---
res:
  bibo_abstract:
  - The exchange of metabolites between the mitochondrial matrix and the cytosol depends
    on β-barrel channels in the outer membrane and α-helical carrier proteins in the
    inner membrane. The essential translocase of the inner membrane (TIM) chaperones
    escort these proteins through the intermembrane space, but the structural and
    mechanistic details remain elusive. We have used an integrated structural biology
    approach to reveal the functional principle of TIM chaperones. Multiple clamp-like
    binding sites hold the mitochondrial membrane proteins in a translocation-competent
    elongated form, thus mimicking characteristics of co-translational membrane insertion.
    The bound preprotein undergoes conformational dynamics within the chaperone binding
    clefts, pointing to a multitude of dynamic local binding events. Mutations in
    these binding sites cause cell death or growth defects associated with impairment
    of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial
    “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins
    in a “nascent chain-like” conformation through a ribosome-free compartment.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Katharina
      foaf_name: Weinhäupl, Katharina
      foaf_surname: Weinhäupl
  - foaf_Person:
      foaf_givenName: Caroline
      foaf_name: Lindau, Caroline
      foaf_surname: Lindau
  - foaf_Person:
      foaf_givenName: Audrey
      foaf_name: Hessel, Audrey
      foaf_surname: Hessel
  - foaf_Person:
      foaf_givenName: Yong
      foaf_name: Wang, Yong
      foaf_surname: Wang
  - foaf_Person:
      foaf_givenName: Conny
      foaf_name: Schütze, Conny
      foaf_surname: Schütze
  - foaf_Person:
      foaf_givenName: Tobias
      foaf_name: Jores, Tobias
      foaf_surname: Jores
  - foaf_Person:
      foaf_givenName: Laura
      foaf_name: Melchionda, Laura
      foaf_surname: Melchionda
  - foaf_Person:
      foaf_givenName: Birgit
      foaf_name: Schönfisch, Birgit
      foaf_surname: Schönfisch
  - foaf_Person:
      foaf_givenName: Hubert
      foaf_name: Kalbacher, Hubert
      foaf_surname: Kalbacher
  - foaf_Person:
      foaf_givenName: Beate
      foaf_name: Bersch, Beate
      foaf_surname: Bersch
  - foaf_Person:
      foaf_givenName: Doron
      foaf_name: Rapaport, Doron
      foaf_surname: Rapaport
  - foaf_Person:
      foaf_givenName: Martha
      foaf_name: Brennich, Martha
      foaf_surname: Brennich
  - foaf_Person:
      foaf_givenName: Kresten
      foaf_name: Lindorff-Larsen, Kresten
      foaf_surname: Lindorff-Larsen
  - foaf_Person:
      foaf_givenName: Nils
      foaf_name: Wiedemann, Nils
      foaf_surname: Wiedemann
  - foaf_Person:
      foaf_givenName: Paul
      foaf_name: Schanda, Paul
      foaf_surname: Schanda
      foaf_workInfoHomepage: http://www.librecat.org/personId=7B541462-FAF6-11E9-A490-E8DFE5697425
    orcid: 0000-0002-9350-7606
  bibo_doi: 10.1016/j.cell.2018.10.039
  bibo_issue: '5'
  bibo_volume: 175
  dct_date: 2018^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/0092-8674
  dct_language: eng
  dct_publisher: Elsevier@
  dct_subject:
  - General Biochemistry
  - Genetics and Molecular Biology
  dct_title: Structural basis of membrane protein chaperoning through the mitochondrial
    intermembrane space@
...