---
res:
  bibo_abstract:
  - Collagens are fundamental components of extracellular matrices, requiring precise
    intracellular post-translational modifications for proper function. Among the
    modifications, prolyl 4-hydroxylation is critical to stabilise the collagen triple
    helix. In humans, this reaction is mediated by collagen prolyl 4-hydroxylases
    (P4Hs). While humans possess three genes encoding these enzymes (P4H⍺s), Drosophila
    melanogaster harbour at least 26 candidates for collagen P4H⍺s despite its simple
    genome, and it is poorly understood which of them are actually working on collagen
    in the fly. In this study, we addressed this question by carrying out thorough
    bioinformatic and biochemical analyses. We demonstrate that among the 26 potential
    collagen P4H⍺s, PH4⍺EFB shares the highest homology with vertebrate collagen P4H⍺s.
    Furthermore, while collagen P4Hs and their substrates must exist in the same cells,
    our transcriptomic analyses at the tissue and single cell levels showed a global
    co-expression of PH4⍺EFB but not the other P4H⍺-related genes with the collagen
    IV genes. Moreover, expression of PH4⍺EFB during embryogenesis was found to precede
    that of collagen IV, presumably enabling efficient collagen modification by PH4⍺EFB.
    Finally, biochemical assays confirm that PH4⍺EFB binds collagen, supporting its
    direct role in collagen IV modification. Collectively, we identify PH4⍺EFB as
    the primary and potentially constitutive prolyl 4-hydroxylase responsible for
    collagen IV biosynthesis in Drosophila. Our findings highlight the remarkably
    simple nature of Drosophila collagen IV biosynthesis, which may serve as a blueprint
    for defining the minimal requirements for collagen engineering.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Yoshihiro
      foaf_name: Ishikawa, Yoshihiro
      foaf_surname: Ishikawa
  - foaf_Person:
      foaf_givenName: Melissa A
      foaf_name: Toups, Melissa A
      foaf_surname: Toups
      foaf_workInfoHomepage: http://www.librecat.org/personId=4E099E4E-F248-11E8-B48F-1D18A9856A87
    orcid: 0000-0002-9752-7380
  - foaf_Person:
      foaf_givenName: Marwan N
      foaf_name: Elkrewi, Marwan N
      foaf_surname: Elkrewi
      foaf_workInfoHomepage: http://www.librecat.org/personId=0B46FACA-A8E1-11E9-9BD3-79D1E5697425
    orcid: 0000-0002-5328-7231
  - foaf_Person:
      foaf_givenName: Allison L.
      foaf_name: Zajac, Allison L.
      foaf_surname: Zajac
  - foaf_Person:
      foaf_givenName: Sally
      foaf_name: Horne-Badovinac, Sally
      foaf_surname: Horne-Badovinac
  - foaf_Person:
      foaf_givenName: Yutaka
      foaf_name: Matsubayashi, Yutaka
      foaf_surname: Matsubayashi
  bibo_doi: 10.1016/j.matbio.2025.09.002
  bibo_issue: '11'
  bibo_volume: 141
  dct_date: 2025^xs_gYear
  dct_identifier:
  - UT:001583892100002
  dct_isPartOf:
  - http://id.crossref.org/issn/0945-053X
  - http://id.crossref.org/issn/1569-1802
  dct_language: eng
  dct_publisher: Springer Nature@
  dct_title: Evidence for the major role of PH4⍺EFB in the prolyl 4-hydroxylation
    of Drosophila collagen IV@
  fabio_hasPubmedId: '40946811'
...