scholarly journals Atomic dynamic functional interaction patterns for characterization of ADHD

2014 ◽  
Vol 35 (10) ◽  
pp. 5262-5278 ◽  
Author(s):  
Jinli Ou ◽  
Zhichao Lian ◽  
Li Xie ◽  
Xiang Li ◽  
Peng Wang ◽  
...  
Keyword(s):  
Interaction Patterns ◽  
Functional Interaction ◽  
Atomic Dynamic

scholarly journals RBP-L, a transcription factor related to RBP-Jkappa.

1997 ◽  
Vol 17 (5) ◽  
pp. 2679-2687 ◽  
Author(s):  
S Minoguchi ◽  
Y Taniguchi ◽  
H Kato ◽  
T Okazaki ◽  
L J Strobl ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Notch Receptor ◽  
In Vitro Assays ◽  
Functional Interaction ◽  
Protein Protein Interaction ◽  
Isolation And Characterization ◽  
Signalling Molecule

RBP-Jkappa is a sequence-specific DNA binding protein which plays a central role in signalling downstream of the Notch receptor by physically interacting with its intracellular region. Although at least four Notch genes exist in mammals, it is unknown whether each Notch requires a specific downstream signalling molecule. Here we report isolation and characterization of a mouse RBP-Jkappa-related gene named RBP-L that is expressed almost exclusively in lung, in contrast to the ubiquitous expression of RBP-Jkappa. For simplicity, we propose to call RBP-Jkappa RBP-J. The RBP-L protein bound to a DNA sequence almost identical to that of RBP-J. Surprisingly, RBP-L did not interact with any of the known four mouse Notch proteins. Although we found that RBP-L and EBNA-2 cooperated in transcriptional activation, they did not show significantly strong protein-protein interaction that can be detected by several in vivo and in vitro assays. This is again in contrast to physical association of RBP-J with EBNA-2. Several models to explain functional interaction between RBP-L and EBNA-2 are discussed.

Biochemical Characterization of the WRN−FEN-1 Functional Interaction

Biochemistry ◽  
2002 ◽  
Vol 41 (40) ◽  
pp. 12204-12216 ◽  
Author(s):  
Robert M. Brosh, ◽  
Henry C. Driscoll ◽  
Grigory L. Dianov ◽  
Joshua A. Sommers
Keyword(s):  
Biochemical Characterization ◽  
Functional Interaction

scholarly journals Characterization of cytoskeletal protein 4.1R interaction with NHE1 (Na+/H+ exchanger isoform 1)

2012 ◽  
Vol 446 (3) ◽  
pp. 427-435 ◽  
Author(s):  
Wataru Nunomura ◽  
Sheryl P. Denker ◽  
Diane L. Barber ◽  
Yuichi Takakuwa ◽  
Philippe Gascard
Keyword(s):  
Amino Acids ◽  
Protein Interaction ◽  
Cytoskeletal Protein ◽  
Functional Interaction ◽  
Ferm Domain ◽  
Protein Protein Interaction ◽  
Nhe1 Activity ◽  
Acidic Conditions ◽  
Protein 4.1R

NHE1 (Na+/H+ exchanger isoform 1) has been reported to be hyperactive in 4.1R-null erythrocytes [Rivera, De Franceschi, Peters, Gascard, Mohandas and Brugnara (2006) Am. J. Physiol. Cell Physiol. 291, C880–C886], supporting a functional interaction between NHE1 and 4.1R. In the present paper we demonstrate that 4.1R binds directly to the NHE1cd (cytoplasmic domain of NHE1) through the interaction of an EED motif in the 4.1R FERM (4.1/ezrin/radixin/moesin) domain with two clusters of basic amino acids in the NHE1cd, K519R and R556FNKKYVKK, previously shown to mediate PIP2 (phosphatidylinositol 4,5-bisphosphate) binding [Aharonovitz, Zaun, Balla, York, Orlowski and Grinstein (2000) J. Cell. Biol. 150, 213–224]. The affinity of this interaction (Kd=100–200 nM) is reduced in hypertonic and acidic conditions, demonstrating that this interaction is of an electrostatic nature. The binding affinity is also reduced upon binding of Ca2+/CaM (Ca2+-saturated calmodulin) to the 4.1R FERM domain. We propose that 4.1R regulates NHE1 activity through a direct protein–protein interaction that can be modulated by intracellular pH and Na+ and Ca2+ concentrations.

scholarly journals Comparison of Structural Architecture of HCV NS3 Genotype 1 versus Pakistani Genotype 3a

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Kaneez Fatima ◽  
Esam Azhar ◽  
Shilu Mathew ◽  
Ghazi Damanhouri ◽  
Ishtiaq Qadri
Keyword(s):  
Amino Acids ◽  
Structural Characterization ◽  
Antiviral Agents ◽  
Interaction Patterns ◽  
Genotype 1 ◽  
Genome Variability ◽  
Structural Architecture ◽  
Genotype 3A

This study described the structural characterization of Pakistani HCV NS3 GT3a in parallel with genotypes 1a and 1b NS3. We investigated the role of amino acids and their interaction patterns in different HCV genotypes by crystallographic modeling. Different softwares were used to study the interaction pattern, for example, CLCBIO sequence viewer, MODELLER, NMRCLUST, ERRAT score, and MODELLER. Sixty models were produced and clustered into groups and the best model of PK-NCVI/Pk3a NS3 was selected and studied further to check the variability with other HCV NS3 genotypes. This study will help in future to understand the structural architecture of HCV genome variability and to further define the conserved targets for antiviral agents.

scholarly journals Inferring consistent functional interaction patterns from natural stimulus FMRI data

NeuroImage ◽  
2012 ◽  
Vol 61 (4) ◽  
pp. 987-999 ◽  
Author(s):  
Jiehuan Sun ◽  
Xintao Hu ◽  
Xiu Huang ◽  
Yang Liu ◽  
Kaiming Li ◽  
...  
Keyword(s):  
Fmri Data ◽  
Interaction Patterns ◽  
Functional Interaction ◽  
Natural Stimulus
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