Sub-cellular biochemistry最新文献_第2页

Golgi Fragmentation as a Potential Link Between SARS-CoV-2 Infection and Alzheimer's Disease: Mechanisms and Implications for Neurodegeneration in Long COVID. 高尔基体碎片化是SARS-CoV-2感染与阿尔茨海默病之间的潜在联系：长COVID的神经退行性变的机制和意义

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-16833-7_19

Yanzhuang Wang, Sam Gandy

引用次数: 0

The Impact of Golgi Organization on Cell Cycle and Cancer Development. 高尔基组织对细胞周期和癌症发展的影响。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-06936-8_6

Antonino Colanzi, Inmaculada Ayala

{"title":"The Impact of Golgi Organization on Cell Cycle and Cancer Development.","authors":"Antonino Colanzi, Inmaculada Ayala","doi":"10.1007/978-3-032-06936-8_6","DOIUrl":"10.1007/978-3-032-06936-8_6","url":null,"abstract":"The Golgi complex plays a pivotal role in the secretory pathway, cell signaling, and cytoskeleton organization. In mammalian cells, it is organized as a ribbon-like structure that can undergo dynamic reorganizations, which are crucial for various cellular processes, including mitosis and cell migration. During mitosis, the Golgi complex is subjected to a tightly regulated disassembly process, essential for proper cell division, while its reformation is critical for inheritance by daughter cells. Disruption of Golgi organization has been linked to pathological conditions, including cancer, as altered organization and function can contribute to tumor progression by impacting glycosylation, cell polarity, and extracellular matrix remodeling. This chapter explores the molecular mechanisms regulating Golgi disassembly during the cell cycle and its involvement in ensuring proper cell division. Additionally, we discuss the emerging understanding of the potential role of modifications of the Golgi organization in tumor development and metastasis. Collectively, the findings presented in this chapter underscore the physiological significance of the Golgi ribbon structure and the pathological implications of its alterations in cancer progression, which could offer novel therapeutic opportunities for cancer treatment.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"109-148"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522821","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}

引用次数: 0

The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism. 单一序列的多生命：通过淀粉样蛋白多态性的功能可塑性。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-05273-5_16

Mariana Pigozzi Cali, Jim Monistrol, Fabio Strati, Janina Schiller, Rinat Indig, Ronja Markworth, Meytal Landau

{"title":"The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.","authors":"Mariana Pigozzi Cali, Jim Monistrol, Fabio Strati, Janina Schiller, Rinat Indig, Ronja Markworth, Meytal Landau","doi":"10.1007/978-3-032-05273-5_16","DOIUrl":"10.1007/978-3-032-05273-5_16","url":null,"abstract":"Amyloids play critical functional roles in biology, including microbial virulence, innate immunity, and cellular organization, broadening their traditional association with neurodegenerative and systemic diseases. This chapter explores the structural and functional plasticity of amyloids, emphasizing how a single protein sequence can adopt multiple fibrillar conformations, termed polymorphs, each with distinct biological outcomes. We synthesise recent high-resolution structural insights from cryo-EM, NMR, and microcrystallography that elucidate the polymorphic behaviour of amyloids in both pathogenic and functional contexts. Particular focus is placed on bacterial functional amyloids that stabilise biofilms and modulate host-pathogen interactions and on antimicrobial peptides that form reversible fibrils with cytotoxic or immune-stimulatory functions. We also highlight the emerging paradigm of amyloid-nucleic acid co-assemblies and their role in immune recognition, autoimmunity, and possibly the origin of life. By examining structure-function relationships across a broad evolutionary spectrum, we argue that amyloid polymorphism constitutes a general mechanism of biological regulation. Understanding how these fibrils shift between states, including cross-β, cross-α, nanotubular, or phase-separated condensates, offers insight into their dual roles in health and disease. This perspective repositions amyloids not merely as pathological end-products but as versatile, ancient scaffolds for structural adaptation and functional innovation.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"521-558"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146012233","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}

引用次数: 0

The Impact of Ageing on Fibrillar Collagens. 衰老对纤维性胶原蛋白的影响。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-05273-5_12

Elizabeth G Canty-Laird, Himadri S Gupta, Helen L Birch

{"title":"The Impact of Ageing on Fibrillar Collagens.","authors":"Elizabeth G Canty-Laird, Himadri S Gupta, Helen L Birch","doi":"10.1007/978-3-032-05273-5_12","DOIUrl":"10.1007/978-3-032-05273-5_12","url":null,"abstract":"The world population is ageing rapidly. The over-60s now outnumber the under- 5s, and 1 in 6 people will be over 60 by 2030 (WHO). Collagen is a key structural component of many tissues and organs, and although a fraction of the collagenous component of tissues is remarkably long-lived, it progressively accumulates damage over a lifetime. The capacity for new collagen synthesis and post-translational modification is altered and dysregulated during ageing. The mature crosslinks that stabilise collagenous tissues can remain stable or increase with age, whereas age-related glycation end-products can increase and affect tissue biomechanics. At the fibrillar nanoscale, changes associated with ageing and disease influence fibril deformation and stress transfer in a tissue-specific manner. Age-related loss of collagen can be caused by proteolytic degradation, but normal collagen turnover is also affected by ageing and its dysregulation is detrimental to tissue homeostasis. Age-related accumulation of senescent cells may contribute to the aberrant turnover of collagen during ageing. Finally, collagen itself may hold the key to counteracting some of the detrimental effects of ageing, with ingested hydrolysed collagen peptides demonstrating beneficial effects on skin and the musculoskeletal system.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"377-412"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146011870","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}

引用次数: 0

Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase. 肌动蛋白的结构生物学：分子组装、构象多态性和atp酶之间的相互作用。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-05273-5_4

Yuichiro Maéda, Toshiro Oda, Akihiro Narita, Yusuke Kanematsu, Mitsusada Iwasa, Shuichi Takeda

{"title":"Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase.","authors":"Yuichiro Maéda, Toshiro Oda, Akihiro Narita, Yusuke Kanematsu, Mitsusada Iwasa, Shuichi Takeda","doi":"10.1007/978-3-032-05273-5_4","DOIUrl":"10.1007/978-3-032-05273-5_4","url":null,"abstract":"Actin was first identified as a major muscle protein with two key activities: polymerization and ATPase. Although the significance of these activities in muscle contraction was unclear, subsequent cell biological studies revealed that actin is abundant also in non-muscle cells, where it drives dynamic remodeling through ATP-dependent treadmilling. Biochemical studies revealed that the polymerization coupled with ATP hydrolysis produces two distinct F-actin states: a stable ADP-Pi state and an unstable ADP state. The transition between the ADP-Pi and ADP states (i.e., Pi release) likely generates the free energy that drives treadmilling.In this chapter, we introduce our structural biological studies of these states and the mechanisms underlying their formation. Our F-actin model showed that polymerization induces a rotation between its two rigid domains, shifting actin from a twisted G-form to a flat F-form. We also resolved the cryo-EM structure of cofilin-decorated F-actin, in which actin adopts a distinct C-form. Analysis of PDB data classified actin structures into four conformations: G-, F-, C-, and O-forms, each linked to specific functions-G-form for nucleotide exchange, F-form for ATP hydrolysis, and C-form for filament severing. High-resolution F-form structures further elucidated the ATP hydrolysis pathway and the basis for the stability of the ADP-Pi state.Despite these advances, key questions remain. Although the global structure of F-form actin is identical across nucleotide states, its properties differ: ATP/ADP-Pi states are stable and cofilin-resistant, whereas the ADP state is prone to depolymerization and cofilin-mediated severing. We suggest that each state should be characterized by the distinct nature of conformational fluctuations from F-form back to G-form.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"81-112"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146011843","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}

引用次数: 0

Aquaphotomics: A Novel Approach to Investigating Water's Role in Cell Membrane Hydration. 水相学：研究水在细胞膜水合作用中的新方法。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-24159-7_2

Roumiana Tsenkova, Zoltan Kovacs, Takaharu Sasaki, Ilina Iordanova

{"title":"Aquaphotomics: A Novel Approach to Investigating Water's Role in Cell Membrane Hydration.","authors":"Roumiana Tsenkova, Zoltan Kovacs, Takaharu Sasaki, Ilina Iordanova","doi":"10.1007/978-3-032-24159-7_2","DOIUrl":"https://doi.org/10.1007/978-3-032-24159-7_2","url":null,"abstract":"Aquaphotomics has evolved into a mature scientific framework that explores water as a molecular mirror of biological function. Since its introduction, the field has expanded in methodology, applications, and theoretical scope. Water at the cell membrane interface plays an essential role in maintaining structure, fluidity, and function through the formation of hydration shells. By analyzing specific water absorbance patterns based on wavelengths showing the highest optical density variations for the respective system under perturbations, known as water matrix coordinates (WAMACs), aquaphotomics reveals how different water molecular species respond to biochemical and biophysical changes in membranes. This updated edition introduces the theoretical and spectral foundations of aquaphotomics, its application in studying membrane hydration, and its integration with chemometric tools to characterize functional water dynamics. Aquaphotomics offers a new paradigm for understanding water's active role in biological systems and opens possibilities for advances in membrane biophysics, diagnostics, and hydration-focused biomedical research. It integrates recent advances in short-wave NIR spectroscopy, aquagram-based diagnostics, and biomedical and agricultural applications that link cellular water structure with health, stress, and system stability. It presents new insights from modern clinical, agricultural, and quantum-biological research, while maintaining aquaphotomics' original vision: to understand water-light interaction as a holistic biomarker of system functionality.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"116 ","pages":"19-42"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148991265","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}

引用次数: 0

Structural and Functional Elements of the Epidermal Appendages in Birds and Reptiles: Conformations and Modes of Assembly of the Constituent β-Filaments and Keratin Intermediate Filaments (IF). 鸟类和爬行动物表皮附属物的结构和功能要素：组成β-丝和角蛋白中间丝（IF）的构象和组装模式。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-05273-5_5

David A D Parry

{"title":"Structural and Functional Elements of the Epidermal Appendages in Birds and Reptiles: Conformations and Modes of Assembly of the Constituent β-Filaments and Keratin Intermediate Filaments (IF).","authors":"David A D Parry","doi":"10.1007/978-3-032-05273-5_5","DOIUrl":"10.1007/978-3-032-05273-5_5","url":null,"abstract":"Much is now known about the structures of the β-filaments and the intermediate filaments that together constitute the bulk of the avian and reptilian (sauropsid) appendages (claws, scales, feathers and beaks). New sequence data from the Rhynchocephalia (the tuatara), the last branch of the phylogenetic classification of the sauropsids to be studied, has confirmed that all members of the sauropsids are based on common structures. In addition, an examination of the sequence data has revealed that the β-filaments in the lepidosaurs (lizards, snakes and tuatara) contain a chain that is likely to be a structural component of two separate filaments, thereby providing a unique feature that could facilitate ordered filament aggregation. Similarly, a Type II IF chain (K80) in lizards appears capable of forming an interaction in inter-filament space that would link adjacent IF through tail-tail interactions. A Type II IF chain in zebra finch (K78LT) also seems likely to play a similar role. More details of the surface lattice structure in the IF have also been obtained, as has information on the lateral packing of the protofilaments in the IF. Consequently, an increasingly detailed picture has emerged of the structure and assembly of the filamentous structures that comprise the corneous appendages in the sauropsids.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"113-142"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146011675","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}

引用次数: 0

The Epigenetic Angle in the Precision Medicine Era for Blood Disorder Advancements. 精准医学时代血液疾病进展的表观遗传学角度。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-08530-6_6

Nadia M Hamdy, Ahmed I Abulsoud, Nehal I Rizk, Tohada M Al-Noshokaty, Mohamed Bakr Zaki, Ahmed S Sultan, Ahmed S Doghish

{"title":"The Epigenetic Angle in the Precision Medicine Era for Blood Disorder Advancements.","authors":"Nadia M Hamdy, Ahmed I Abulsoud, Nehal I Rizk, Tohada M Al-Noshokaty, Mohamed Bakr Zaki, Ahmed S Sultan, Ahmed S Doghish","doi":"10.1007/978-3-032-08530-6_6","DOIUrl":"10.1007/978-3-032-08530-6_6","url":null,"abstract":"This work examined the integration of epigenetics and precision medicine in the management of various blood disorders, including anemias, antiphospholipid syndrome, hemochromatosis, hemophilia, leukemia, lymphoma, multiple myeloma, porphyria, thalassemia, thrombocytopenia, thrombocytosis, polycythemia, von Willebrand disease, and coagulopathy. It begins with an overview of key concepts and the significance of precision medicine in treating blood diseases, supported by current statistics. The role of noncoding RNAs (ncRNAs) is highlighted, detailing their mechanisms of action and clinical implications as potential biomarkers and therapeutic targets. Additionally, the chapter explores natural products used in personalized medicine, examining their sources, mechanisms, and successful case studies in blood disorders. A comprehensive review of recent clinical trials provides insights into the impact of innovative therapies and FDA approvals on treatment protocols, emphasizing the importance of combination therapies. Future directions address emerging research technologies such as clustered regularly interspaced short palindromic repeats (CRISPR) and ethical considerations surrounding genetic testing and patient consent. The synthesis of findings underscores the contributions of epigenetics and precision medicine to blood disease treatment, advocating for interdisciplinary research and ongoing education to enhance patient care and outcomes.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"114 ","pages":"299-353"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889588","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}

引用次数: 0

Revealing Golgi Architecture: Novel Insights Through Light Microscopy. 揭示高尔基建筑：通过光学显微镜的新见解。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-06936-8_3

Divyanshu Mahajan, Lei Lu

{"title":"Revealing Golgi Architecture: Novel Insights Through Light Microscopy.","authors":"Divyanshu Mahajan, Lei Lu","doi":"10.1007/978-3-032-06936-8_3","DOIUrl":"10.1007/978-3-032-06936-8_3","url":null,"abstract":"The Golgi is a eukaryotic organelle that modifies, sorts, and transports proteins and lipids to their destinations. In mammals, the Golgi is a complex network of interconnected stacks, with each stack made up of closely packed flat membrane sacs called cisternae. The Golgi remains a poorly understood organelle, fraught with controversies despite decades of research. The challenge of visually resolving the cisternal organization of the Golgi under light or electron microscopy contributes to its enigmatic nature. We have developed new imaging methods, including GLIM, en face averaging, and side averaging, to resolve the nocodazole-induced Golgi ministacks. These tools provide new insights into the organization and functions of the Golgi. They enabled us to rapidly and quantitatively investigate cisternal Golgi organization and intra-Golgi transport of secretory cargos. New insights have been revealed about the spatial distribution of Golgi proteins involved in processing and trafficking, the differential partitioning of secretory cargos within cisternae based on their sizes, and the specific Golgi exit sites for constitutive versus signal-dependent secretory cargos. Additionally, the intra-Golgi transport kinetic data acquired from these tools provide a basis for evaluating different intra-Golgi transport models.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"43-65"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522851","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}

引用次数: 0

The Neuronal Golgi Network and Its Acolytes. 神经元高尔基网络及其助手。

Sub-cellular biochemistry Pub Date : 2026-01-01 DOI: 10.1007/978-3-032-06936-8_7

Alexandre Varangot, Cyril Hanus

引用次数: 0