Results 181 to 190 of about 9,732 (196)
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Two rice MADS domain proteins interact with OsMADS1
Plant Molecular Biology, 2000OsMADS1 is a MADS box gene controlling flower development in rice. In order to learn more about the function of OsMADS1, we searched for cellular proteins interacting with OsMADS1 employing the yeast two-hybrid system. Two novel proteins with MADS domains, which were named OsMADS14 and OsMADS15, were isolated from a rice cDNA library.
Lim, J, Moon, YH, An, G, Jang, SK
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Gene, 2005
MIKC-type proteins represent a class of MADS-domain transcription factors and are defined by a unique domain structure: in addition to the highly conserved DNA-binding MADS-domain, they have three other domains ('I', 'K' and 'C'), with the keratin-like K-domain being the most highly conserved and characteristic one.
Kerstin Kaufmann +2 more
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MIKC-type proteins represent a class of MADS-domain transcription factors and are defined by a unique domain structure: in addition to the highly conserved DNA-binding MADS-domain, they have three other domains ('I', 'K' and 'C'), with the keratin-like K-domain being the most highly conserved and characteristic one.
Kerstin Kaufmann +2 more
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MADS domain proteins in plant development.
Biological chemistry, 1997© 1997 Walter de Gruyter GmbH.
Riechmann, José Luis +1 more
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Plant Cell, 1996 MADS domain proteins are members of a highly conserved family found in all eukaryotes. Genetic studies clearly indicate that many plant MADS domain proteins have different regulatory functions in flower development, yet they share a highly conserved DNA binding domain and can bind to very similar sequences.
H, Huang +5 more
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PFMAGO, a MAGO NASHI-Like Factor, Interacts with the MADS-Domain Protein MPF2 from Physalis floridana [PDF]
Molecular Biology and Evolution, 2007 MADS-domain proteins serve as regulators of plant development and often form dimers and higher order complexes to function. Heterotopic expression of MPF2, a MADS-box gene, in reproductive tissues is a key component in the evolution of the inflated calyx syndrome in Physalis, but RNAi studies demonstrate that MPF2 has also acquired a role in male ...
Chaoying He +2 more
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Biochemical and Biophysical Research Communications, 2008
We are interested in identifying proteins that interact with the MADS domain protein NMH7 of Medicago sativa. We use an affinity column with a synthetic peptide derived from the MADS domain of NMH7 which has been reported to mediate protein-protein interaction with non-MADS domain interacting proteins.
Julio Páez Valencia +2 more
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We are interested in identifying proteins that interact with the MADS domain protein NMH7 of Medicago sativa. We use an affinity column with a synthetic peptide derived from the MADS domain of NMH7 which has been reported to mediate protein-protein interaction with non-MADS domain interacting proteins.
Julio Páez Valencia +2 more
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The MADS-domain protein AGAMOUS-like 15 accumulates in embryonic tissues with diverse origins.
Plant physiology, 1999AGL15 (AGAMOUS-like 15), a member of the MADS-domain family of regulatory factors, accumulates preferentially in the organs and tissues derived from double fertilization in flowering plants (i.e. the embryo, suspensor, and endosperm). The developmental role of AGL15 is still undefined. If it is involved in embryogenesis rather than some other aspect of
S E, Perry, M D, Lehti, D E, Fernandez
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MADS-Domain Transcription Factors and their Accessory Proteins (TCFS)
1996Michael A. Cahill +2 more
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