M. Wada

Tyrosine phosphorylation of the EGF receptor by the kinase Jak2 is induced by growth hormone

Kohjiro Ueki, Masaru Honjo, Takashi Kadowaki, 1997, Nature.

The full agonistic effect of recombinant 20 kDa human growth hormone (hGH) on CHO cells stably transfected with hGH receptor cDNA

Y. Takahashi, M. Takahashi, K. Chang, 1997, Molecular and Cellular Endocrinology.

Growth hormone-induced tyrosine phosphorylation of EGF receptor as an essential element leading to MAP kinase activation and gene expression.

Y. Yazaki, I. Komuro, T. Kadowaki, 1998, Endocrine journal.

GH induced lipolysis stimulation in 3T3-L1 adipocytes stably expressing hGHR: analysis on signaling pathway and activity of 20K hGH

Y. Takahashi, M. Wada, M. Honjo, 2000, Molecular and Cellular Endocrinology.

The 20-kilodalton (kDa) human growth hormone (hGH) differs from the 22-kDa hGH in the effect on the human prolactin receptor.

M. Wada, M. Honjo, M. Ikeda, 1999, Endocrinology.

A novel specific bioassay for serum human growth hormone.

R. Horikawa, N. Katsumata, O. Arisaka, 2000, The Journal of clinical endocrinology and metabolism.

Cellular Activities of 20K- and 22K-hGH Do Not Necessarily Correlate with Their Binding Affinities for Rat GH Receptor

K. Matsumoto, M. Wada, M. Honjo, 2001, Hormone Research in Paediatrics.

A novel bioassay based on human growth hormone (hGH) receptor mediated cell proliferation: measurement of 20K-hGH and its modified forms.

S. Takahashi, M. Wada, M. Honjo, 2000, Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society.

Secretion of authentic 20-kDa human growth hormone (20K hGH) in Escherichia coli and properties of the purified product.

K. Nakashima, N. Kusuhara, H. Kobayashi, 1997, Journal of biotechnology.

The 20-kilodalton (kDa) human growth hormone (hGH) differs from the 22-kDa hGH in the complex formation with cell surface hGH receptor and hGH-binding protein circulating in human plasma.

M. Wada, M. Honjo, S. Banba, 1998, Molecular endocrinology.

Reversible dimerization of 20 kilodalton human growth hormone (hGH).

N. Kusuhara, H. Kobayashi, K. Mabuchi, 2000, Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society.

The Binding between the Stem Regions of Human Growth Hormone (GH) Receptor Compensates for the Weaker Site 1 Binding of 20-kDa Human GH (hGH) than That of 22-kDa hGH*

M. Wada, M. Honjo, S. Banba, 2000, The Journal of Biological Chemistry.

Analysis of binding properties between 20 kDa human growth hormone (hGH) and hGH receptor (hGHR): the binding affinity for hGHR extracellular domain and mode of receptor dimerization.

K. Matsumoto, M. Wada, M. Honjo, 1999, Journal of Molecular Endocrinology.