% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{CantutiCastelvetri:164307,
      author       = {Cantuti-Castelvetri, Ludovico and Ojha, Ravi and Pedro,
                      Liliana Domingues and Djannatian, Minou and Franz, Jonas and
                      Kuivanen, Suvi and van der Meer, Franziska and Kallio, Katri
                      and Kaya, Tugberk and Anastasina, Maria and Smura, Teemu and
                      Levanov, Lev and Szirovicza, Leonora and Tobi, Allan and
                      Kallio-Kokko, Hannimari and Österlund, Pamela and Joensuu,
                      Merja and Meunier, Frédéric A and Butcher, Sarah J and
                      Winkler, Martin Sebastian and Mollenhauer, Brit and
                      Helenius, Ari and Gökce, Ozgun and Teesalu, Tambet and
                      Hepojoki, Jussi and Vapalahti, Olli and Stadelmann,
                      Christine and Balistreri, Giuseppe and Simons, Mikael},
      title        = {{N}europilin-1 facilitates {SARS}-{C}o{V}-2 cell entry and
                      infectivity.},
      journal      = {Science / Science now},
      volume       = {370},
      number       = {6518},
      issn         = {0036-8075},
      address      = {Washington, DC},
      publisher    = {Assoc.},
      reportid     = {DZNE-2022-00961},
      pages        = {856 - 860},
      year         = {2020},
      note         = {ISSN 1095-9203 not unique: **3 hits**.},
      abstract     = {The causative agent of coronavirus disease 2019 (COVID-19)
                      is the severe acute respiratory syndrome coronavirus 2
                      (SARS-CoV-2). For many viruses, tissue tropism is determined
                      by the availability of virus receptors and entry cofactors
                      on the surface of host cells. In this study, we found that
                      neuropilin-1 (NRP1), known to bind furin-cleaved substrates,
                      significantly potentiates SARS-CoV-2 infectivity, an effect
                      blocked by a monoclonal blocking antibody against NRP1. A
                      SARS-CoV-2 mutant with an altered furin cleavage site did
                      not depend on NRP1 for infectivity. Pathological analysis of
                      olfactory epithelium obtained from human COVID-19 autopsies
                      revealed that SARS-CoV-2 infected NRP1-positive cells facing
                      the nasal cavity. Our data provide insight into SARS-CoV-2
                      cell infectivity and define a potential target for antiviral
                      intervention.},
      keywords     = {Angiotensin-Converting Enzyme 2 / Animals / Antibodies,
                      Monoclonal: immunology / Betacoronavirus: genetics /
                      Betacoronavirus: physiology / COVID-19 / Caco-2 Cells /
                      Coronavirus Infections: virology / Female / HEK293 Cells /
                      Host Microbial Interactions / Humans / Lung: metabolism /
                      Male / Metal Nanoparticles / Mice / Mice, Inbred C57BL /
                      Mutation / Neuropilin-1: chemistry / Neuropilin-1: genetics
                      / Neuropilin-1: immunology / Neuropilin-1: metabolism /
                      Neuropilin-2: metabolism / Olfactory Mucosa: metabolism /
                      Olfactory Mucosa: virology / Pandemics / Peptide Fragments:
                      metabolism / Peptidyl-Dipeptidase A: genetics /
                      Peptidyl-Dipeptidase A: metabolism / Pneumonia, Viral:
                      virology / Protein Binding / Protein Domains / Respiratory
                      Mucosa: metabolism / SARS-CoV-2 / Serine Endopeptidases:
                      genetics / Serine Endopeptidases: metabolism / Spike
                      Glycoprotein, Coronavirus: chemistry / Spike Glycoprotein,
                      Coronavirus: metabolism / Virus Internalization /
                      Antibodies, Monoclonal (NLM Chemicals) / NRP1 protein, human
                      (NLM Chemicals) / Neuropilin-2 (NLM Chemicals) / Peptide
                      Fragments (NLM Chemicals) / Spike Glycoprotein, Coronavirus
                      (NLM Chemicals) / neuropilin-2, human (NLM Chemicals) /
                      spike protein, SARS-CoV-2 (NLM Chemicals) / Neuropilin-1
                      (NLM Chemicals) / Peptidyl-Dipeptidase A (NLM Chemicals) /
                      ACE2 protein, human (NLM Chemicals) / Ace2 protein, mouse
                      (NLM Chemicals) / Angiotensin-Converting Enzyme 2 (NLM
                      Chemicals) / Serine Endopeptidases (NLM Chemicals) / TMPRSS2
                      protein, human (NLM Chemicals)},
      cin          = {AG Simons},
      ddc          = {320},
      cid          = {I:(DE-2719)1110008},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33082293},
      pmc          = {pmc:PMC7857391},
      doi          = {10.1126/science.abd2985},
      url          = {https://pub.dzne.de/record/164307},
}