Pharmacogenomics of GH-Induced Catch-Up Growth in Prepubertal Short Children. The Role of the Exon 3-Deleted/Full-Length Growth Hormone Receptor Polymorphism

2011 ◽  
pp. 917-933
Author(s):  
Antonio Carrascosa ◽  
Laura Audí
Keyword(s):  
Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Full Length ◽  
Length Growth ◽  
Short Children ◽  
Catch Up ◽  
Receptor Polymorphism

scholarly journals The Distribution of Exon 3-Deleted/Full-Length Growth Hormone Receptor Polymorphism in the Turkish Population

2011 ◽  
Vol 3 (3) ◽  
pp. 126-131 ◽  
Author(s):  
Firdevs Baş ◽  
Fatih Keleşoğlu ◽  
Özlem Timirci ◽  
Sema Kabataş Eryılmaz ◽  
Banu Küçükemre Aydın ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Turkish Population ◽  
Full Length ◽  
Length Growth ◽  
Receptor Polymorphism

scholarly journals Activation of Chimeric and Full-length Growth Hormone Receptors by Growth Hormone Receptor Monoclonal Antibodies

1998 ◽  
Vol 273 (9) ◽  
pp. 5307-5314 ◽  
Author(s):  
Scott W. Rowlinson ◽  
Stuart N. Behncken ◽  
Jennifer E. Rowland ◽  
Richard W. Clarkson ◽  
Christian J. Strasburger ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Monoclonal Antibodies ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Hormone Receptors ◽  
Full Length ◽  
Length Growth ◽  
Growth Hormone Receptors

scholarly journals Order and disorder—An integrative structure of the full-length human growth hormone receptor

2021 ◽  
Vol 7 (27) ◽  
pp. eabh3805
Author(s):  
Noah Kassem ◽  
Raul Araya-Secchi ◽  
Katrine Bugge ◽  
Abigail Barclay ◽  
Helena Steinocher ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Lipid Membrane ◽  
Human Growth ◽  
Full Length ◽  
Saxs Data ◽  
X Ray ◽  
Human Growth Hormone Receptor

Because of its small size (70 kilodalton) and large content of structural disorder (>50%), the human growth hormone receptor (hGHR) falls between the cracks of conventional high-resolution structural biology methods. Here, we study the structure of the full-length hGHR in nanodiscs with small-angle x-ray scattering (SAXS) as the foundation. We develop an approach that combines SAXS, x-ray diffraction, and NMR spectroscopy data obtained on individual domains and integrate these through molecular dynamics simulations to interpret SAXS data on the full-length hGHR in nanodiscs. The hGHR domains reorient freely, resulting in a broad structural ensemble, emphasizing the need to take an ensemble view on signaling of relevance to disease states. The structure provides the first experimental model of any full-length cytokine receptor in a lipid membrane and exemplifies how integrating experimental data from several techniques computationally may access structures of membrane proteins with long, disordered regions, a widespread phenomenon in biology.

scholarly journals Mutations of the Growth Hormone Receptor Found in Japanese Short Children.

2001 ◽  
Vol 10 (1) ◽  
pp. 75-87
Author(s):  
Keiji Iida ◽  
Yutaka Takahashi ◽  
Hidesuke Kaji ◽  
Kazuo Chihara
Keyword(s):  
Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Short Children
Sign in / Sign up

Export Citation Format

Share Document