TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, No. 17, Issue of April 23, pp. 12163–12170, 1999 © 1999 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. THEIR COMMON AND DISTINCT PROPERTIES* (Received for publication, December 16, 1998, and in revised form, January 28, 1999) Norihisa Masuyama‡, Hiroshi Hanafusa‡, Morioh Kusakabe‡, Hiroshi Shibuya§, and Eisuke Nishida‡ From the ‡Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502 and the §Division of Morphogenesis, Department of Developmental Biology, National Institute for Basic Biology, Okazaki 444- 8585, Japan Smad family proteins have been identified as media- which is not a direct substrate of receptors but participates in tors of intracellular signal transduction by the trans- signaling by associating with pathway-restricted Smads. The forming growth factor-b (TGF-b) superfamily. Each third subtype consists of those Smads that inhibit the activa- member of the pathway-restricted, receptor-activated tion of pathway-restricted Smads and are referred to as anti- Smad family cooperates and synergizes with Smad4, Smads (6 – 8). called co-Smad, to transduce the signals. Only Smad4 Pathway-restricted Smads contain a consensus phosphoryl- has been shown able to function as a common partner of ation motif, SS(V/M)S, for the type 
TI - Identification of Two Smad4 Proteins in Xenopus
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.274.17.12163
DA - 1999-04-01
UR - https://www.deepdyve.com/lp/unpaywall/identification-of-two-smad4-proteins-in-xenopus-G34u82DoRo
DP - DeepDyve
ER -