Journal of Molecular Recognition最新文献

{"title":"Editorial: The Journal of Molecular Recognition: Changing of the guard","authors":"Rebecca C. Wade","doi":"10.1002/jmr.3081","DOIUrl":"10.1002/jmr.3081","url":null,"abstract":"<p>At the beginning of 2024, I took over from Marc van Regenmortel as the third Editor-in-Chief of JMR. The journal was established by Irwin Chaiken in 1988 with affiliation to the International Society for Molecular Recognition (ismr.org) and with a strong focus on methods to measure affinity. Presciently, and quite unusually, the journal was founded to focus on a phenomenon—molecular recognition—and it is a phenomenon that is central to biomolecular science. This has enabled the content of the journal to evolve over time as new techniques, ideas, and applications have emerged. In 1999, Marc van Regenmortel became Editor-in-Chief, introduced new types of articles, and broadened the scope of the journal. For example, the series of comprehensive critical reviews on methods, such as surface plasmon resonance, isothermal calorimetry, and molecular docking, were particularly well read. We, the editors and advisory board members, thank him for his vision, inspiration, dedication, and hard work in successfully steering the journal over the last 25 years. He leaves the journal on solid foundations, publishing on a broad range of molecular recognition topics. Marc sought to make the journal, not only THE place to publish high-quality research on molecular recognition but also a venue for discussion on concepts and controversial issues relating to molecular recognition. We will continue to pursue these aims. For this purpose, we are introducing an additional article category called “Perspective” for short articles with commentaries, discussions, or reviews on current topics. The first two Perspectives are on Marc's contributions to science and the scientific community<span><sup>1, 2</sup></span> and highly recommended reading. We will also aim to nurture the broad community of molecular recognition researchers, for example, through awards at conferences and with the establishment of a new Early Career Advisory Board for the journal.</p><p>Now is an appropriate time for JMR to enter into its third epoch. The growing prominence of computational science and the dramatic advances in artificial intelligence are changing how research into molecular recognition is done. This is reflected in the appointment of a theoretical and computational scientist at the helm of JMR. Moreover, the panel of Associate Editors includes two theoreticians as well as other scientists who combine computation with their experimental work. We will be looking to see how artificial intelligence and data science complement our existent methodological toolbox to accelerate molecular recognition research and enable the discovery of new molecules, new binding mechanisms, and new conceptual insights. However, in all the excitement over the new possibilities that such approaches bring, it is important to ensure that computational and machine learning tools and techniques are applied rigorously and carefully, with experimental validation whenever possible. Moreover, we expect that AI will be a","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3081","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140101756","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Marc van Regenmortel, personal recollections on a forward-thinking editor","authors":"Jean-Luc Pellequer,&nbsp;Eric Westhof","doi":"10.1002/jmr.3080","DOIUrl":"10.1002/jmr.3080","url":null,"abstract":"<p>Marc van Regenmortel was the Editor-in-Chief of the Journal of Molecular Recognition for the last 25 years. Without attempting to summarize Marc's exceptional career and achievements, we would like to tell the story of the tortuous and contingent path to the unravelling of a key molecular recognition process in antigenicity. Life is indeed full of contingencies and scientific life, full of meetings and random encounters, is prone to contingencies, a key element in discovery and innovation.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3080","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140028253","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Marc H. V. van Regenmortel, a virtual friend and a real colleague","authors":"Vladimir N. Uversky","doi":"10.1002/jmr.3079","DOIUrl":"10.1002/jmr.3079","url":null,"abstract":"&lt;p&gt;Unlike Jean-Luc Pellequer and Eric Westhof,&lt;span&gt;&lt;sup&gt;1&lt;/sup&gt;&lt;/span&gt; who were colleagues of Marc H.V. van Regenmortel, I have never met him in person. However, I can add my voice to the discussion of how contingency or serendipity has led me to productively collaborate with Marc (unfortunately, exclusively in the on-line format), resulting in the publication of a joint paper in 2020.&lt;span&gt;&lt;sup&gt;2&lt;/sup&gt;&lt;/span&gt; Before moving to this part of my story, a short historical excurse is needed.&lt;/p&gt;&lt;p&gt;My first (once again, exclusively virtual) encounter with Marc took place in 2004, when he played a crucial role in our work on one of the first comprehensive reviews on the roles of intrinsically disordered proteins and regions (IDPs/IDRs) in molecular recognition, regulation, and cell signaling.&lt;span&gt;&lt;sup&gt;3&lt;/sup&gt;&lt;/span&gt; In the middle of 2004, I joined the Center for Computational Biology and Bioinformatics (CCBB) at the Indiana University-Purdue University at Indianapolis (IUPUI) that was created and headed by Prof. A. Keith Dunker, whom I worked with for 6 years on different aspects of the protein intrinsic disorder phenomenon. One of my first projects there was analysis of the then-available literature data on the functionality of intrinsic disorder.&lt;/p&gt;&lt;p&gt;By that time, it became clear that although IDPs/IDRs have been mostly ignored by the scientific community since the inception of the lock-and-key model by Hermann Emil Louis Fischer (1852–1919) in 1894,&lt;span&gt;&lt;sup&gt;4, 5&lt;/sup&gt;&lt;/span&gt; many aspects of protein functionality could not be explained using this important model and its associated sequence-structure-function paradigm. In fact, many protein functions do not require specific structures, instead relying on conformational flexibility, and as a result, many biologically active proteins (or protein regions) do not have unique structures, instead being intrinsically disordered.&lt;span&gt;&lt;sup&gt;6-15&lt;/sup&gt;&lt;/span&gt; However, the concept of functional disorder was still met with strong skepticism by the scientific community, especially by those who worked in structural biology.&lt;/p&gt;&lt;p&gt;This brings us to my first example of Marc-centric contingency or serendipity. When Keith contacted Marc to check if the manuscript we were working on would fit the scope of the Journal of Molecular Recognition, to our big surprise, we received very enthusiastic support. Those times were still the early days of protein intrinsic disorder, and many scientific journals were simply dismissing the idea of functional disorder as nonsensical (as an example, it took more than a year to publish my first paper on this subject (Ref. &lt;span&gt;16&lt;/span&gt;), which was rejected by 14 journals before being eventually accepted by Proteins&lt;span&gt;&lt;sup&gt;7&lt;/sup&gt;&lt;/span&gt;). During the preparation of the manuscript for the Journal of Molecular Recognition, we had a productive exchange with Marc, which was very useful and is reflected in the acknowledgement in the resulting paper that reads “Both A.K.D. and V.N.U. t","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-02-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3079","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139990347","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tenth International AFMBioMed Conference on AFM in Life Sciences and Medicine, August 30–September 2, 2022, Nagoya-Okasaki, Japan","authors":"Takayuki Uchihashi,&nbsp;Felix Rico,&nbsp;Jean-Luc Pellequer","doi":"10.1002/jmr.3077","DOIUrl":"10.1002/jmr.3077","url":null,"abstract":"&lt;p&gt;Founded in June 2006, after a first seminal French-speaking conference held on the topic “Atelier Nanobiosciences: protéines et membranes” in &lt;i&gt;Nîmes&lt;/i&gt; in June 2004, the AFMBioMed Conference brings researchers and students from around the world together to discuss the latest scientific results of atomic force microscopy in life sciences and medicine.&lt;span&gt;&lt;sup&gt;1, 2&lt;/sup&gt;&lt;/span&gt; A full account of the AFMBioMed history can be found here.&lt;span&gt;&lt;sup&gt;3&lt;/sup&gt;&lt;/span&gt; AFMBioMed organized its first international meeting in &lt;i&gt;Barcelona&lt;/i&gt;, Spain, in spring 2007&lt;span&gt;&lt;sup&gt;4&lt;/sup&gt;&lt;/span&gt; and this was followed, at 18-month intervals, by &lt;i&gt;Monterey&lt;/i&gt;, CA, USA, in fall 2008,&lt;span&gt;&lt;sup&gt;5&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Crveni otok&lt;/i&gt; (Red Island) near the Adriatic City of Rovinj, Croatia, in spring 2010,&lt;span&gt;&lt;sup&gt;6&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Paris&lt;/i&gt; in summer 2011,&lt;span&gt;&lt;sup&gt;7&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Shanghai&lt;/i&gt; in spring 2013,&lt;span&gt;&lt;sup&gt;8&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;San Diego&lt;/i&gt; in fall 2014,&lt;span&gt;&lt;sup&gt;9&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Porto&lt;/i&gt; in spring 2016,&lt;span&gt;&lt;sup&gt;10&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Krakow&lt;/i&gt; in fall 2017,&lt;span&gt;&lt;sup&gt;3&lt;/sup&gt;&lt;/span&gt; and &lt;i&gt;Münster&lt;/i&gt; in fall 2019.&lt;span&gt;&lt;sup&gt;11&lt;/sup&gt;&lt;/span&gt;&lt;/p&gt;&lt;p&gt;Members of the scientific committee for the tenth edition of the AFMBioMed meeting in Nagoya-Okasaki, Japan, in summer 2022 include past and present organizers &lt;i&gt;Takayuki Uchihashi&lt;/i&gt; (Nagoya University, Japan), &lt;i&gt;Hermann Schillers&lt;/i&gt; (University of Münster, Germany), &lt;i&gt;Malgorzata Lekka&lt;/i&gt; (Polish Academy of Sciences, Poland), &lt;i&gt;Susana R. Sousa&lt;/i&gt; (i3S|INEB, Porto, Portugal), &lt;i&gt;Adam Engler&lt;/i&gt; (UCSD, San Diego, USA), &lt;i&gt;Jun Hu&lt;/i&gt; (SINAP, Shanghai, China), &lt;i&gt;Sanjay Kumar&lt;/i&gt; (University of California, Berkeley, USA), &lt;i&gt;Daniel Navajas&lt;/i&gt; (Universitat de Barcelona, Barcelona, Spain), &lt;i&gt;Simon Scheuring&lt;/i&gt; (Institut National de la Santé et de la Recherche Médicale (INSERM) U1006, Marseille, France), &lt;i&gt;Vesna Svetlicic&lt;/i&gt; (Rudjer Boskovic Institute, Zagreb, Croatia), the original founders of the conference &lt;i&gt;Pierre Parot&lt;/i&gt; (IACA) and &lt;i&gt;Jean-Luc Pellequer&lt;/i&gt; (CEA/DRF, Institut de Biologie Structurale, Grenoble, France), as well as the four invited chairs: &lt;i&gt;Alice Pyne&lt;/i&gt; (Sheffield University, UK), &lt;i&gt;Felix Rico&lt;/i&gt; (Aix-Marseille University—INSERM, France), &lt;i&gt;Takaharu Okajima&lt;/i&gt; (Hokkaido University, Japan), and &lt;i&gt;Noriyuki Kodera&lt;/i&gt; (Kanazawa University, Japan).&lt;/p&gt;&lt;p&gt;The 10th AFMBioMed was scheduled as a landmark conference. Despite the round number 10, it was the last conference organized with a single AFM sponsor (more below). It should have been the last conference that Pierre Parot, the co-founder of AFMBioMed, would participate in. At the end of the 9th conference in Münster, the 10th AFMBioMed conference was initially planned for spring 2021, the cherry blossom season in Japan. Unfortunately, the COVID-19 pandemic modified our plan. The conference was postponed every 6 months while waiting for the reopening of travel to Japan (as well as other countries). In early 2022, the organi","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3077","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139983169","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Utilizing fab fragment-conjugated surface plasmon resonance-based biosensor for detection of Salmonella Enteritidis","authors":"Esma Eser,&nbsp;Okan Öner Ekiz,&nbsp;H. İbrahim Ekiz","doi":"10.1002/jmr.3078","DOIUrl":"10.1002/jmr.3078","url":null,"abstract":"<p>Although antibodies, a key element of biorecognition, are frequently used as biosensor probes, the use of these large molecules can lead to adverse effects. Fab fragments can be reduced to allow proper antigen-binding orientation via thiol groups containing Fab sites that can directly penetrate Au sites chemically. In this study, the ability of the surface plasmon resonance (SPR) sensor to detect <i>Salmonella</i> was studied. Tris(2-carboxyethyl)phosphine was used as a reducing agent to obtain half antibody fragments. Sensor surface was immobilized with antibody, and bacteria suspensions were injected from low to high concentrations. Response units were changed by binding first reduced antibody fragments, then bacteria. The biosensor was able to determine the bacterial concentrations between 10³ and 10⁸ CFU/mL. Based on these results, the half antibody fragmentation method can be generalized for faster, label-free, sensitive, and selective detection of other bacteria species.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139940083","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biophysical and structural characterization of tetramethrin serum protein complex and its toxicological implications","authors":"Pratik Singh,&nbsp;Priyanka Gopi,&nbsp;Majji Sai Sudha Rani,&nbsp;Shweta Singh,&nbsp;Prateek Pandya","doi":"10.1002/jmr.3076","DOIUrl":"10.1002/jmr.3076","url":null,"abstract":"<p>Tetramethrin (TMT) is a commonly used insecticide and has a carcinogenic and neurodegenerative effect on humans. The binding mechanism and toxicological implications of TMT to human serum albumin (HSA) were examined in this study employing a combination of biophysical and computational methods indicating moderate binding affinity and potential hepato and renal toxicity. Fluorescence quenching experiments showed that TMT binds to HSA with a moderate affinity, and the binding process was spontaneous and predominantly enthalpy-driven. Circular dichroism spectroscopy revealed that TMT binding did not induce any significant conformational changes in HSA, resulting in no changes in its alpha-helix content. The binding site and modalities of TMT interactions with HSA as computed by molecular docking and molecular dynamics simulations revealed that it binds to Sudlow site II of HSA via hydrophobic interactions through its dimethylcyclopropane carboxylate methyl propanyl group. The structural dynamics of TMT induce proper fit into the binding site creating increased and stabilizing interactions. Additionally, molecular mechanics–Poisson Boltzmann surface area calculations also indicated that non-polar and van der Waals were found to be the major contributors to the high binding free energy of the complex. Quantum mechanics (QM) revealed the conformational energies of the binding confirmation and the degree of deviation from the global minimum energy conformation of TMT. The results of this study provide a comprehensive understanding of the binding mechanism of TMT with HSA, which is important for evaluating the toxicity of this insecticide in humans.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139746758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Investigation of steric hindrance effect on the interactions between four alkaloids and HSA by isothermal titration calorimetry and molecular docking","authors":"Xinluan Lv,&nbsp;Wenjin Li,&nbsp;Miao Zhang,&nbsp;Ruiyong Wang,&nbsp;Junbiao Chang","doi":"10.1002/jmr.3075","DOIUrl":"10.1002/jmr.3075","url":null,"abstract":"<p>The binding of four alkaloids with human serum albumin (HSA) was investigated by isothermal titration calorimetry (ITC), spectroscopy and molecular docking techniques. The findings demonstrated that theophylline or caffeine can bind to HAS, respectively. The number of binding sites and binding constants are obtained. The binding mode is a static quenching process. The effects of steric hindrance, temperature, salt concentration and buffer solution on the binding indicated that theophylline and HSA have higher binding affinity than caffeine. The fluorescence and ITC results showed that the interaction between HSA and theophylline or caffeine is an entropy-driven spontaneous exothermic process. The hydrophobic force was the primary driving factor. The experimental results were consistent with the molecular docking data. Based on the molecular structures of the four alkaloids, steric hindrance might be a major factor in the binding between HSA and these four alkaloids. This study elucidates the mechanism of interactions between four alkaloids and HSA.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 2","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139403309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Spectroscopic, computational, cytotoxicity, and docking studies of 6-bromobenzimidazole as anti-breast cancer agent","authors":"V. S. Kunjumol,&nbsp;S. Jeyavijayan,&nbsp;S. Sumathi,&nbsp;N. Karthik","doi":"10.1002/jmr.3074","DOIUrl":"10.1002/jmr.3074","url":null,"abstract":"<p>6-Bromobenzimidazole (6BBZ) has been calculated in this study utilizing the 6-311++G(d,p) basis set and the Becke-3-Lee-Yang-Parr density functional approaches. The basic frequencies and geometric optimization are known. FTIR, FT-Raman, and UV–Vis spectra of the substance are compared between its computed and observed values. The energy gap between highest occupied molecular orbital–lowest unoccupied molecular orbital and molecule electrostatic potentials has been represented by charge density distributions that may be associated with the biological response. Time-dependent density functional theory calculations in the gas phase and dimethyl sulfoxide were carried out to ascertain the electronic properties and energy gap values using the same basis set. Molecular orbital contributions are investigated using the overlap population, partial, and total densities of states. Natural bond analysis was found to have strong electron delocalization by means of π(C4–C9) → π*(C5–C6), LP (N1) → π*(C7–C8), and LP(Br12) → π*(C5–C6) interactions. The Fukui function and Mulliken analysis have been explored on the atomic charges of the molecule. The nuclear magnetic resonance chemical shifts for ¹H and ¹³C have been computed using the gauge-independent atomic orbital technique. With the highest binding affinity (−6.2 kcal mol⁻¹) against estrogen sulfotransferase receptor (PDB ID: 1AQU) and low IC₅₀ value of 17.23 μg/mL, 6BBZ demonstrated potent action against the MCF-7 breast cancer cell line. Studies on the antibacterial activity and ADMET prediction of the molecule have also been carried out.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 2","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139087185","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Immune infiltration is associated with pan-cancer prognostic biomarker RING finger protein 187","authors":"Xin-Tong Fan,&nbsp;Bing-Fang Gao,&nbsp;Xiao-Fei Wang,&nbsp;Kai Zhou,&nbsp;Ying Zhao,&nbsp;Jie Yuan","doi":"10.1002/jmr.3071","DOIUrl":"10.1002/jmr.3071","url":null,"abstract":"<p>Cancer is associated with the highest mortality rate globally. While life-saving screening and treatments exist, better awareness is needed. RNF187, an E3 ligase regulating biological processes, belongs to the RING domain-containing E3 ligase family. RNF187 may serve as an oncogene due to abnormal expression in tumors. However, its association with immune infiltration and prognosis across various cancers remains unclear. We searched several databases including TCGA, GTE x, CCLE, TIMER, and GSEA. R software was used to evaluate RNF187 differential expression, survival, pathology stage, DNA methylation, tumor mutational burden (TMB), microsatellite instability (MSI), gene co-expression analysis, mismatch repairs (MMRs), tumor microenvironment (TME), and immune cell infiltration. Clinicopathological data were collected, and immunohistochemistry was used to verify RNF187 expression in tumor tissues. RNF187 expression was up-regulated in various cancers compared to that in normal tissues and associated with poor patient outcomes. Dysregulation of RNF187 expression in multiple cancer types was strongly correlated with DNA methylation, MMR, MSI, and TMB. RNF187 could interact with different immune cells in cancers. Biomarkers associated with RNF187 may be helpful for prognosis and immunology in treating pan-cancer patients.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 2","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139087184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Nucleic acid-based electrochemical biosensor for detection of influenza B by gold nanoparticles","authors":"Isar Yahyavi,&nbsp;Fahime Edalat,&nbsp;Neda Pirbonyeh,&nbsp;Arash Letafati,&nbsp;Naghmeh Sattarahmady,&nbsp;Hossein Heli,&nbsp;Afagh Moattari","doi":"10.1002/jmr.3073","DOIUrl":"10.1002/jmr.3073","url":null,"abstract":"<p>The influenza virus is a pervasive pathogen that exhibits increased prevalence during colder seasons, resulting in a significant annual occurrence of infections. Notably, pharmaceutical interventions effective against influenza A strains often exhibit limited efficacy against influenza B variants. Against this backdrop, the need for innovative approaches to accurately and swiftly differentiate and detect influenza B becomes evident. Biosensors play a pivotal role in this detection process, offering rapid, specific, and sensitive identification of the virus, facilitating timely intervention and containment efforts. Oligonucleotide sequences targeting the conserved B/Victoria/2/87 influenza virus NP region were designed. Nasopharyngeal swabs were collected from patients suspected of influenza virus infection, and viral RNA was extracted. RNA quality was assessed through one-step PCR. cDNA synthesis was performed using random hexamers, and real-time PCR quantified the influenza genome. Gold nanoparticles were immobilized on a surface to immobilize the specific DNA probe, and electrochemical hybridization was electrochemically followed. The biosensor exhibited high selectivity and effective distinction of complementary sequences from mismatches and influenza virus cDNA genome. The biosensor successfully detected the influenza B virus genome in real samples. Non-influenza samples yielded no significant hybridization signals. The comparison between the results obtained from the biosensor and real-time PCR revealed full agreement of these methods. The biosensor utilized electrochemical detection of hybridization and proved effective in detecting the influenza B virus genome with high specificity, sensitivity, and selectivity. Comparative analysis with real-time PCR underscored the accuracy and potential applicability of the biosensor in rapid and specific virus detection. This innovative approach holds promise for future diagnostic and epidemiological applications in detecting influenza B virus and other pathogens.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 2","pages":""},"PeriodicalIF":2.7,"publicationDate":"2023-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138830115","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}