:43Z
  date_updated: 2024-04-10T08:53:43Z
  file_id: '15308'
  file_name: 2021_PlosGenetics_Tang.pdf
  file_size: 4224934
  relation: main_file
  success: 1
file_date_updated: 2024-04-10T08:53:43Z
fulldoi: https://doi.org/10.1371/journal.pgen.1009475
has_accepted_license: '1'
intvolume: '        17'
issue: '7'
keyword:
- Cancer Research
- Genetics (clinical)
- Genetics
- Molecular Biology
- Ecology
- Evolution
- Behavior and Systematics
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: PLOS Genetics
publication_identifier:
  issn:
  - 1553-7404
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
status: public
title: The CATP-8/P5A-type ATPase functions in multiple pathways during neuronal patterning
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 17
year: '2021'
...
