Indian Institute of Technology, Jodhpur

About: Indian Institute of Technology, Jodhpur is a education organization based out in Jodhpur, India. It is known for research contribution in the topics: Computer science & Welding. The organization has 914 authors who have published 2221 publications receiving 19243 citations.

Glucose and lipid metabolism alterations in liver and adipose tissue pre-dispose p47phox knockout mice to systemic insulin resistance.

Abstract: Oxidative stress due to enhanced production or reduced scavenging of reactive oxygen species (ROS) has been associated with diet (dyslipidemia) induced obesity and insulin resistance (IR). The present study was undertaken to assess the role of p47phox in IR using wild type (WT) and p47phox-/- mice, fed with different diets (HFD, LFD or Chow). Augmented body weight, glucose intolerance and reduced insulin sensitivity were observed in p47phox-/- mice fed with 45% HFD and 10% LFD. Further, body fat and circulating lipids were increased significantly with 5 weeks LFD feeding in p47phox-/- mice, while parameters of energy homeostasis were reduced as compared with WT mice. LFD fed knockout (KO) mice showed an enhanced hepatic glycogenolysis, and reduced insulin signalling in liver and adipose tissue, while skeletal muscle tissue remained unaffected. A significant increase in hepatic lipids, adiposity, as well as expression of genes regulating lipid synthesis, breakdown and efflux were observed in LFD fed p47phox-/- mice after 5 weeks. On the other hand, mice lacking p47phox demonstrated altered glucose tolerance and tissue insulin sensitivity after 5 weeks chow feeding, while changes in body weight, respiratory exchange ratio (RER) and heat production are non-significant. Our data demonstrate that lack of p47phox is sufficient to induce IR through altered glucose and lipid utilization by the liver and adipose tissue.

Efficient Space-time Video Super Resolution using Low-Resolution Flow and Mask Upsampling

Abstract: This paper explores an efficient solution for Space-time Super-Resolution, aiming to generate High-resolution Slow-motion videos from Low Resolution and Low Frame rate videos. A simplistic solution is the sequential running of Video Super Resolution and Video Frame interpolation models. However, this type of solutions are memory inefficient, have high inference time, and could not make the proper use of space-time relation property. To this extent, we first interpolate in LR space using quadratic modeling. Input LR frames are super-resolved using a state-of-the-art Video Super-Resolution method. Flowmaps and blending mask which are used to synthesize LR interpolated frame is reused in HR space using bilinear upsampling. This leads to a coarse estimate of HR intermediate frame which often contains artifacts along motion boundaries. We use a refinement network to improve the quality of HR intermediate frame via residual learning. Our model is lightweight and performs better than current state-of-the-art models in REDS STSR Validation set.

Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding

Abstract: Nucleosome assembly proteins (Naps) influence chromatin dynamics by directly binding to histones. Here we provide a comprehensive structural and biochemical analysis of a Nap protein from Caenorhabditis elegans (CeNap1). CeNap1 naturally lacks the acidic N-terminal tail and has a short C-terminal tail compared to many other Nap proteins. Comparison of CeNap1 with full length and tail-less constructs of Saccharomyces cerevisiae Nap1 uncovers the role of these tails in self-association, histone binding, and Nap competition with DNA for H2A-H2B. We find that the presence of tails influences the stoichiometry of H2A-H2B binding and is required to complete the interactions between H2A-H2B and DNA. The absolute stoichiometry of the Nap protein and H2A-H2B complex is 2:1 or 2:2, with only a very small population of higher-order oligomers occurring at 150 mM NaCl. We also show that H3-H4 binds differently than H2A-H2B and that an (H3-H4)2 tetramer can simultaneously bind two Nap2 protein homodimers.