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Bone morphogenetic proteins (BMPs) are members of the transforming growth factor-β family (TGFβ), which signal through hetero-tetrameric complexes of type I and type II receptors.
Removal of all halogen atoms from complexes [3] and [4] with AgBF4 in acetonitrile yielded dinuclear iridium III) and rhodium III) complexes of type [Cp*(MeCN 2M benzodicarbene)M(MeCN 2Cp*](BF4)2 [10](BF4)4–[11](BF4)4.
The strikingly pleiotropic effects of BMPs/OPs spring from amino acid sequence variations in the carboxy-terminal domain and in the transduction of distinct signalling pathways by individual Smad proteins after transmembrane serine/threonine kinase complexes of type I and II receptors.
The strikingly pleiotropic effects of the bone morphogenetic and osteogenic proteins (BMPs/OPs) spring from amino acid sequence variations in the carboxy-terminal domain and in the transduction of distinct signalling pathways by individual Smad proteins after transmembrane serine/threonine kinase complexes of type I and II receptors.
Reactions of metal chloride or sulfate and the sodium salt of 5-nitrosalicylic acid (5-nsa) in aqueous solution result in isomorphous complexes of type [M H2O 5 5-nsa)]+ (5-nsa)− · H2O [M H2O 5 5-nsan (2), Co (3), Ni (4)] in the solid state.
Complexation of these ligands with vanadyl(IV) sulphate leads to the formation of new oxovanadium(IV) complexes of type VIVOL.H2O.
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We have crystallised four dinuclear paddle wheel copper II) complexes of types Cu2 RCOO 4(L)2 and Cu2 RCOO) 4(S)2 Cu2(RCOO)4(L)2, which retain the Copper acetate paddle wheel geometry.
During long exposure to temperature near boiling point, some of the polymeric species (including TiOSO4, [TiO SO4 2]2−) were destroyed which encourages the formation of multinuclear complexes of types [Ti2O2(OH 3]+ and [Ti4O6(OH)3]+ [12].
As can be seen in Fig. 3, while the correspondence clusters-complexes (of type PC1) is still acceptable, the percentages of subunits detected for the complexes are drastically reduced with respect to E.coli.
Bone morphogenetic protein signals through a heteromeric complex of type I and type II transmembrane serine/threonine kinase receptors.
The receptor complex of type III IFNs is composed of the IL-10 receptor beta (IL-10Rβ) and a novel IL-28 receptor alpha (IL-28Rα).
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