{"title":"Comprehensive review on some food-derived bioactive peptides with anti-hypertension therapeutic potential for angiotensin-converting enzyme (ACE) inhibition","authors":"O. A. Olalere, P. Yap, C. Gan","doi":"10.1007/s42485-023-00106-8","DOIUrl":"https://doi.org/10.1007/s42485-023-00106-8","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"60 1","pages":"129-161"},"PeriodicalIF":0.0,"publicationDate":"2023-05-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73508899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Amit Gupta, Niharika Sahu, Vinay Kumar Singh, Rajeshwar P Sinha
{"title":"Evolutionary aspects of mutation in functional motif and post-translational modifications in SARS-CoV-2 3CLpro (Mpro): an in-silico study.","authors":"Amit Gupta, Niharika Sahu, Vinay Kumar Singh, Rajeshwar P Sinha","doi":"10.1007/s42485-023-00105-9","DOIUrl":"10.1007/s42485-023-00105-9","url":null,"abstract":"<p><p>SARS CoV-2 is the virus that caused the COVID-19 pandemic. The main protease is one of the most prominent pharmacological targets for developing anti-COVID-19 therapeutic drugs (Mpro); SARS-CoV-2 replication is dependent on this component. SARS CoV-2's Mpro/cysteine protease is quite identical to SARS CoV-1's Mpro/cysteine protease. However, there is limited information on its structural and conformational properties. The present study aims to perform a complete in silico evaluation of Mpro protein's physicochemical properties. The motif prediction, post-translational modifications, effect of point mutation, and phylogenetic links were studied with other homologs to understand the molecular and evolutionary mechanisms of these proteins. The Mpro protein sequence was obtained in FASTA format from the RCSB Protein Data Bank. The structure of this protein was further characterized and analyzed using standard bioinformatics methods. According to Mpro's in-silico characterization, the protein is a basic, non-polar, and thermally stable globular protein. The outcomes of the phylogenetic and synteny study showed that the protein's functional domain amino acid sequence is substantially conserved. Furthermore, it has undergone many changes at the motif level over time from porcine epidemic diarrhoea virus to SARS-CoV 2, possibly to achieve various functions. Several post-translational modifications (PTMs) were also observed, and the possibilities of changes in Mpro protein exhibit additional orders of peptidase function regulation. During heatmap development, the effect of a point mutation on the Mpro protein was seen. This protein's structural characterization will aid in a better understanding of its function and mechanism of action.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s42485-023-00105-9.</p>","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":" ","pages":"1-11"},"PeriodicalIF":0.0,"publicationDate":"2023-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10099016/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10092436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Amitava Talukdar, A. Malhotra, H. Lalremsanga, Vishal Santra, Robin Doley
{"title":"Bungarus fasciatus venom from eastern and north-east India: venom variation and immune cross-reactivity with Indian polyvalent antivenoms","authors":"Amitava Talukdar, A. Malhotra, H. Lalremsanga, Vishal Santra, Robin Doley","doi":"10.1007/s42485-022-00104-2","DOIUrl":"https://doi.org/10.1007/s42485-022-00104-2","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"57 1","pages":"61-76"},"PeriodicalIF":0.0,"publicationDate":"2023-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81552161","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Back2Basics: animal lectins: an insight into a highly versatile recognition protein.","authors":"Akshaya Radhakrishnan, Hethesh Chellapandian, Pasiyappazham Ramasamy, Sivakamavalli Jeyachandran","doi":"10.1007/s42485-022-00102-4","DOIUrl":"https://doi.org/10.1007/s42485-022-00102-4","url":null,"abstract":"<p><p>The rapid advancement of molecular research has contributed to the discovery of 'Lectin', a carbohydrate-binding protein which specifically interacts with receptors on surface glycan moieties that regulate various critical cellular activities. The first animal lectin reported was 'the asialoglycoprotein receptor' in mammalian cells which helped analyze how animal lectins differ in glycoconjugate binding. Animal lectins are classified into several families, depending on their diverse cellular localization, and the binding specificities of their Carbohydrate-Recognition Domain (CRD) modules. Earlier characterization of animal lectins classified them into two structural families, the C-type (Ca<sup>2+</sup>-dependent binding) and S-type galectins (sulfhydryl-dependent binding) lectins. The C-type lectin includes the most significant animal lectins, such as endocytic receptors, mannose receptors, selectins, and collectins. The recent developments in research based on the complexity of the carbohydrate ligands, the metabolic processes they perform, their expression levels, and their reliance on divalent cations have identified more than 100 animal lectins and classified them into around 13 different families, such as Calnexin, F-lectin, Intelectin, Chitinase-like lectin, F-box lectin, etc. Understanding their structure and expression patterns have aided in defining their significant functions including cell adhesion, antimicrobial activity, innate immunity, disease diagnostic biomarkers, and drug delivery through specific carbohydrate-protein interactions. Such extensive potential roles of animal lectins made it equally important to plant lectins among researchers. Hence, the review focuses on providing an overview of animal lectins, their taxonomy, structural characteristics, and functions in diverse aspects interconnected to their specific carbohydrate and glycoconjugate binding.</p><p><strong>Graphical abstract: </strong></p>","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"14 1","pages":"43-59"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9799708/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9129954","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Structure–function relationship of α-crystallin in the context of vertebrate lens evolution and its role in eye disorders","authors":"Aparajita Chakraborty, P. De, S. Saha","doi":"10.1007/s42485-022-00101-5","DOIUrl":"https://doi.org/10.1007/s42485-022-00101-5","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"29 1","pages":"25-41"},"PeriodicalIF":0.0,"publicationDate":"2022-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73013240","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Shrestha Dutta, Swatilekha Ghosh, A. Mishra, Rajgourab Ghosh
{"title":"Oncoproteomics: insight into current proteomic technologies in cancer biomarker discovery and treatment","authors":"Shrestha Dutta, Swatilekha Ghosh, A. Mishra, Rajgourab Ghosh","doi":"10.1007/s42485-022-00100-6","DOIUrl":"https://doi.org/10.1007/s42485-022-00100-6","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"78 1","pages":"1-24"},"PeriodicalIF":0.0,"publicationDate":"2022-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89834904","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Evaluation of steric entanglement in coiled-coil and domain-swapped protein interfaces using 3D printed models","authors":"M. Blaber","doi":"10.1007/s42485-022-00099-w","DOIUrl":"https://doi.org/10.1007/s42485-022-00099-w","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"44 1","pages":"219 - 226"},"PeriodicalIF":0.0,"publicationDate":"2022-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74351791","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Pangenome and subtractive genomic analysis of Clostridioides difficile reveals putative drug targets","authors":"A. Fatoba, D. Fatoba, S. O. Babalola","doi":"10.1007/s42485-022-00097-y","DOIUrl":"https://doi.org/10.1007/s42485-022-00097-y","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"57 1","pages":"247-256"},"PeriodicalIF":0.0,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84417558","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sravani Polepalli, Richa Singh, Shoma Naskar, Pasupuleti Skdb Punyasri, Kongari Ranjith Kumar, Kameshwari Yele, V. Krishnakumari, Raman Bakthisaran, D. Jain, G. Chandak, Swasti Raychaudhuri
{"title":"Rapid and deep plasma proteomics workflows for robust identification and quantification of biomarkers of sickle cell anaemia","authors":"Sravani Polepalli, Richa Singh, Shoma Naskar, Pasupuleti Skdb Punyasri, Kongari Ranjith Kumar, Kameshwari Yele, V. Krishnakumari, Raman Bakthisaran, D. Jain, G. Chandak, Swasti Raychaudhuri","doi":"10.1007/s42485-022-00096-z","DOIUrl":"https://doi.org/10.1007/s42485-022-00096-z","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"3 1","pages":"205 - 218"},"PeriodicalIF":0.0,"publicationDate":"2022-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76576667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Md. Yasir Arafat, Kanika Narula, Pragya Nalwa, Atreyee Sengupta, N. Chakraborty, S. Chakraborty
{"title":"Proteomic analysis of phytopathogenic fungus Macrophomina phaseolina identify known and novel mycelial proteins with roles in growth and virulence","authors":"Md. Yasir Arafat, Kanika Narula, Pragya Nalwa, Atreyee Sengupta, N. Chakraborty, S. Chakraborty","doi":"10.1007/s42485-022-00095-0","DOIUrl":"https://doi.org/10.1007/s42485-022-00095-0","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"69 1","pages":"149 - 157"},"PeriodicalIF":0.0,"publicationDate":"2022-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85739341","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}