Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Aileen M Barnes"'
Autor:
Wayne A Cabral, Masaki Ishikawa, Matthias Garten, Elena N Makareeva, Brandi M Sargent, MaryAnn Weis, Aileen M Barnes, Emma A Webb, Nicholas J Shaw, Leena Ala-Kokko, Felicitas L Lacbawan, Wolfgang Högler, Sergey Leikin, Paul S Blank, Joshua Zimmerberg, David R Eyre, Yoshihiko Yamada, Joan C Marini
Publikováno v:
PLoS Genetics, Vol 12, Iss 7, p e1006156 (2016)
Recessive osteogenesis imperfecta (OI) is caused by defects in proteins involved in post-translational interactions with type I collagen. Recently, a novel form of moderately severe OI caused by null mutations in TMEM38B was identified. TMEM38B encod
Externí odkaz:
https://doaj.org/article/658422182509483ea7dca5eabb1f1822
Autor:
Masaki Takagi, Tomohiro Ishii, Aileen M Barnes, Maryann Weis, Naoko Amano, Mamoru Tanaka, Ryuji Fukuzawa, Gen Nishimura, David R Eyre, Joan C Marini, Tomonobu Hasegawa
Publikováno v:
PLoS ONE, Vol 7, Iss 5, p e36809 (2012)
Prolyl 3-hydroxylase 1 (P3H1), encoded by the LEPRE1 gene, forms a molecular complex with cartilage-associated protein (CRTAP) and cyclophilin B (encoded by PPIB) in the endoplasmic reticulum (ER). This complex is responsible for one step in collagen
Externí odkaz:
https://doaj.org/article/0d93908116af42a4875fa8c97b151bee
Autor:
Ahmed El-Gazzar, Heeseog Kang, Nadja Fratzl-Zelman, Emma Webb, Aileen M. Barnes, Milena Jovanovic, Sarju G. Mehta, Vipan Datta, Vrinda Saraff, Ryan K. Dale, Frank Rauch, Joan C. Marini, Wolfgang Högler
Publikováno v:
Bone Reports, Vol 17, Iss , Pp 101603- (2022)
Loss-of-function mutations in SMAD3 cause Loeys-Dietz syndrome type 3 (LDS3), a rare autosomal-dominant connective tissue disorder characterized by vascular pathology and skeletal abnormalities. Dysregulation of TGF-β/SMAD signaling is associated wi
Externí odkaz:
https://doaj.org/article/1f68113aa43d49cb8cfd80c68511f175
Autor:
Uschi Lindert, Wayne A. Cabral, Surasawadee Ausavarat, Siraprapa Tongkobpetch, Katja Ludin, Aileen M. Barnes, Patra Yeetong, Maryann Weis, Birgit Krabichler, Chalurmpon Srichomthong, Elena N. Makareeva, Andreas R. Janecke, Sergey Leikin, Benno Röthlisberger, Marianne Rohrbach, Ingo Kennerknecht, David R. Eyre, Kanya Suphapeetiporn, Cecilia Giunta, Joan C. Marini, Vorasuk Shotelersuk
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Osteogenesis imperfecta (OI) is genetically linked to autosomal dominant or autosomal recessive mutations. Here, Marini et al. describe two families with X-chromosome-linked OI with mutations in MBTPS2 that alter regulated intramembrane proteolysis a
Externí odkaz:
https://doaj.org/article/a84048b3358e400b90b24ee8963af381
Autor:
Nadia Garibaldi, Roberta Besio, Raymond Dalgleish, Simona Villani, Aileen M. Barnes, Joan C. Marini, Antonella Forlino
Publikováno v:
Disease Models & Mechanisms. 15
Osteogenesis imperfecta (OI) is a heterogeneous family of collagen type I-related diseases characterized by bone fragility. OI is most commonly caused by single-nucleotide substitutions that replace glycine residues or exon splicing defects in the CO
Autor:
MaryAnn Weis, Nadja Fratzl-Zelman, Paul Roschger, Joseph E. Perosky, Sergey Leikin, Wayne A. Cabral, David R. Eyre, Kenneth M. Kozloff, Heeseog Kang, Peter S. Backlund, Elena Makareeva, Antonella Forlino, Joan C. Marini, Adrienne Alimasa, Rachel Harris, Klaus Klaushofer, Aileen M. Barnes
Publikováno v:
Matrix Biol
Null mutations in CRTAP or P3H1, encoding cartilage-associated protein and prolyl 3-hydroxylase 1, cause the severe bone dysplasias, types VII and VIII osteogenesis imperfecta. Lack of either protein prevents formation of the ER prolyl 3-hydroxylatio
Autor:
Carsten G. Bönnemann, Johanna Myllyharju, M. Leach, Monkol Lek, Wendy DiNonno, Aileen M. Barnes, Ying Hu, Joan C. Marini, Jahannaz Dastgir, Antti M. Salo, Payam Mohassel, Fransiska Malfait, A. Reghan Foley, Sergey Leikin, Matthew A. Deardorff, Ronald D. Cohn, Sandra Donkervoort, Yaqun Zou, Elena Makareeva
Publikováno v:
Human Molecular Genetics. 26:2207-2217
Collagen prolyl 4-hydroxylases (C-P4Hs) play a central role in the formation and stabilization of the triple helical domain of collagens. P4HA1 encodes the catalytic α(I) subunit of the main C-P4H isoenzyme (C-P4H-I). We now report human bi-allelic
Autor:
Catherine Moali, Joan C. Marini, David R. Eyre, Elena Makareeva, Aileen M. Barnes, Sergey Leikin, Emmanuel Bettler, Marina Brusel, John Cassella, Wayne A. Cabral, David J.S. Hulmes, Aarthi Ashok, Efrat Kessler, MaryAnn Weis
Publikováno v:
Biochim Biophys Acta Mol Basis Dis
Biochimica et Biophysica Acta-Molecular Basis of Disease
Biochimica et Biophysica Acta-Molecular Basis of Disease, Elsevier, 2019, 1865 (9), pp.2210-2223. ⟨10.1016/j.bbadis.2019.04.018⟩
Biochimica et Biophysica Acta-Molecular Basis of Disease
Biochimica et Biophysica Acta-Molecular Basis of Disease, Elsevier, 2019, 1865 (9), pp.2210-2223. ⟨10.1016/j.bbadis.2019.04.018⟩
Mutations in the type I procollagen C-propeptide occur in ~6.5% of Osteogenesis Imperfecta (OI) patients. They are of special interest because this region of procollagen is involved in α chain selection and folding, but is processed prior to fibril
Autor:
Frank Rauch, Joan C. Marini, Cathleen L. Raggio, Paul Roschger, Aileen M. Barnes, Erin Carter, Nadja Fratzl-Zelman, Theresa E. Hefferan, Klaus Klaushofer, David R. Eyre, Peter A. Smith, Giorgio Perino, Weizhong Chang, Francis H. Glorieux, MaryAnn Weis
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 101:3516-3525
Context: Type VIII osteogenesis imperfecta (OI; OMIM 601915) is a recessive form of lethal or severe OI caused by null mutations in P3H1, which encodes prolyl 3-hydroxylase 1. Objectives: Clinical and bone material description of non-lethal type VIII
Autor:
Yan Ma, Joan C. Marini, Min Wang, Yihe Huang, Marco Masci, Adele L. Boskey, Matthew L. Warman, Lyudmila Lukashova, Christina Jacobsen, Laurianne Imbert, Aileen M. Barnes, Lyudmila Spevak
Publikováno v:
Bone. 87:120-129
The Col1a2(+/G610C) knock-in mouse, models osteogenesis imperfecta in a large old order Amish family (OOA) with type IV OI, caused by a G-to-T transversion at nucleotide 2098, which alters the gly-610 codon in the triple-helical domain of the α2(I)