Faculty Opinions recommendation of Sequence and structural conservation in RNA ribose zippers.

2013 ◽  
Author(s):  
Luc Jaeger
Keyword(s):  
Structural Conservation

scholarly journals Mosaic evolution of prepropancreatic polypeptide. II. Structural conservation and divergence in pancreatic polypeptide gene.

1988 ◽  
Vol 263 (6) ◽  
pp. 2990-2997
Author(s):  
H Yonekura ◽  
K Nata ◽  
T Watanabe ◽  
Y Kurashina ◽  
H Yamamoto ◽  
...  
Keyword(s):  
Pancreatic Polypeptide ◽  
Structural Conservation ◽  
Mosaic Evolution

scholarly journals Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition

2019 ◽  
Vol 20 (8) ◽  
pp. 1996 ◽  
Author(s):  
Katharine A. Michie ◽  
Adam Bermeister ◽  
Neil O. Robertson ◽  
Sophia C. Goodchild ◽  
Paul M. G. Curmi
Keyword(s):  
Actin Cytoskeleton ◽  
Protein Complexes ◽  
Membrane Vesicle ◽  
Contact Inhibition ◽  
Cell Junctions ◽  
Cellular Membranes ◽  
Membrane Structures ◽  
Cortical Actin ◽  
Erm Proteins ◽  
Structural Conservation

The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell–cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in the formation and maintenance of specialized plasma membrane structures and membrane vesicle structures. These two protein families share a common evolutionary history, having arisen and separated via gene duplication near the origin of metazoa. During approximately 0.5 billion years of evolution, the merlin and ERM family proteins have maintained both sequence and structural conservation to an extraordinary level. Comparing crystal structures of merlin-ERM proteins and their complexes, a picture emerges of the merlin-ERM proteins acting as switchable interaction hubs, assembling protein complexes on cellular membranes and linking them to the actin cytoskeleton. Given the high level of structural conservation between the merlin and ERM family proteins we speculate that they may function together.

Structural conservation of the short α-helix in modified higher and lower polarity water solutions

RSC Advances ◽  
2015 ◽  
Vol 5 (13) ◽  
pp. 9627-9634 ◽  
Author(s):  
Hao Shen ◽  
Wei Cheng ◽  
Feng-Shou Zhang
Keyword(s):  
Water Molecules ◽  
Water Solutions ◽  
Structural Conservation ◽  
Α Helix

Which conformation is preferred when the polarity of water molecules is scaled by EP = ELJ + S2EC?

scholarly journals Structural Conservation and Effects of Alterations in T Cell Receptor Transmembrane Interfaces

2018 ◽  
Vol 114 (5) ◽  
pp. 1030-1035 ◽  
Author(s):  
Soohyung Park ◽  
Logesvaran Krshnan ◽  
Melissa J. Call ◽  
Matthew E. Call ◽  
Wonpil Im
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Structural Conservation

scholarly journals Genetic Diversity of Near Genome-Wide Hepatitis C Virus Sequences during Chronic Infection: Evidence for Protein Structural Conservation Over Time

PLoS ONE ◽  
2011 ◽  
Vol 6 (5) ◽  
pp. e19562 ◽  
Author(s):  
Hui Li ◽  
Austin L. Hughes ◽  
Nazneen Bano ◽  
Susan McArdle ◽  
Stephen Livingston ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Chronic Infection ◽  
Genome Wide ◽  
Structural Conservation ◽  
Over Time

scholarly journals Sequence variation and structural conservation in the D-loop region and flanking genes of mitochondrial DNA from Japanese pond frogs.

2000 ◽  
Vol 75 (2) ◽  
pp. 79-92 ◽  
Author(s):  
Masayuki Sumida ◽  
Hideki Kaneda ◽  
Yoji Kato ◽  
Yasushi Kanamori ◽  
Hiromichi Yonekawa ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Sequence Variation ◽  
Loop Region ◽  
D Loop ◽  
Structural Conservation

scholarly journals The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain

2014 ◽  
Vol 70 (8) ◽  
pp. 1022-1026 ◽  
Author(s):  
Francois-Xavier Chauviac ◽  
Giles Robertson ◽  
Doris H. X. Quay ◽  
Claire Bagnéris ◽  
Christian Dumas ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Catalytic Domain ◽  
Anomalous Scattering ◽  
Molecular Replacement ◽  
Catalytic Domains ◽  
Domain Composition ◽  
Resuscitation Promoting Factors ◽  
Structural Conservation ◽  
High Degree ◽  
Very High

The first structure of the catalytic domain of RpfC (Rv1884), one of the resuscitation-promoting factors (RPFs) fromMycobacterium tuberculosis, is reported. The structure was solved using molecular replacement once the space group had been correctly identified as twinnedP21rather than the apparentC2221by searching for anomalous scattering sites inP1. The structure displays a very high degree of structural conservation with the previously published structures of the catalytic domains of RpfB (Rv1009) and RpfE (Rv2450). This structural conservation highlights the importance of the versatile domain composition of the RPF family.

scholarly journals Structural Conservation of Ligand Binding Reveals a Bile Acid-like Signaling Pathway in Nematodes

2011 ◽  
Vol 287 (7) ◽  
pp. 4894-4903 ◽  
Author(s):  
Xiaoyong Zhi ◽  
X. Edward Zhou ◽  
Karsten Melcher ◽  
Daniel L. Motola ◽  
Verena Gelmedin ◽  
...  
Keyword(s):  
Bile Acid ◽  
Ligand Binding ◽  
Signaling Pathway ◽  
Structural Conservation
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