Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Erich J. Goebel"'
Autor:
Dushyanth Srinivasan, Martin Arostegui, Erich J. Goebel, Kaitlin N. Hart, Senem Aykul, John B. Lees-Shepard, Vincent Idone, Sarah J. Hatsell, Aris N. Economides
Publikováno v:
Biomolecules, Vol 14, Iss 1, p 101 (2024)
Fibrodysplasia ossificans progressiva (FOP) is a rare genetic disorder characterized by episodic yet cumulative heterotopic ossification (HO) of skeletal muscles, tendons, ligaments, and fascia. FOP arises from missense mutations in Activin Receptor
Externí odkaz:
https://doaj.org/article/6a6e2232b14c493f961ed09f4a9f494e
Autor:
Erich J. Goebel, Chandramohan Kattamuri, Gregory R. Gipson, Lavanya Krishnan, Moises Chavez, Magdalena Czepnik, Michelle C. Maguire, Rosa Grenha, Maria Håkansson, Derek T. Logan, Asya V. Grinberg, Dianne Sako, Roselyne Castonguay, Ravindra Kumar, Thomas B. Thompson
Publikováno v:
iScience, Vol 25, Iss 1, Pp 103590- (2022)
Summary: The 30+ unique ligands of the TGFβ family signal by forming complexes using different combinations of type I and type II receptors. Therapeutically, the extracellular domain of a single receptor fused to an Fc molecule can effectively neutr
Externí odkaz:
https://doaj.org/article/0b41a10071f446298a7ec2b0eff0ed7a
Autor:
Erich J Goebel, Luisina Ongaro, Emily C Kappes, Kylie Vestal, Elitza Belcheva, Roselyne Castonguay, Ravindra Kumar, Daniel J Bernard, Thomas B Thompson
Publikováno v:
eLife, Vol 11 (2022)
Activin ligands are formed from two disulfide-linked inhibin β (Inhβ) subunit chains. They exist as homodimeric proteins, as in the case of activin A (ActA; InhβA/InhβA) or activin C (ActC; InhβC/InhβC), or as heterodimers, as with activin AC (
Externí odkaz:
https://doaj.org/article/45502bd4407a4075bf81ff99f93c4015
Autor:
Senem Aykul, Richard A Corpina, Erich J Goebel, Camille J Cunanan, Alexandra Dimitriou, Hyon Jong Kim, Qian Zhang, Ashique Rafique, Raymond Leidich, Xin Wang, Joyce McClain, Johanna Jimenez, Kalyan C Nannuru, Nyanza J Rothman, John B Lees-Shepard, Erik Martinez-Hackert, Andrew J Murphy, Thomas B Thompson, Aris N Economides, Vincent Idone
Publikováno v:
eLife, Vol 9 (2020)
Activin A functions in BMP signaling in two ways: it either engages ACVR1B to activate Smad2/3 signaling or binds ACVR1 to form a non-signaling complex (NSC). Although the former property has been studied extensively, the roles of the NSC remain unex
Externí odkaz:
https://doaj.org/article/f046d1441e0d4e23a1f1b1baf6223516
Publikováno v:
Biochem J
Growth differentiation factor 8 (GDF8), a.k.a. myostatin, is a member of the larger TGFβ superfamily of signaling ligands. GDF8 has been well characterized as a negative regulator of muscle mass. After synthesis, GDF8 is held latent by a noncovalent
Autor:
Erich J Goebel, Luisina Ongaro, Emily C Kappes, Kylie Vestal, Elitza Belcheva, Roselyne Castonguay, Ravindra Kumar, Daniel J Bernard, Thomas B Thompson
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a387e1d0e3e56a03978a63763bf95f62
https://doi.org/10.7554/elife.78197.sa2
https://doi.org/10.7554/elife.78197.sa2
Autor:
Ryan G. Walker, John A. Tainer, Robert J. Linhardt, Chandramohan Kattamuri, Erich J Goebel, Thomas B. Thompson, Michal Hammel, Fuming Zhang
Publikováno v:
Exp Biol Med (Maywood)
Experimental biology and medicine (Maywood, N.J.), vol 246, iss 4
Experimental biology and medicine (Maywood, N.J.), vol 246, iss 4
Heparin and heparan sulfate (HS) are highly sulfated polysaccharides covalently bound to cell surface proteins, which directly interact with many extracellular proteins, including the transforming growth factor-β (TGFβ) family ligand antagonist, fo
Autor:
Erich J. Goebel, Luisina Ongaro, Emily Kappes, Elitza Belcheva, Roselyne Castonguay, Ravindra Kumar, Daniel J Bernard, Thomas B. Thompson
Activin ligands are formed from two disulfide-linked inhibin β subunit chains. They exist as homodimeric proteins, as in the case of activin A (ActA; InhβA/InhβA) or activin C (ActC; InhβC/InhβC), or as heterodimers, as with activin AC (ActAC; I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56b73316f112d886666371bff48e2245
https://doi.org/10.1101/2022.03.16.484571
https://doi.org/10.1101/2022.03.16.484571
Autor:
Erich J. Goebel, Chandramohan Kattamuri, Gregory R. Gipson, Lavanya Krishnan, Moises Chavez, Magdalena Czepnik, Michelle C. Maguire, Rosa Grenha, Maria Håkansson, Derek T. Logan, Asya V. Grinberg, Dianne Sako, Roselyne Castonguay, Ravindra Kumar, Thomas B. Thompson
Publikováno v:
iScience
iScience, Vol 25, Iss 1, Pp 103590-(2022)
iScience, Vol 25, Iss 1, Pp 103590-(2022)
Summary The 30+ unique ligands of the TGFβ family signal by forming complexes using different combinations of type I and type II receptors. Therapeutically, the extracellular domain of a single receptor fused to an Fc molecule can effectively neutra
Autor:
Magdalena Czepnik, Jason C. McCoy, Erich J Goebel, Kelly L. Walton, Miook Cho, Craig A. Harrison, Gauthier Schang, Amy J. Wagers, Erik Martinez-Hackert, Ryan G. Walker, Daniel J. Bernard, Andrew P. Hinck, Senem Aykul, Juhyun Oh, Thomas B. Thompson, Ana Vujic, Richard T. Lee
Publikováno v:
BMC Biology
Background Growth/differentiation factor 8 (GDF8) and GDF11 are two highly similar members of the transforming growth factor β (TGFβ) family. While GDF8 has been recognized as a negative regulator of muscle growth and differentiation, there are con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1297a842fc51892500d150836c2c8b13