SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human molecular …, 2015 - academic.oup.com
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human Molecular …, 2014 - europepmc.org
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

[PDF][PDF] SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human Molecular …, 2014 - Citeseer
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 …

M Marino, T Stoilova, C Giorgi, A Bachi… - HUMAN MOLECULAR …, 2015 - sfera.unife.it
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

[PDF][PDF] SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human Molecular …, 2015 - iris.unife.it
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human Molecular …, 2015 - search.ebscohost.com
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

[PDF][PDF] SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human Molecular …, 2014 - scholar.archive.org
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 …

M Marino, T Stoilova, C Giorgi, A Bachi… - HUMAN MOLECULAR …, 2015 - ora.uniurb.it
: Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 …

M Marino, T Stoilova, C Giorgi… - Human molecular …, 2015 - pubmed.ncbi.nlm.nih.gov
Selenoprotein N (SEPN1) is a broadly expressed resident protein of the endoplasmic
reticulum (ER) whose loss-of-function inexplicably leads to human muscle disease. We …

[引用][C] SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating …

M Marino, T Stoilova, C Giorgi, A Bachi… - Human Molecular …, 2014 - cir.nii.ac.jp
SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle
pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity …