Molecular profiling of frontal and occipital subcortical white matter hyperintensities in Alzheimer’s disease by Sulochan Malla, Sulochan Malla, Annie G. Bryant, Annie G. Bryant, Rojashree Jayakumar, Benjamin Woost, Nina Wolf, Andrew Li, Sudeshna Das, Sudeshna Das, Susanne J. van Veluw, Susanne J. van Veluw, Rachel E. Bennett, Rachel E. Bennett

“…To further elucidate vasculature-specific transcriptomic features, we performed RNA-seq analysis on blood vessels isolated from these white matter regions, which revealed an upregulation of genes related to protein folding pathways. Finally, comparing gene expression profiles between AD individuals with high- versus low-WMH burden showed an increased expression of pathways associated with immune function. …”
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Genes involved in DMSO-mediated yield increase of entomopathogenic nematodes by Xingxin Liu, Zhongchen Rao, Richou Han, Linhong Jin, Li Cao

“…The biological processes involved included regulation of biological processes, metabolism, binding, signal transduction, post-transcriptional modifications, metabolism, and protein folding. By using RNAi, knockdown of three genes, Hint module, PAN domain protein, and Dpy-13, significantly regulated the egg load (at least a 17% increase in eggs per hermaphroditic adult) and the yield of infective juveniles (at least a 48% increase), in an optimized 96-well plates containing the medium with 1.6% nutrient broth, 1% corn oil and 1.2% agar, without DMSO. qRT-PCR results confirmed that the expression levels of the knockdown genes decreased significantly, compared to the control. …”
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Insight into the role of antioxidant in microbial lignin degradation: Ascorbic acid as a fortifier of lignin-degrading enzymes by Aipeng Li, Weimin Wang, Shuqi Guo, Changzhi Li, Xinying Wang, Qiang Fei

“…Proteomics analysis suggested that the enhancement in enzyme activity was more likely to attributed to the reinforcement of AA on oxidative protein folding and transportation, rather than changes in enzyme expression. …”
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NMR Studies on the Structure of Yeast Sis1 and the Dynamics of Its Interaction with Ssa1-EEVD by Carolina O. Matos, Glaucia M. S. Pinheiro, Icaro P. Caruso, Gisele C. Amorim, Fabio C. L. Almeida, Carlos H. I. Ramos

“…HSP70 chaperones play pivotal roles in facilitating protein folding, refolding, and disaggregation through their binding and releasing activities. …”
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Mannogalactoglucan from mushrooms protects pancreatic islets via restoring UPR and promotes insulin secretion in T1DM mice by Ting Liu, Si Chen, Yunhe Qu, Lujuan Zheng, Xiaoxuan Yang, Shuhan Men, Yuanning Wang, Hanrui Ma, Yifa Zhou, Yuying Fan

“…AAMP-N activated unfolded protein response (UPR) signaling pathway to maintain ER protein folding homeostasis and promote insulin secretion in vivo. …”
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Identification of Host–Protein Interaction Network of Canine Parvovirus Capsid Protein VP2 in F81 Cells by Hongzhuan Zhou, Huanhuan Zhang, Xia Su, Fuzhou Xu, Bing Xiao, Jin Zhang, Qi Qi, Lulu Lin, Kaidi Cui, Qinqin Li, Songping Li, Bing Yang

“…The results showed that CPV VP2 protein participated mainly in cell metabolism, cell biosynthesis, protein folding and various signal transduction processes. …”
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The DnaJ-Hsp70-Hsp90 co-chaperon networks in scallops under toxic Alexandrium dinoflagellates exposure by Moli Li, Jie Cheng, Huizhen Wang, Jiaoxia Shi, Xiaogang Xun, Wei Lu, Xubo Wang, Jingjie Hu, Zhenmin Bao, Xiaoli Hu

“…A large set of co-chaperons comprising J-domain proteins (DnaJs) regulate the ATPase cycle of Hsp70s with Hsp90s, together constituting a dynamic and functionally versatile network for protein folding/unfolding and regulation. Marine bivalves could accumulate and tolerate paralytic shellfish toxins (PSTs), the well-noted neurotoxins generated during harmful algal blooms. …”
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Hidden route of protein damage through oxygen-confined photooxidation by Seoyoon Kim, Eojin Kim, Mingyu Park, Seong Ho Kim, Byung-Gyu Kim, Seungjin Na, Victor W. Sadongo, W. C. Bhashini Wijesinghe, Yu-Gon Eom, Gwangsu Yoon, Hannah Jeong, Eunhye Hwang, Chaiheon Lee, Kyungjae Myung, Chae Un Kim, Jeong-Mo Choi, Seung Kyu Min, Tae-Hyuk Kwon, Duyoung Min

“…Abstract Oxidative modifications can disrupt protein folds and functions, and are strongly associated with human aging and diseases. …”
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Evolutionary origins and functional diversification of Auxin Response Factors by Jorge Hernández-García, Vanessa Polet Carrillo-Carrasco, Juriaan Rienstra, Keita Tanaka, Martijn de Roij, Melissa Dipp-Álvarez, Alejandra Freire-Ríos, Isidro Crespo, Roeland Boer, Willy A. M. van den Berg, Simon Lindhoud, Dolf Weijers

“…We reveal the shared origin of ARFs from preexisting domains, uncovering a protein fold homologous to the ARF DNA-binding fold in a conserved eukaryotic chromatin regulator. …”
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DIA-based quantitative proteomic analysis on porcine meat quality at different chilling rates by Yuqiang Bai, Tongjing Yan, Fei Fang, Xin Li, Su Wang, Juan Li, Chengli Hou, Dequan Zhang

“…Seventy-nine differential abundant proteins (fold change >1.5, P <0.05), including 46 up-regulated and 33 down-regulated proteins, were identified and mainly involved in carbon metabolism, pyruvate metabolism and proteasome pathways. …”
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Generic residue numbering of the GAIN domain of adhesion GPCRs by Florian Seufert, Guillermo Pérez-Hernández, Gáspár Pándy-Szekeres, Ramon Guixà-González, Tobias Langenhan, David E. Gloriam, Peter W. Hildebrand

“…Abstract The GPCR autoproteolysis inducing (GAIN) domain is an ancient protein fold ubiquitous in adhesion G protein-coupled receptors (aGPCR). …”
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Genetic and biochemical characterization of a radical SAM enzyme required for post-translational glutamine methylation of methyl-coenzyme M reductase by Roy J. Rodriguez Carrero, Cody T. Lloyd, Janhavi Borkar, Shounak Nath, Liviu M. Mirica, Satish Nair, Squire J. Booker, William Metcalf

“…Structural characterization of the Ni(II) form of Gln-methylated M. acetivorans MCR revealed no significant differences in the protein fold between the modified and unmodified enzyme; however, the purified enzyme contained the heterodisulfide reaction product, as opposed to the free cofactors found in eight prior M. acetivorans MCR structures, suggesting that substrate/product binding is altered in the modified enzyme. …”
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