scholarly journals Multiple Modulation of Acid-Sensing Ion Channel 1a by the Alkaloid Daurisoline

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 336 ◽  
Author(s):  
Dmitry I. Osmakov ◽  
Sergey G. Koshelev ◽  
Ekaterina N. Lyukmanova ◽  
Mikhail A. Shulepko ◽  
Yaroslav A. Andreev ◽  
...  
Keyword(s):  
Mathematical Model ◽  
Steady State ◽  
Binding Sites ◽  
Structure And Function ◽  
Main Peak ◽  
Activation Curve ◽  
Acid Sensing Ion Channels ◽  
Central Nervous Systems ◽  
And Function ◽  
Second Peak

Acid-sensing ion channels (ASICs) are proton-gated sodium-selective channels that are expressed in the peripheral and central nervous systems. ASIC1a is one of the most intensively studied isoforms due to its importance and wide representation in organisms, but it is still largely unexplored as a target for therapy. In this study, we demonstrated response of the ASIC1a to acidification in the presence of the daurisoline (DAU) ligand. DAU alone did not activate the channel, but in combination with protons, it produced the second peak component of the ASIC1a current. This second peak differs from the sustained component (which is induced by RF-amide peptides), as the second (DAU-induced) peak is completely desensitized, with the same kinetics as the main peak. The co-application of DAU and mambalgin-2 indicated that their binding sites do not overlap. Additionally, we found an asymmetry in the pH activation curve of the channel, which was well-described by a mathematical model based on the multiplied probabilities of protons binding with a pool of high-cooperative sites and a single proton binding with a non-cooperative site. In this model, DAU targeted the pool of high-cooperative sites and, when applied with protons, acted as an inhibitor of ASIC1a activation. Moreover, DAU’s occupation of the same binding site most probably reverses the channel from steady-state desensitization in the pH 6.9–7.3 range. DAU features disclose new opportunities in studies of ASIC structure and function.

scholarly journals The Significance of Calcium in Photosynthesis

2019 ◽  
Vol 20 (6) ◽  
pp. 1353 ◽  
Author(s):  
Quan Wang ◽  
Sha Yang ◽  
Shubo Wan ◽  
Xinguo Li
Keyword(s):  
Signal Transduction ◽  
Binding Sites ◽  
Current Knowledge ◽  
Structure And Function ◽  
Biochemical Reactions ◽  
Chloroplast Proteins ◽  
Secondary Messenger ◽  
And Function ◽  
The Relationship ◽  
Physiological And Biochemical

As a secondary messenger, calcium participates in various physiological and biochemical reactions in plants. Photosynthesis is the most extensive biosynthesis process on Earth. To date, researchers have found that some chloroplast proteins have Ca2+-binding sites, and the structure and function of some of these proteins have been discussed in detail. Although the roles of Ca2+ signal transduction related to photosynthesis have been discussed, the relationship between calcium and photosynthesis is seldom systematically summarized. In this review, we provide an overview of current knowledge of calcium’s role in photosynthesis.

State-of-the-Art Neural Networks Applications in Biology

2013 ◽  
Vol 2 (4) ◽  
pp. 63-85 ◽  
Author(s):  
Arianna Filntisi ◽  
Nikitas Papangelopoulos ◽  
Elena Bencurova ◽  
Ioannis Kasampalidis ◽  
George Matsopoulos ◽  
...  
Keyword(s):  
Neural Networks ◽  
Game Theory ◽  
State Of The Art ◽  
Disease Diagnosis ◽  
General Term ◽  
Structure And Function ◽  
Computational Method ◽  
Processing Abilities ◽  
Central Nervous Systems ◽  
And Function

Artificial neural networks (ANNs) are a well-established computational method inspired by the structure and function of biological central nervous systems. Since their conception, ANNs have been utilized in a vast variety of applications due to their impressive information processing abilities. A vibrant field, ANNs have been utilized in bioinformatics, a general term for describing the combination of informatics, biology and medicine. This article is an effort to investigate recent advances in the area of bioinformatical applications of ANNs, with emphasis in disease diagnosis, genetics, proteomics, and chemoinformatics. The combination of neural networks and game theory in some of these application is also discussed.

scholarly journals Effect of cross-linkers on the structure and function of pig-renal sodium–glucose cotransporters after papain treatment

1998 ◽  
Vol 330 (2) ◽  
pp. 733-736 ◽  
Author(s):  
Jean GIUDICELLI ◽  
Marie-France BERTRAND ◽  
Stephane BILSKI ◽  
T. Than TRAN ◽  
Jean-Claude POIREE
Keyword(s):  
Binding Sites ◽  
Specific Inhibitor ◽  
Structure And Function ◽  
Scatchard Analysis ◽  
High Affinity ◽  
Phlorizin Binding ◽  
Sodium Dependent ◽  
Spacer Arm ◽  
Molecular Masses ◽  
And Function

Kidney brush-border membranes contain two sodium-dependent glucose transporters, one with low and one with high affinity for phlorizin, the specific inhibitor of these transporters. Using Scatchard analysis of phlorizin binding and Western blotting with specific antibodies against these transporters, we demonstrate in this study that although both transporters were proteolysed by papain treatment, only the high-affinity phlorizin-binding sites were decreased. Papain treatment followed by cross-linking with homobifunctional disuccinimidyl tartarate restored only the structure of the low-affinity phlorizin-binding protein (approx. molecular mass 70 kDa) without modifying the phlorizin-binding sites. When disuccinimidyl tartarate was replaced with dithiobis(succinimidyl acetate), another homobifunctional cross-linker with a higher spacer arm, the low- and high-affinity sites were both restored, with reappearance of two phlorizin-binding proteins with approx. molecular masses of 70 and 120 kDa. We conclude that high-affinity phlorizin-binding sites depend on the presence of the heterodimeric 120 kDa protein.

The extracellular matrix of the central and peripheral nervous systems: structure and function

1988 ◽  
Vol 69 (2) ◽  
pp. 155-170 ◽  
Author(s):  
James T. Rutka ◽  
Gerard Apodaca ◽  
Robert Stern ◽  
Mark Rosenblum
Keyword(s):  
Extracellular Matrix ◽  
Nervous System ◽  
Cell Types ◽  
Structure And Function ◽  
Nervous Systems ◽  
Content Type ◽  
Body Of Knowledge ◽  
Central Nervous Systems ◽  
Biological Adhesive ◽  
And Function

✓ The extracellular matrix (ECM) is the naturally occurring substrate upon which cells migrate, proliferate, and differentiate. The ECM functions as a biological adhesive that maintains the normal cytoarchitecture of different tissues and defines the key spatial relationships among dissimilar cell types. A loss of coordination and an alteration in the interactions between mesenchymal cells and epithelial cells separated by an ECM are thought to be fundamental steps in the development and progression of cancer. Although a substantial body of knowledge has been accumulated concerning the role of the ECM in most other tissues, much less is known of the structure and function of the ECM in the nervous system. Recent experiments in mammalian systems have shown that an increased knowledge of the ECM in the nervous system can lead to a better understanding of complex neurobiological processes under developmental, normal, and pathological conditions. This review focuses on the structure and function of the ECM in the peripheral and central nervous systems and on the importance of ECM macromolecules in axonal regeneration, cerebral edema, and cerebral neoplasia.

Locomotive Bogie Wheelset Assembly Jidoka

2014 ◽  
Vol 687-691 ◽  
pp. 117-120
Author(s):  
Qiang Cheng ◽  
Li Sun ◽  
Zi Qin Ma ◽  
Peng Zhang ◽  
Xiu Ling Sun ◽  
...  
Keyword(s):  
Mathematical Model ◽  
Retrieval System ◽  
Structure And Function ◽  
System Structure ◽  
Storage And Retrieval ◽  
Set Up ◽  
And Function

The process of locomotive bogie wheelset assembly was investigated in-depth. And the Jidoka process of wheelset assembly based on automatic storage and retrieval system was researched. The wheelset assembly Jidoka system structure and function were discussed. The wheelset fitted optimization mathematical model was set up.

scholarly journals Filopodome mapping identifies p130Cas as a mechanosensitive regulator of filopodia stability

2018 ◽  
Author(s):  
Guillaume Jacquemet ◽  
Rafael Saup ◽  
Hellyeh Hamidi ◽  
Mitro Miihkinen ◽  
Johanna Ivaska
Keyword(s):  
Binding Sites ◽  
Focal Adhesions ◽  
Structure And Function ◽  
Structured Illumination ◽  
Structured Illumination Microscopy ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Cellular Behaviour ◽  
And Function ◽  
Fine Tune

AbstractFilopodia are adhesive cellular protrusions specialised in the detection of extracellular matrix (ECM)-derived cues. While ECM engagement at focal adhesions is known to trigger the recruitment of hundreds of proteins (“adhesome”) to fine-tune cellular behaviour, the components of the filopodia adhesions remain undefined. Here, we performed a structured illumination microscopy-based screen to map the localisation of 80 target proteins, linked to cell adhesion and migration, within filopodia. We demonstrate preferential enrichment of several adhesion proteins to either filopodia tips, filopodia shafts, or shaft subdomains suggesting divergent, spatially restricted functions for these proteins. Moreover, proteins with phospho-inositide (PI) binding sites are particularly enriched in filopodia. This, together with the strong localisation of PI(3,4)P2 in filopodia tips, predicts critical roles for PIs in regulating filopodia ultra-structure and function. Our mapping further reveals that filopodia adhesions consist of a unique set of proteins, the filopodome, that are distinct from classical nascent adhesions, focal adhesions and fibrillar adhesions. Using live imaging, we observe that filopodia adhesions can give rise to nascent adhesions, which, in turn, form focal adhesions. Finally, we demonstrate that p130Cas (BCAR1) is recruited to filopodia tips via its CCHD domain and acts as a mechanosensitive regulator of filopodia stability.

scholarly journals Identification and Computational Analysis of 3D-Structure Of MOCS1

2021 ◽  
Author(s):  
Maham Hamid ◽  
uzma habib ◽  
Javeria Batool ◽  
Arshemah Qaisar ◽  
Rehan Zafar Paracha
Keyword(s):  
Binding Sites ◽  
Biosynthetic Pathway ◽  
Computational Analysis ◽  
Tertiary Structure ◽  
3D Structure ◽  
Structure And Function ◽  
Molybdenum Cofactor ◽  
Recognition Method ◽  
And Function ◽  
Ramachandran Plots

Abstract Cyclic pyranopterin monophosphate (cPMP) is one of the most stable intermediates in Molybdenum cofactor (MoCo) biosynthetic pathway. In humans, synthesis of cPMP from Guanosine triphosphate (GTP) requires functional genes i.e. Molybdenum Cofactor Synthesis-1 (MOCS1) genes that contains for two catalytic proteins MOCS1A and MOCS1B. Importance of MOCS1A and MOCS1B for biosynthesis of MoCo reveals from the fact that its deficiency leads to MoCo type A deficiency. As there is no structure available for MOCS1 genes in the literature, tertiary structure of MOCS1 genes were investigated in this research via threading or folds recognition method by i-TASSER and validation was done using ERRAT, Verify3D and Ramachandran plots. Binding sites were predicted and validated. Docking of MOCS1A with GTP and MOCS1B with 3, 8 dihydroguanosine was done using Autodock via PyRx. Apart from this, highly confident mutations were also predicted using SIFT and polyphen2 that can alter the structure and function of MOCS1 gene.

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