Interaction Domains as Cooperative Phenomena in SmCo 2:17 Magnets

2006 ◽  
Author(s):  
K. Mueller ◽  
O. Gutfleisch ◽  
K. Khlopkov ◽  
R. Schaefer ◽  
L. Schultz
Keyword(s):  
Cooperative Phenomena ◽  
Interaction Domains

Protein Interaction Domains and Post-Translational Modifications: Structural Features and Drug Discovery Applications

2020 ◽  
Vol 27 (37) ◽  
pp. 6306-6355 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Drug Discovery ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Structural Information ◽  
Protein Complexes ◽  
Structural Features ◽  
Protein Protein Interactions ◽  
Modular Architecture ◽  
Post Translational Modifications ◽  
Interaction Domains

Background:: Many pathways regarding healthy cells and/or linked to diseases onset and progression depend on large assemblies including multi-protein complexes. Protein-protein interactions may occur through a vast array of modules known as protein interaction domains (PIDs). Objective:: This review concerns with PIDs recognizing post-translationally modified peptide sequences and intends to provide the scientific community with state of art knowledge on their 3D structures, binding topologies and potential applications in the drug discovery field. Method:: Several databases, such as the Pfam (Protein family), the SMART (Simple Modular Architecture Research Tool) and the PDB (Protein Data Bank), were searched to look for different domain families and gain structural information on protein complexes in which particular PIDs are involved. Recent literature on PIDs and related drug discovery campaigns was retrieved through Pubmed and analyzed. Results and Conclusion:: PIDs are rather versatile as concerning their binding preferences. Many of them recognize specifically only determined amino acid stretches with post-translational modifications, a few others are able to interact with several post-translationally modified sequences or with unmodified ones. Many PIDs can be linked to different diseases including cancer. The tremendous amount of available structural data led to the structure-based design of several molecules targeting protein-protein interactions mediated by PIDs, including peptides, peptidomimetics and small compounds. More studies are needed to fully role out, among different families, PIDs that can be considered reliable therapeutic targets, however, attacking PIDs rather than catalytic domains of a particular protein may represent a route to obtain selective inhibitors.

Phase transformation and Raman spectra in BaTiO3 nanocrystals

2002 ◽  
Vol 718 ◽  
Author(s):  
Jian Yu ◽  
X. J. Meng ◽  
J.L. Sun ◽  
G.S. Wang ◽  
J.H. Chu
Keyword(s):  
Particle Size ◽  
Phase Transformation ◽  
Low Temperature ◽  
Long Range ◽  
Lattice Expansion ◽  
Inversion Symmetry ◽  
Range Interaction ◽  
Cooperative Phenomena ◽  
Long Range Interaction ◽  
Hydrothermal Methods

AbstractIn this paper, size-induced ferroelectricit yweakening, phase transformation, and anomalous lattice expansion are observed in nanocrystalline BaTiO3 (nc-BaTiO3) deriv ed b y low temperature hydrothermal methods, and they are w ellunderstood using the terms of the long-range interaction and its cooperative phenomena altered by particle size in covalen t ionic nanocrystals. In cubic nc-BaTiO3, five modes centerd at 186, 254, 308, 512 and 716 cm-1 are observed Raman active in cubic nanophase, and they are attributed to local rhombohedral distortion breaking inversion-symmetry in cubic nanophase. The254 and 308 cm-1 modes are significantly affected not only by the concentration of hydroxyl defects, but also their particular configuration. And the 806 cm-1 modes found to be closely associated with OH - absorbed on grain boundaries.

scholarly journals Structural and Functional Integration of the PLCγ Interaction Domains Critical for Regulatory Mechanisms and Signaling Deregulation

Structure ◽  
2012 ◽  
Vol 20 (12) ◽  
pp. 2062-2075 ◽  
Author(s):  
Tom D. Bunney ◽  
Diego Esposito ◽  
Corine Mas-Droux ◽  
Ekatarina Lamber ◽  
Rhona W. Baxendale ◽  
...  
Keyword(s):  
Functional Integration ◽  
Regulatory Mechanisms ◽  
Interaction Domains

Evaluation of web reinforcements in prestressed concrete box girders through shear-transverse bending domains

2020 ◽  
pp. 136943322098170
Author(s):  
Michele Fabio Granata ◽  
Antonino Recupero
Keyword(s):  
Analytical Model ◽  
Prestressed Concrete ◽  
3D Analysis ◽  
Box Girders ◽  
Element Analysis ◽  
Cross Sectional ◽  
Interaction Domains ◽  
Global And Local ◽  
Resultant Forces

In concrete box girders, the amount and distribution of reinforcements in the webs have to be estimated considering the local effects due to eccentric external loads and cross-sectional distortion and not only the global effect due to the resultant forces of a longitudinal analysis: shear, torsion and bending. This work presents an analytical model that allows designers to take into account the interaction of all these effects, global and local, for the determination of the reinforcements. The model is based on the theory of stress fields and it has been compared to a 3D finite element analysis, in order to validate the interaction domains. The results show how the proposed analytical model allows an easy and reliable reinforcement evaluation, in agreement with a more refined 3D analysis but with a reduced computational burden.

scholarly journals Mutations and Protein Interaction Landscape Reveal Key Cellular Events Perturbed in Upper Motor Neurons with HSP and PLS

2021 ◽  
Vol 11 (5) ◽  
pp. 578
Author(s):  
Oge Gozutok ◽  
Benjamin Ryan Helmold ◽  
P. Hande Ozdinler
Keyword(s):  
Motor Neurons ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Cortical Neurons ◽  
Therapeutic Interventions ◽  
Functional Identification ◽  
Protein Protein Interaction ◽  
Cellular Events ◽  
Interaction Domains ◽  
Upper Motor Neurons

Hereditary spastic paraplegia (HSP) and primary lateral sclerosis (PLS) are rare motor neuron diseases, which affect mostly the upper motor neurons (UMNs) in patients. The UMNs display early vulnerability and progressive degeneration, while other cortical neurons mostly remain functional. Identification of numerous mutations either directly linked or associated with HSP and PLS begins to reveal the genetic component of UMN diseases. Since each of these mutations are identified on genes that code for a protein, and because cellular functions mostly depend on protein-protein interactions, we hypothesized that the mutations detected in patients and the alterations in protein interaction domains would hold the key to unravel the underlying causes of their vulnerability. In an effort to bring a mechanistic insight, we utilized computational analyses to identify interaction partners of proteins and developed the protein-protein interaction landscape with respect to HSP and PLS. Protein-protein interaction domains, upstream regulators and canonical pathways begin to highlight key cellular events. Here we report that proteins involved in maintaining lipid homeostasis and cytoarchitectural dynamics and their interactions are of great importance for UMN health and stability. Their perturbation may result in neuronal vulnerability, and thus maintaining their balance could offer therapeutic interventions.

scholarly journals Novel Roles of SH2 and SH3 Domains in Lipid Binding

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1191
Author(s):  
Szabolcs Sipeki ◽  
Kitti Koprivanacz ◽  
Tamás Takács ◽  
Anita Kurilla ◽  
Loretta László ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Specific Protein ◽  
Lipid Binding ◽  
Sh2 Domain ◽  
Essential Property ◽  
Cellular Regulation ◽  
Sh3 Domains ◽  
Protein Partners ◽  
Interaction Domains ◽  
Central Paradigm

Signal transduction, the ability of cells to perceive information from the surroundings and alter behavior in response, is an essential property of life. Studies on tyrosine kinase action fundamentally changed our concept of cellular regulation. The induced assembly of subcellular hubs via the recognition of local protein or lipid modifications by modular protein interactions is now a central paradigm in signaling. Such molecular interactions are mediated by specific protein interaction domains. The first such domain identified was the SH2 domain, which was postulated to be a reader capable of finding and binding protein partners displaying phosphorylated tyrosine side chains. The SH3 domain was found to be involved in the formation of stable protein sub-complexes by constitutively attaching to proline-rich surfaces on its binding partners. The SH2 and SH3 domains have thus served as the prototypes for a diverse collection of interaction domains that recognize not only proteins but also lipids, nucleic acids, and small molecules. It has also been found that particular SH2 and SH3 domains themselves might also bind to and rely on lipids to modulate complex assembly. Some lipid-binding properties of SH2 and SH3 domains are reviewed here.

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