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Journal of Medical Genetics|July 4, 2001
Disruption of one intra-chain disulphide bond in the carboxyl-terminal propeptide of the proalpha1(I) chain of type I procollagen permits slow assembly and secretion of overmodified, but stable procollagen trimers and results in mild osteogenesis imperfectaJ M Pace, C D Kuslich, M C Willing, et al.
Journal of Veterinary Internal Medicine|February 2, 2011
Neurological causes of diaphragmatic paralysis in 11 alpacas (Vicugna pacos)S Byers, G Barrington, D Nelson, et al.
The Journal of Biological Chemistry|October 25, 1990
Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretionG A Wallis, B J Starman, M F Schwartz, et al.
Nature|December 20, 1990
Localization of dystrophin to postsynaptic regions of central nervous system cortical neuronsH G Lidov, T J Byers, S C Watkins, et al.
Archives of Pathology|May 1, 1975
Acute pulmonary alveolitis in narcotics abuseJ M Byers, J S Soin, R S Fisher, et al.
Journal of Lipid Research|December 31, 1998
Chinese hamster ovary cells overexpressing the oxysterol binding protein (OSBP) display enhanced synthesis of sphingomyelin in response to 25-hydroxycholesterolT A Lagace, D M Byers, H W Cook, et al.
The International Journal of Cardiovascular Imaging|November 29, 2007
MRI of great vessel morphology and function in Ehlers-Danlos syndrome type IVWilliam Kerwin, Melanie Pepin, Lee Mitsumori, et al.
Neurology|August 1, 1996
Spontaneous multivessel cervical artery dissection in a patient with a substitution of alanine for glycine (G13A) in the alpha 1 (I) chain of type I collagenS A Mayer, B S Rubin, B J Starman, et al.
Neurology|March 1, 1992
ELISA quantitation of dystrophin for the diagnosis of Duchenne and Becker muscular dystrophiesT J Byers, P E Neumann, A H Beggs, et al.
The Journal of Biological Chemistry|September 30, 1994
Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein trafficR Duden, M Hosobuchi, S Hamamoto, et al.
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