The role of the secondary structure of helical poly(phenylacetylene)s in the formation of nanoparticles from polymer–metal complexes (HPMCs)

The secondary structure of chiral helical polymers forming helical polymer–metal complexes (HPMCs) plays a major role in their subsequent nanostructuration.

Download Full-text

Helical Polymer–Metal Complexes: The Role of Metal Ions on the Helicity and the Supramolecular Architecture of Poly(phenylacetylene)s

Hierarchical Macromolecular Structures: 60 Years after the Staudinger Nobel Prize II - Advances in Polymer Science ◽

10.1007/12_2013_260 ◽

2013 ◽

pp. 123-140 ◽

Cited By ~ 15

Author(s):

Felix Freire ◽

José Manuel Seco ◽

Emilio Quiñoá ◽

Ricardo Riguera

Keyword(s):

Metal Ions ◽

Metal Complexes ◽

Supramolecular Architecture ◽

Helical Polymer ◽

Polymer Metal

Download Full-text

A general route to chiral nanostructures from helical polymers: P/M switch via dynamic metal coordination

Polymer Chemistry ◽

10.1039/c7py00561j ◽

2017 ◽

Vol 8 (24) ◽

pp. 3740-3745 ◽

Cited By ~ 21

Author(s):

Sandra Arias ◽

Manuel Núñez-Martínez ◽

Emilio Quiñoá ◽

Ricardo Riguera ◽

Félix Freire

Keyword(s):

Coordination Chemistry ◽

Metal Complexes ◽

Metal Coordination ◽

Helical Polymers ◽

Helical Polymer ◽

Dynamic Coordination ◽

Polymer Metal ◽

Chiral Nanostructures

Macroscopically enantiomeric chiral nanospheres made from P or M helical polymer metal complexes can be obtained via dynamic coordination chemistry.

Download Full-text

Nanospheres with Tunable Size and Chirality from Helical Polymer–Metal Complexes

Journal of the American Chemical Society ◽

10.1021/ja3061112 ◽

2012 ◽

Vol 134 (47) ◽

pp. 19374-19383 ◽

Cited By ~ 74

Author(s):

Félix Freire ◽

José Manuel Seco ◽

Emilio Quiñoá ◽

Ricardo Riguera

Keyword(s):

Metal Complexes ◽

Helical Polymer ◽

Polymer Metal

Download Full-text

Role of Hydrophobicity on Structure of Polymer−Metal Complexes

The Journal of Physical Chemistry B ◽

10.1021/jp002310+ ◽

2001 ◽

Vol 105 (23) ◽

pp. 5368-5373 ◽

Cited By ~ 30

Author(s):

Shyni Varghese ◽

Ashish K. Lele ◽

D. Srinivas ◽

Raghunath A. Mashelkar

Keyword(s):

Metal Complexes ◽

Polymer Metal

Download Full-text

Role of metal ions in development of specific properties of polymer metal complexes

Makromolekulare Chemie Macromolecular Symposia ◽

10.1002/masy.19860040126 ◽

1986 ◽

Vol 4 (1) ◽

pp. 233-244 ◽

Cited By ~ 1

Author(s):

S.S H. Rashidova ◽

E. U. Urinov ◽

S. G. Khodjaev

Keyword(s):

Metal Ions ◽

Metal Complexes ◽

Polymer Metal

Download Full-text

RNA secondary structure dependence in METTL3–METTL14 mRNA methylation is modulated by the N-terminal domain of METTL3

Biological Chemistry ◽

10.1515/hsz-2020-0265 ◽

2020 ◽

Vol 402 (1) ◽

pp. 89-98

Author(s):

Nathalie Meiser ◽

Nicole Mench ◽

Martin Hengesbach

Keyword(s):

Secondary Structure ◽

Rna Binding ◽

Specific Protein ◽

Structure Dependence ◽

Terminal Domain ◽

Methylation Assay ◽

A Site ◽

Methylation Activity

AbstractN6-methyladenosine (m6A) is the most abundant modification in mRNA. The core of the human N6-methyltransferase complex (MTC) is formed by a heterodimer consisting of METTL3 and METTL14, which specifically catalyzes m6A formation within an RRACH sequence context. Using recombinant proteins in a site-specific methylation assay that allows determination of quantitative methylation yields, our results show that this complex methylates its target RNAs not only sequence but also secondary structure dependent. Furthermore, we demonstrate the role of specific protein domains on both RNA binding and substrate turnover, focusing on postulated RNA binding elements. Our results show that one zinc finger motif within the complex is sufficient to bind RNA, however, both zinc fingers are required for methylation activity. We show that the N-terminal domain of METTL3 alters the secondary structure dependence of methylation yields. Our results demonstrate that a cooperative effect of all RNA-binding elements in the METTL3–METTL14 complex is required for efficient catalysis, and that binding of further proteins affecting the NTD of METTL3 may regulate substrate specificity.

Download Full-text