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Each big journey starts with a first step: Importance of oligomerization. 每一段伟大的旅程都始于第一步：低聚的重要性
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-03-31 DOI: 10.1016/bs.pmbts.2024.03.011
Mansoureh Mirza Agha, Fatemeh Aziziyan, Vladimir N Uversky
{"title":"Each big journey starts with a first step: Importance of oligomerization.","authors":"Mansoureh Mirza Agha, Fatemeh Aziziyan, Vladimir N Uversky","doi":"10.1016/bs.pmbts.2024.03.011","DOIUrl":"10.1016/bs.pmbts.2024.03.011","url":null,"abstract":"<p><p>Protein oligomers, widely found in nature, have significant physiological and pathological functions. They are classified into three groups based on their function and toxicity. Significant advancements are being achieved in the development of functional oligomers, with a focus on various applications and their engineering. The antimicrobial peptides oligomers play roles in death of bacterial and cancer cells. The predominant pathogenic species in neurodegenerative disorders, as shown by recent results, are amyloid oligomers, which are the main subject of this chapter. They are generated throughout the aggregation process, serving as both intermediates in the subsequent aggregation pathways and ultimate products. Some of them may possess potent cytotoxic properties and through diverse mechanisms cause cellular impairment, and ultimately, the death of cells and disease progression. Information regarding their structure, formation mechanism, and toxicity is limited due to their inherent instability and structural variability. This chapter aims to provide a concise overview of the current knowledge regarding amyloid oligomers.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141176234","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Therapeutic approaches in proteinopathies. 蛋白质病的治疗方法。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-04-04 DOI: 10.1016/bs.pmbts.2024.03.008
Mohsen Nabi Afjadi, Bahareh Dabirmanesh, Vladimir N Uversky
{"title":"Therapeutic approaches in proteinopathies.","authors":"Mohsen Nabi Afjadi, Bahareh Dabirmanesh, Vladimir N Uversky","doi":"10.1016/bs.pmbts.2024.03.008","DOIUrl":"10.1016/bs.pmbts.2024.03.008","url":null,"abstract":"<p><p>A family of maladies known as amyloid disorders, proteinopathy, or amyloidosis, are characterized by the accumulation of abnormal protein aggregates containing cross-β-sheet amyloid fibrils in many organs and tissues. Often, proteins that have been improperly formed or folded make up these fibrils. Nowadays, most treatments for amyloid illness focus on managing symptoms rather than curing or preventing the underlying disease process. However, recent advances in our understanding of the biology of amyloid diseases have led to the development of innovative therapies that target the emergence and accumulation of amyloid fibrils. Examples of these treatments include the use of small compounds, monoclonal antibodies, gene therapy, and others. In the end, even if the majority of therapies for amyloid diseases are symptomatic, greater research into the biology behind these disorders is identifying new targets for potential therapy and paving the way for the development of more effective treatments in the future.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141176248","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Advances in CRISPR-Cas systems for gut microbiome. 用于肠道微生物组的 CRISPR-Cas 系统的进展。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-08-22 DOI: 10.1016/bs.pmbts.2024.07.008
Namra Ali, Chaitali Vora, Anshu Mathuria, Naina Kataria, Indra Mani
{"title":"Advances in CRISPR-Cas systems for gut microbiome.","authors":"Namra Ali, Chaitali Vora, Anshu Mathuria, Naina Kataria, Indra Mani","doi":"10.1016/bs.pmbts.2024.07.008","DOIUrl":"https://doi.org/10.1016/bs.pmbts.2024.07.008","url":null,"abstract":"<p><p>CRISPR-Cas technology has revolutionized microbiome research by enabling precise genetic manipulation of microbial communities. This review explores its diverse applications in gut microbiome studies, probiotic development, microbiome diagnostics, pathogen targeting, and microbial community engineering. Engineered bacteriophages and conjugative probiotics exemplify CRISPR-Cas's capability for targeted bacterial manipulation, offering promising strategies against antibiotic-resistant infections and other gut-related disorders. CRISPR-Cas systems also enhance probiotic efficacy by improving stress tolerance and colonization in the gastrointestinal tract. CRISPR-based techniques in diagnostics enable early intervention by enabling fast and sensitive pathogen identification. Furthermore, CRISPR-mediated gene editing allows tailored modification of microbial populations, mitigating risks associated with horizontal gene transfer and enhancing environmental and health outcomes. Despite its transformative potential, ethical and regulatory challenges loom large, demanding robust frameworks to guide its responsible application. This chapter highlights CRISPR-Cas's pivotal role in advancing microbiome research toward personalized medicine and microbial therapeutics while emphasizing the imperative of balanced ethical deliberations and comprehensive regulatory oversight.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142294135","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
An update on the therapeutic role of RNAi in NAFLD/NASH. RNAi在非酒精性脂肪肝/NASH中的最新治疗作用。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2023-12-29 DOI: 10.1016/bs.pmbts.2023.12.005
Hamideh Dehghan, Alireza Ghasempour, Mahboobeh Sabeti Akbar-Abad, Zahra Khademi, Mahsa Sedighi, Tannaz Jamialahmadi, Amirhossein Sahebkar
{"title":"An update on the therapeutic role of RNAi in NAFLD/NASH.","authors":"Hamideh Dehghan, Alireza Ghasempour, Mahboobeh Sabeti Akbar-Abad, Zahra Khademi, Mahsa Sedighi, Tannaz Jamialahmadi, Amirhossein Sahebkar","doi":"10.1016/bs.pmbts.2023.12.005","DOIUrl":"10.1016/bs.pmbts.2023.12.005","url":null,"abstract":"<p><p>Unhealthy lifestyles have given rise to a growing epidemic of metabolic liver diseases, including nonalcoholic fatty liver disease (NAFLD) and nonalcoholic steatohepatitis (NASH). NAFLD often occurs as a consequence of obesity, and currently, there is no FDA-approved drug for its treatment. However, therapeutic oligonucleotides, such as RNA interference (RNAi), represent a promising class of pharmacotherapy that can target previously untreatable conditions. The potential significance of RNAi in maintaining physiological homeostasis, understanding pathogenesis, and improving metabolic liver diseases, including NAFLD, is discussed in this article. We explore why NAFLD/NASH is an ideal target for therapeutic oligonucleotides and provide insights into the delivery platforms of RNAi and its therapeutic role in addressing NAFLD/NASH.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140065805","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Experimental techniques for detecting and evaluating the amyloid fibrils. 检测和评估淀粉样纤维的实验技术。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-03-31 DOI: 10.1016/bs.pmbts.2024.03.004
Farnoosh Farzam, Bahareh Dabirmanesh
{"title":"Experimental techniques for detecting and evaluating the amyloid fibrils.","authors":"Farnoosh Farzam, Bahareh Dabirmanesh","doi":"10.1016/bs.pmbts.2024.03.004","DOIUrl":"10.1016/bs.pmbts.2024.03.004","url":null,"abstract":"<p><p>Amyloid fibrils are insoluble proteins with intricate β-sheet structures associated with various human diseases, including Parkinson's, Alzheimer's, and prion diseases. Proteins can form aggregates when their structure is misfolded, resulting in highly organized amyloid fibrils or amorphous aggregates. The formation of protein aggregates is a promising research field for mitigating diseases and the pharmaceutical and food industries. It is important to monitor and minimize the appearance of aggregates in these protein products. Several methods exist to assess protein aggregation, that includes from basic investigations to advanced biophysical techniques. Physicochemical parameters such as molecular weight, conformation, structure, and dimension are examined to study aggregation. There is an urgent need to develop methods for the detection of protein aggregation and amyloid fibril formation both in vitro and in vivo. This chapter focuses on a comprehensive discussion of the methods used to characterize and evaluate aggregates and amyloid fibrils.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141176236","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Liquid-liquid phase separation as triggering factor of fibril formation. 液-液相分离是纤维形成的触发因素。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-04-04 DOI: 10.1016/bs.pmbts.2024.03.006
Fereshteh Ramezani Khorsand, Vladimir N Uversky
{"title":"Liquid-liquid phase separation as triggering factor of fibril formation.","authors":"Fereshteh Ramezani Khorsand, Vladimir N Uversky","doi":"10.1016/bs.pmbts.2024.03.006","DOIUrl":"https://doi.org/10.1016/bs.pmbts.2024.03.006","url":null,"abstract":"<p><p>Liquid-liquid phase separation (LLPS) refers to the phenomenon, where a homogeneous solution spontaneously undergoes a transition into two or more immiscible phases. Through transient weak multivalent macromolecular interactions, a homogeneous solution can spontaneously separate into two phases: one rich in biomolecules and the other poor in biomolecules. Phase separation is believed to serve as the physicochemical foundation for the formation of membrane-less organelles (MLOs) and bio-molecular condensates within cells. Moreover, numerous biological processes depend on LLPS, such as transcription, immunological response, chromatin architecture, DNA damage response, stress granule formation, viral infection, etc. Abnormalities in phase separation can lead to diseases, such as cancer, neurodegeneration, and metabolic disorders. LLPS is regulated by various factors, such as concentration of molecules undergoing LLPS, salt concentration, pH, temperature, post-translational modifications, and molecular chaperones. Recent research on LLPS of biomolecules has progressed rapidly and led to the development of databases containing information pertaining to various aspects of the biomolecule separation analysis. However, more comprehensive research is still required to fully comprehend the specific molecular mechanisms and biological effects of LLPS.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141176242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Advances in CRISPR-Cas systems for human bacterial disease. 用于人类细菌疾病的 CRISPR-Cas 系统的进展。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-08-21 DOI: 10.1016/bs.pmbts.2024.07.013
Anshu Mathuria, Chaitali Vora, Namra Ali, Indra Mani
{"title":"Advances in CRISPR-Cas systems for human bacterial disease.","authors":"Anshu Mathuria, Chaitali Vora, Namra Ali, Indra Mani","doi":"10.1016/bs.pmbts.2024.07.013","DOIUrl":"https://doi.org/10.1016/bs.pmbts.2024.07.013","url":null,"abstract":"<p><p>Prokaryotic adaptive immune systems called CRISPR-Cas systems have transformed genome editing by allowing for precise genetic alterations through targeted DNA cleavage. This system comprises CRISPR-associated genes and repeat-spacer arrays, which generate RNA molecules that guide the cleavage of invading genetic material. CRISPR-Cas is classified into Class 1 (multi-subunit effectors) and Class 2 (single multi-domain effectors). Its applications span combating antimicrobial resistance (AMR), targeting antibiotic resistance genes (ARGs), resensitizing bacteria to antibiotics, and preventing horizontal gene transfer (HGT). CRISPR-Cas3, for example, effectively degrades plasmids carrying resistance genes, providing a precise method to disarm bacteria. In the context of ESKAPE pathogens, CRISPR technology can resensitize bacteria to antibiotics by targeting specific resistance genes. Furthermore, in tuberculosis (TB) research, CRISPR-based tools enhance diagnostic accuracy and facilitate precise genetic modifications for studying Mycobacterium tuberculosis. CRISPR-based diagnostics, leveraging Cas endonucleases' collateral cleavage activity, offer highly sensitive pathogen detection. These advancements underscore CRISPR's transformative potential in addressing AMR and enhancing infectious disease management.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142294148","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Advances in the polymeric nanoparticulate delivery systems for RNA therapeutics. 用于 RNA 治疗的聚合物纳米颗粒输送系统的进展。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-01-30 DOI: 10.1016/bs.pmbts.2024.01.001
Sristi, Waleed H Almalki, Ritu Karwasra, Garima Gupta, Surender Singh, Ajay Sharma, Amirhossein Sahebkar, Prashant Kesharwani
{"title":"Advances in the polymeric nanoparticulate delivery systems for RNA therapeutics.","authors":"Sristi, Waleed H Almalki, Ritu Karwasra, Garima Gupta, Surender Singh, Ajay Sharma, Amirhossein Sahebkar, Prashant Kesharwani","doi":"10.1016/bs.pmbts.2024.01.001","DOIUrl":"10.1016/bs.pmbts.2024.01.001","url":null,"abstract":"<p><p>RNA therapeutics have emerged as potential treatments for genetic disorders, infectious diseases, and cancer. RNA delivery to target cells for efficient therapeutic applications remains challenging due to instability and poor uptake. Polymeric nanoparticulate delivery systems offer stability, protection, and controlled release. These systems shield RNA from degradation, enabling efficient uptake and extended circulation. Various polymeric nanoparticle platforms have been explored, including lipid-based nanoparticles, polymeric micelles, dendrimers, and polymer-drug conjugates. This review outlines recent breakthroughs of recent advances, design principles, characterization techniques, and performance evaluation of these delivery systems. It highlights their potential in translating preclinical studies into clinical applications. Additionally, the review discusses the application of polymeric nanoparticles in ophthalmic drug delivery, particularly for medications that dissolve poorly in water, and the progress made in siRNA-based therapies for viral infections, autoimmune diseases, and cancers. SiRNA holds great promise for precision medicine and therapeutic intervention, with the ability to target specific genes and modulate disease-associated pathways. The versatility and potency of siRNA-based drugs offer a broader scope for therapeutic intervention compared to traditional biological drugs. As research in RNA therapeutics continues to advance, these technologies hold tremendous potential to revolutionize the treatment of various diseases and improve patient outcomes.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140065804","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Pathways of amyloid fibril formation and protein aggregation. 淀粉样纤维形成和蛋白质聚集的途径。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-04-15 DOI: 10.1016/bs.pmbts.2024.03.010
Elaheh Tavili, Fatemeh Aziziyan, Bahareh Dabirmanesh
{"title":"Pathways of amyloid fibril formation and protein aggregation.","authors":"Elaheh Tavili, Fatemeh Aziziyan, Bahareh Dabirmanesh","doi":"10.1016/bs.pmbts.2024.03.010","DOIUrl":"10.1016/bs.pmbts.2024.03.010","url":null,"abstract":"<p><p>The main cause of many neurodegenerative diseases and systemic amyloidoses is protein and peptide aggregation and the formation of amyloid fibrils. The study of aggregation mechanisms, the discovery and description of aggregate structures, and a comprehensive understanding of the molecular mechanisms of amyloid formation are of great importance for the diagnostic processes at the molecular level and for the development of therapeutic strategies to counter aggregation-associated disorders. Given that understanding protein misfolding phenomena is directly related to the protein folding process, we will briefly explain the protein folding mechanism and then discuss the important factors involved in protein aggregation. In the following, we review different mechanisms of amyloid formation and finally represent the current knowledge on how amyloid fibrils are formed based on kinetic and thermodynamic factors.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141176244","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Protein aggregation: An overview. 蛋白质聚集：概述。
3区 生物学
Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-03-31 DOI: 10.1016/bs.pmbts.2024.03.007
Bahareh Dabirmanesh, Khosro Khajeh, Vladimir N Uversky
{"title":"Protein aggregation: An overview.","authors":"Bahareh Dabirmanesh, Khosro Khajeh, Vladimir N Uversky","doi":"10.1016/bs.pmbts.2024.03.007","DOIUrl":"10.1016/bs.pmbts.2024.03.007","url":null,"abstract":"<p><p>In order for an ordered protein to perform its specific function, it must have a specific molecular structure. Information about this structure is encoded in the protein's amino acid sequence. The unique functional state is achieved as a result of a specific process, known as protein folding. However, as a result of partial or complete unfolding of the polypeptide chain, proteins may misfold and aggregate, leading to the formation of various aggregated structures, such as like amyloid aggregates with the cross-β structure. A variety of cellular biological processes can be affected by protein aggregates that consume essential factors necessary for maintaining proteostasis, which leads to the proteostasis imbalance and further accumulation of protein aggregates, often resulting in age-related neurodegenerative disease progression and aging. However, in addition to their well-established pathological effects, amyloids also play various physiological roles, and many important biological processes involve such 'functional amyloids'. This chapter represents a brief overview of the protein aggregation phenomenon outlines a timeline provides of some key discoveries in this exciting field.</p>","PeriodicalId":21157,"journal":{"name":"Progress in molecular biology and translational science","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141176246","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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