{"title":"Plant Golgi and GECCO: The Universality of ER-Golgi Interface.","authors":"Yoko Ito, Tomohiro Uemura","doi":"10.1007/978-3-032-06936-8_10","DOIUrl":"10.1007/978-3-032-06936-8_10","url":null,"abstract":"<p><p>In spite of its highly conserved molecular constituents, the Golgi apparatus shows diverse morphologies depending on the organism and cell type. In particular, in plant cells, the distribution and dynamics of the Golgi differ considerably from that seen in their mammalian or yeast counterparts. The architecture of the ER-Golgi interface, the first transfer station of the whole secretory traffic, has also been thought to differ between plants and the better-known mammalian system that possesses the ER-Golgi intermediate compartment (ERGIC). However, detailed observations with plant cells gave rise to the identification of GECCO, the ER-Golgi intermediate that is likely to correspond to the mammalian ERGIC. The existence of compartments that are seemingly different, but still share common features across multiple eukaryotic kingdoms, highlights the universality of the ER-Golgi interface. In this chapter, after summarizing the characteristics of the plant Golgi, we will introduce the findings about GECCO by comparing plants with mammals and yeast. In addition, we will discuss the universal identity of the ER-Golgi intermediate compartments in order to transcend the morphological diversity for a deeper understanding of the ER-Golgi interface.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"110 ","pages":"245-265"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522886","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":"Fibrin as a Versatile Fibrous Biopolymer.","authors":"John W Weisel, Rustem I Litvinov","doi":"10.1007/978-3-032-05273-5_13","DOIUrl":"10.1007/978-3-032-05273-5_13","url":null,"abstract":"<p><p>Fibrin is a fibrous biopolymer that plays a crucial role in hemostasis, thrombosis, wound healing, and various other biological functions and pathological conditions. The X-ray crystallographic structure of fibrinogen, along with computational reconstructions of missing regions and extensive biochemical and biophysical studies, has provided significant insights into the molecular mechanisms of fibrin formation, its structural organization, and its biological and mechanical properties. Upon cleavage of fibrinopeptides by thrombin, the blood protein fibrinogen is converted into fibrin monomers, which then interact through \"knobs\" exposed by the removal of fibrinopeptides in the central region and \"holes\" that are constitutively available at the ends of the molecules. The result is half-staggered, double-stranded oligomers that elongate into protofibrils, which then aggregate laterally to form fibers, and branch to create a three-dimensional network. Much has been learned about how the structure of fibrin contributes to the mechanical properties of the clot, including changes in fiber orientation, stretching, buckling, and the forced unfolding of molecular domains. Recent research into the mechanical stability of fibrin has enhanced our understanding of its rupture resistance, which is relevant to thrombotic embolization and mechanical thrombectomy. The fibrinolytic system, in which plasminogen, along with tissue-type plasminogen activator, binds to fibrin and is activated to plasmin, leads to the digestion of fibrin at specific lysine residues. Fibrin has been utilized in hemostatic fibrin sealants and as a biomaterial in tissue engineering and regenerative medicine. Despite significant advances in our understanding of these interconnected processes, much remains unknown about the molecular mechanisms underlying fibrin's biological functions, particularly concerning the molecular origins of its mechanical properties and the more complex structure and properties of hemostatic clots and pathological thrombi and their clinical implications.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"413-473"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146012315","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":"Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.","authors":"Christopher W Wood, Guto G Rhys, Evangelia Notari","doi":"10.1007/978-3-032-05273-5_1","DOIUrl":"10.1007/978-3-032-05273-5_1","url":null,"abstract":"<p><p>The coiled coil is one of the most widespread and versatile protein folding motifs and is involved in a vast array of biological functions. The study and design of these assemblies have been shaped by the development of specialised computational tools. This review charts the landscape of these in silico methods, beginning with the foundational sequence-based algorithms for coiled-coil prediction and classification, before moving to the powerful parametric methods that enable the generation of idealised, atomic-resolution structural models. We argue that while indispensable, these tools can promote a view of coiled coils as static, singular structures. Challenging this, we highlight the structural plasticity of coiled coils, the remarkable and increasingly evident ability of these assemblies to adopt multiple distinct conformations and dynamically switch between states. To understand the energetic and mechanistic principles governing this complex behaviour, we explore the crucial role of molecular dynamics (MD) simulations in providing atomistic insights that are inaccessible to static modelling. Finally, we look forward, considering how the next generation of coiled-coil bioinformatics must evolve to address these challenges to take advantage of the opportunities presented by the current explosion in genomic sequence data and the proliferation of AI-predicted protein structures.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"1-34"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146011631","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":"Designability of α-Helical Protein Filaments.","authors":"Abhinaba Das, Vincent Conticello","doi":"10.1007/978-3-032-05273-5_15","DOIUrl":"10.1007/978-3-032-05273-5_15","url":null,"abstract":"<p><p>Helix-helix interactions are mediated through highly designable interfaces within tertiary and quaternary structures of proteins and protein assemblies. The structural regularity of these interfaces suggests that ordered self-assembled structures could be constructed from implementation of these interactions between appropriately designed helical protomers. This review summarizes the current understanding of helix-helix interactions within different classes of naturally occurring α-helical protein filaments. The implications of this structural information for the de novo design of synthetic filamentous nanomaterials will be discussed with reference to examples in which these principles have been successfully implemented. A specific case study will focus on the designability of cross-α helical filaments, a recently discovered structural class in which the helical protomers are arranged in a perpendicular orientation with respect to the protofilament axis. This discussion will include an evaluation of the frequency of occurrence of cross-α interfaces in the PDB, the effectiveness of structural prediction from sequence information, and the potential for de novo design of interfaces that promote cross-α interactions.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"493-520"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146012383","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":"Golgi Membrane-Associated Degradation (GOMED), a New Intracellular Proteolysis Mechanism.","authors":"Shigeomi Shimizu, Shinya Honda, Satoru Torii, Satoko Arakawa, Masatsune Tsujioka, Hirofumi Yamaguchi, Hajime Tajima Sakurai","doi":"10.1007/978-3-032-16833-7_14","DOIUrl":"10.1007/978-3-032-16833-7_14","url":null,"abstract":"<p><p>The Golgi apparatus is a crucial organelle that is involved in various cellular processes, including cellular secretion, and is primarily responsible for the modification, sorting, and transport of proteins and lipids. However, recently, we discovered a novel Golgi function, namely, Golgi membrane-associated degradation (GOMED). GOMED is a cellular function in which the trans-Golgi membrane undergoes deformation and becomes spherical, breaking down proteins and lipids that have been internalized. This process is conserved from yeast to mammalian cells. GOMED primarily plays a role in the quality control of hormones, cytokines, and cell membrane receptors that pass through the Golgi apparatus, and is crucial for maintaining the normal function of pancreatic β cell, neurons, and intestinal epithelial cells. Therefore, abnormalities in GOMED can lead to neurodegenerative diseases and inflammatory bowel diseases.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"111 ","pages":"331-350"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146259606","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":"Applications of Carbonic Anhydrase Inhibitors in Neurological Disorders, Mechanisms and Therapeutic Potential.","authors":"Neera Raghav, Rashmi Pundeer","doi":"10.1007/978-3-032-23172-7_7","DOIUrl":"10.1007/978-3-032-23172-7_7","url":null,"abstract":"<p><p>Eleven carbonic anhydrase isoforms are known to be present in different parts of the central nervous system and are involved in signal transduction, cerebral fluid homeostasis, bicarbonate generation, respiratory response to carbon dioxide, seizure activity, and fluid and ion compartmentation. Therefore, carbonic anhydrase inhibitors profoundly influence several neurological therapeutic approaches. Many CAIs, such as acetazolamide, zonisamide, topiramate, lacosamide, and levetiracetam are successfully used in cerebral pathologies. To improve the efficacy, selectivity, and to minimize the side effects, the bespoke medications are engineered using \"one-tail approach\" and their pharmacological mechanisms of actions are elucidated.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"123 ","pages":"147-162"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147821041","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":"Physics and Life at Interfaces: Momentum Conservation and Albert Einstein's Thermodynamics in 2D.","authors":"Matthias F Schneider, Andreas Gruhn","doi":"10.1007/978-3-032-24159-7_9","DOIUrl":"https://doi.org/10.1007/978-3-032-24159-7_9","url":null,"abstract":"<p><p>The great power of biomolecules may be their capability to organize water into 2D-interfaces and control their physical state. Just as water, these interfaces are hence omnipresent in the living system and are here considered to create the platform that the physics of life is taking place in.We describe how fundamental physical principles-the laws of thermodynamics and momentum conservation-applied within these interfaces will lead to the propagation of pulses along the interfaces. Together with the realization that all physical properties of the hydrated interface are thermodynamic (e.g., the compressibility, conductivity, binding properties, etc.) and have as such a state diagram, pulses can become nonlinear with exciting new properties arising.Finally, I would like to outline how Ling's association induction hypothesis arrives from Einstein's approach to thermodynamics, which became only clear to me through discussions with Luis Bagatolli.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"116 ","pages":"193-202"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148991276","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}
Nadia M Hamdy, Ahmed S Sultan, John Frederick Kennedy
{"title":"Correction to: From (Epi)genetics-to-Precision (E2P): Non-protein Coding RNAs (ncRNAs) a Step-toward Precision Medicine.","authors":"Nadia M Hamdy, Ahmed S Sultan, John Frederick Kennedy","doi":"10.1007/978-3-032-08530-6_9","DOIUrl":"https://doi.org/10.1007/978-3-032-08530-6_9","url":null,"abstract":"","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"114 ","pages":"C1"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147356538","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}
Mohamed E Abdel Aziz, Heba Momtaz, Basel Mohamed, Mariam Amr, Alhassan Soliman Wadan, Shaimaa Abdel-Ghany, Borros Arneth, Hussein Sabit
{"title":"Mapping Non-Coding Epimutations in Breast Cancer: Advancing Epigenetics Towards Precision Medicine.","authors":"Mohamed E Abdel Aziz, Heba Momtaz, Basel Mohamed, Mariam Amr, Alhassan Soliman Wadan, Shaimaa Abdel-Ghany, Borros Arneth, Hussein Sabit","doi":"10.1007/978-3-032-08530-6_3","DOIUrl":"10.1007/978-3-032-08530-6_3","url":null,"abstract":"<p><p>Breast cancer remains a leading cause of cancer-related morbidity and mortality in women worldwide. While extensive research has focused on mutations in protein-coding genes, emerging evidence underscores the pivotal role of the noncoding genome-including long noncoding RNAs (lncRNAs), microRNAs (miRNAs), circular RNAs (circRNAs), and piwi-interacting RNAs (piRNAs)-in tumorigenesis, progression, and therapeutic resistance. These noncoding RNAs (ncRNAs) are regulated through diverse epigenetic mechanisms such as DNA methylation, histone modifications, and N6-methyladenosine (m6A) RNA methylation. Aberrant epigenetic modifications in noncoding regions can silence tumor suppressors or activate oncogenes, thereby reprogramming cellular behavior and contributing to breast cancer heterogeneity. High-throughput techniques like whole-genome bisulfite sequencing (WGBS), ATAC-seq, and ChIP-seq have facilitated the discovery of noncoding epimutations with clinical significance. Moreover, ncRNA-based epigenetic alterations are increasingly explored as diagnostic biomarkers, prognostic indicators, and therapeutic targets, particularly in subtype-specific contexts such as triple-negative breast cancer (TNBC) and HER2-positive tumors. Despite advances, challenges remain in interpreting functional noncoding elements and translating findings into clinical interventions. This chapter provides a comprehensive examination of the noncoding epigenome in breast cancer, highlighting current methodologies, molecular mechanisms, and translational potential while also identifying future directions needed to leverage noncoding epigenetics for personalized cancer care.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"114 ","pages":"123-182"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145889433","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":"Insights into the Structure of Intermediate Filaments.","authors":"Matthias Eibauer, Ohad Medalia","doi":"10.1007/978-3-032-05273-5_6","DOIUrl":"10.1007/978-3-032-05273-5_6","url":null,"abstract":"<p><p>Intermediate filaments (IFs) are central to the mechanical integrity of metazoan cells and play critical roles in various fundamental cellular and multicellular processes, including cell motility, signal transduction, and wound healing. To perform their functions, IF proteins self-assemble into nanoscale biopolymers, each exhibiting unique properties that are finely tuned to their specific roles across different tissue types. However, the 3D structure of IFs has remained largely unresolved due to their intrinsic flexibility and polymorphism. This chapter reviews recent advances in the structural analysis of IFs, with a focus on vimentin IFs (VIFs), which are featuring a helical tube with a central luminal fiber. We discuss how AlphaFold-based modeling, chemical cross-linking data, and cryo-electron microscopy (cryo-EM) reconstructions have been integrated to generate a detailed structural model of VIFs, highlighting key features such as the helical symmetry of the filaments and the nature of the luminal fiber. Additionally, we explore potential sources of IF polymorphism and their implications for the analysis of IF structures.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"113 ","pages":"143-161"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146012373","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}