Associated Papers
Pathobiologic Mechanisms of Neurodegeneration in Osteopetrosis Derived From Structural and Functional Analysis of 14 ClC-7 Mutants.
Di Zanni E et al.
Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research, 2021
Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1.
Schrecker M et al.
Elife, 2020
Molecular insights into the human CLC-7/Ostm1 transporter.
Zhang S et al.
Science Advances, 2020
A Novel Variant in CLCN7 Regulates the Coupling of Angiogenesis and Osteogenesis.
Peng H et al.
Frontiers in Cell and Developmental Biology, 2020
Common gating of both CLC transporter subunits underlies voltage-dependent activation of the 2Cl-/1H+ exchanger ClC-7/Ostm1.
Ludwig CF et al.
The Journal of Biological Chemistry, 2013
ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1 for transport activity.
Leisle L et al.
The Embo Journal, 2011
CBS domains: structure, function, and pathology in human proteins.
Ignoul S et al.
American Journal of Physiology. Cell Physiology, 2005
Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis.
Frattini A et al.
Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research, 2003
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