scholarly journals Unraveling the mysteries of the titin–N2A signalosome

2021 ◽  
Vol 153 (8) ◽  
Author(s):  
Anthony L. Hessel ◽  
Wolfgang A. Linke

The sarcomeric titin springs and accessory proteins modulate muscle force and mechanical signaling at the N2A signalosome.

2020 ◽  
Author(s):  
Ze Gong ◽  
Katrina M. Wisdom ◽  
Eóin McEvoy ◽  
Julie Chang ◽  
Kolade Adebowale ◽  
...  

2020 ◽  
Vol 28 ◽  
Author(s):  
Alireza Milani ◽  
Kazem Baesi ◽  
Elnaz Agi ◽  
Ghazal Marouf ◽  
Maryam Ahmadi ◽  
...  

Background:: The combination antiretroviral therapy (cART) could increase the number of circulating naive CD4 T lymphocytes, but was not able to eradicate human immunodeficiency virus-1 (HIV-1) infection. Objective:: Thus, induction of strong immune responses is important for control of HIV-1 infection. Furthermore, a simple and perfect serological method is required to detect virus in untreated-, treated- and drug resistant- HIV-1 infected individuals. Methods:: This study was conducted to assess and compare immunogenic properties of Nef, Vif, Vpr and Vpu accessory proteins as an antigen candidate in mice and their diagnostic importance in human as a biomarker. Results:: Our data showed that in mice, all heterologous prime/ boost regimens were more potent than homologous prime/ boost regimens in eliciting Th1 response and Granzyme B secretion as CTL activity. Moreover, the Nef, Vpu and Vif proteins could significantly increase Th1 immune response. In contrast, the Vpr protein could considerably induce Th2 immune response. On the other hand, among four accessory proteins, HIV-1 Vpu could significantly detect treated group from untreated group as a possible biomarker in human. Conclusion:: Generally, among accessory proteins, Nef, Vpu and Vif antigens were potentially more suitable vaccine antigen candidates than Vpr antigen. Human antibodies against all these proteins were higher in HIV-1 different groups than healthy group. Among them, Vpu was known as a potent antigen in diagnosis of treated from untreated individuals. The potency of accessory proteins as an antigen candidate in an animal model and a human cohort study are underway.


2015 ◽  
Vol 14 (1) ◽  
pp. 9-23 ◽  
Author(s):  
Maxime Veillette ◽  
Jonathan Richard ◽  
Marzena Pazgier ◽  
George K. Lewis ◽  
Matthew S. Parsons ◽  
...  

2020 ◽  
Author(s):  
Anurag Sohane ◽  
Ravinder Agarwal

Abstract Various simulation type tools and conventional algorithms are being used to determine knee muscle forces of human during dynamic movement. These all may be good for clinical uses, but have some drawbacks, such as higher computational times, muscle redundancy and less cost-effective solution. Recently, there has been an interest to develop supervised learning-based prediction model for the computationally demanding process. The present research work is used to develop a cost-effective and efficient machine learning (ML) based models to predict knee muscle force for clinical interventions for the given input parameter like height, mass and angle. A dataset of 500 human musculoskeletal, have been trained and tested using four different ML models to predict knee muscle force. This dataset has obtained from anybody modeling software using AnyPyTools, where human musculoskeletal has been utilized to perform squatting movement during inverse dynamic analysis. The result based on the datasets predicts that the random forest ML model outperforms than the other selected models: neural network, generalized linear model, decision tree in terms of mean square error (MSE), coefficient of determination (R2), and Correlation (r). The MSE of predicted vs actual muscle forces obtained from the random forest model for Biceps Femoris, Rectus Femoris, Vastus Medialis, Vastus Lateralis are 19.92, 9.06, 5.97, 5.46, Correlation are 0.94, 0.92, 0.92, 0.94 and R2 are 0.88, 0.84, 0.84 and 0.89 for the test dataset, respectively.


2021 ◽  
Vol 15 ◽  
pp. 117793222110258
Author(s):  
Ritesh Gorkhali ◽  
Prashanna Koirala ◽  
Sadikshya Rijal ◽  
Ashmita Mainali ◽  
Adesh Baral ◽  
...  

SARS-CoV-2 virus, the causative agent of COVID-19 pandemic, has a genomic organization consisting of 16 nonstructural proteins (nsps), 4 structural proteins, and 9 accessory proteins. Relative of SARS-CoV-2, SARS-CoV, has genomic organization, which is very similar. In this article, the function and structure of the proteins of SARS-CoV-2 and SARS-CoV are described in great detail. The nsps are expressed as a single or two polyproteins, which are then cleaved into individual proteins using two proteases of the virus, a chymotrypsin-like protease and a papain-like protease. The released proteins serve as centers of virus replication and transcription. Some of these nsps modulate the host’s translation and immune systems, while others help the virus evade the host immune system. Some of the nsps help form replication-transcription complex at double-membrane vesicles. Others, including one RNA-dependent RNA polymerase and one exonuclease, help in the polymerization of newly synthesized RNA of the virus and help minimize the mutation rate by proofreading. After synthesis of the viral RNA, it gets capped. The capping consists of adding GMP and a methylation mark, called cap 0 and additionally adding a methyl group to the terminal ribose called cap1. Capping is accomplished with the help of a helicase, which also helps remove a phosphate, two methyltransferases, and a scaffolding factor. Among the structural proteins, S protein forms the receptor of the virus, which latches on the angiotensin-converting enzyme 2 receptor of the host and N protein binds and protects the genomic RNA of the virus. The accessory proteins found in these viruses are small proteins with immune modulatory roles. Besides functions of these proteins, solved X-ray and cryogenic electron microscopy structures related to the function of the proteins along with comparisons to other coronavirus homologs have been described in the article. Finally, the rate of mutation of SARS-CoV-2 residues of the proteome during the 2020 pandemic has been described. Some proteins are mutated more often than other proteins, but the significance of these mutation rates is not fully understood.


Soft Matter ◽  
2021 ◽  
Author(s):  
Farid Alisafaei ◽  
Xingyu Chen ◽  
Thomas Leahy ◽  
Paul A. Janmey ◽  
Vivek B. Shenoy

Correction for ‘Long-range mechanical signaling in biological systems’ by Farid Alisafaei et al., Soft Matter, 2020, DOI: 10.1039/d0sm01442g.


2021 ◽  
Vol 9 (1) ◽  
pp. 11
Author(s):  
Clinton Rice ◽  
Oindrila De ◽  
Haifa Alhadyian ◽  
Sonia Hall ◽  
Robert E. Ward

The septate junction (SJ) provides an occluding function for epithelial tissues in invertebrate organisms. This ability to seal the paracellular route between cells allows internal tissues to create unique compartments for organ function and endows the epidermis with a barrier function to restrict the passage of pathogens. Over the past twenty-five years, numerous investigators have identified more than 30 proteins that are required for the formation or maintenance of the SJs in Drosophila melanogaster, and have determined many of the steps involved in the biogenesis of the junction. Along the way, it has become clear that SJ proteins are also required for a number of developmental events that occur throughout the life of the organism. Many of these developmental events occur prior to the formation of the occluding junction, suggesting that SJ proteins possess non-occluding functions. In this review, we will describe the composition of SJs, taking note of which proteins are core components of the junction versus resident or accessory proteins, and the steps involved in the biogenesis of the junction. We will then elaborate on the functions that core SJ proteins likely play outside of their role in forming the occluding junction and describe studies that provide some cell biological perspectives that are beginning to provide mechanistic understanding of how these proteins function in developmental contexts.


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