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Shank3-mutant mice lacking exon 9 show altered excitation/inhibition balance, enhanced rearing, and spatial memory deficit
It is suggested that ankyrin repeat-containing Shank3 splice variants are important for E/I balance, rearing behavior, and spatial memory.
De Novo Mutations in the Motor Domain of KIF1A Cause Cognitive Impairment, Spastic Paraparesis, Axonal Neuropathy, and Cerebellar Atrophy
It is indicated that de novo missense mutations in the MD of KIF1A cause a phenotype that overlaps with, while being more severe, than that associated with recessive mutation in the same gene.
Dominant transmission of de novo KIF1A motor domain variant underlying pure spastic paraplegia
- E. Ylikallio, Doyoun Kim, H. Tyynismaa
- Medicine, PsychologyEuropean Journal of Human Genetics
- 14 January 2015
It is concluded that KIF1A should be considered a candidate gene for hereditary paraplegias regardless of inheritance pattern and the spectrum of phenotypes caused by heterozygous Kif1A motor domain variants to include pure spastic paraplegia is expanded.
Therapeutic Strategies Against COVID-19 and Structural Characterization of SARS-CoV-2: A Review
- Gi Uk Jeong, H. Song, G. Yoon, Doyoun Kim, Young-Chan Kwon
- Biology, ChemistryFrontiers in Microbiology
- 14 July 2020
The novel coronavirus, SARS-CoV-2, or 2019-nCoV, which originated in Wuhan, Hubei province, China in December 2019, is a grave threat to public health worldwide. A total of 3,672,238 confirmed cases…
The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNA
- S. Ha, Doyoun Kim, H. Hwang, A. Rich, Yang‐Gyun Kim, K. Kim
- Biology, ChemistryProceedings of the National Academy of Sciences
- 30 December 2008
This article reveals that hZβDAI has a similar fold to that of other ZBDs, but adopts an unusual binding mode for recognition of Z-DNA, and suggests that binding 2 DAIs to 1 dsDNA brings about dimerization of DAI that might facilitate DNA-mediated innate immune activation.
Intrinsic Z-DNA is stabilized by the conformational selection mechanism of Z-DNA-binding proteins.
- S. Bae, Doyoun Kim, K. Kim, Yang‐Gyun Kim, S. Hohng
- Biology, ChemistryJournal of the American Chemical Society
- 2 February 2011
The results reveal that intrinsic Z-DNAs are dynamically formed and effectively stabilized by Z-DNA-binding proteins through efficient trapping of the Z conformation rather than being actively induced by them.
Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion.
A model in which Slitrks mediate synaptogenic functions through direct binding to LAR-RPTPs and the subsequent lateral assembly of LAR- RPTPs/SlitrKS complexes is proposed.
Distinct Z-DNA binding mode of a PKR-like protein kinase containing a Z-DNA binding domain (PKZ)
It is concluded that the positive charge in the β-wing largely affects fast B-to-Z transition activity by enhancing the DNA binding rate.
SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development
It is suggested that postsynaptic SALM5 promotes synapse development by trans-synaptically interacting with presynaptic LAR-RPTPs and is important for the regulation of excitatory synaptic strength.
SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3–LAR adhesion
It is reported that SALM4, a member of the SALM/Lrfn family of synaptic adhesion molecules, suppresses excitatory synapse development through cis inhibition of SALM3, another SALM family protein with synaptogenic activity.