Sub-cellular biochemistry最新文献_第6页

Oligomerization of Monoamine Transporters. 单胺转运体的寡聚化。

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-58843-3_7

Arnav Paul, Diwakar Shukla

引用次数: 0

Role of Vitamin B in Healthy Ageing and Disease. 维生素B在健康衰老和疾病中的作用。

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-66768-8_12

Kathleen Mikkelsen, Maria Trapali, Vasso Apostolopoulos

引用次数: 0

Nucleic Acid Packaging in Viruses. 病毒中的核酸包装。

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-65187-8_13

María I Daudén, Mar Pérez-Ruiz, José L Carrascosa, Ana Cuervo

引用次数: 0

Maturation of Viruses. 病毒的成熟

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-65187-8_14

Gabriela N Condezo, Carmen San Martín

引用次数: 0

Viral Genomic DNA Packaging Machinery. 病毒基因 DNA 包装机械

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-58843-3_9

Dorothy E D P Hawkins, Owen C Godwin, Alfred A Antson

{"title":"Viral Genomic DNA Packaging Machinery.","authors":"Dorothy E D P Hawkins, Owen C Godwin, Alfred A Antson","doi":"10.1007/978-3-031-58843-3_9","DOIUrl":"10.1007/978-3-031-58843-3_9","url":null,"abstract":"Tailed double-stranded DNA bacteriophage employs a protein terminase motor to package their genome into a preformed protein shell-a system shared with eukaryotic dsDNA viruses such as herpesviruses. DNA packaging motor proteins represent excellent targets for antiviral therapy, with Letermovir, which binds Cytomegalovirus terminase, already licensed as an effective prophylaxis. In the realm of bacterial viruses, these DNA packaging motors comprise three protein constituents: the portal protein, small terminase and large terminase. The portal protein guards the passage of DNA into the preformed protein shell and acts as a protein interaction hub throughout viral assembly. Small terminase recognises the viral DNA and recruits large terminase, which in turn pumps DNA in an ATP-dependent manner. Large terminase also cleaves DNA at the termination of packaging. Multiple high-resolution structures of each component have been resolved for different phages, but it is only more recently that the field has moved towards cryo-EM reconstructions of protein complexes. In conjunction with highly informative single-particle studies of packaging kinetics, these structures have begun to inspire models for the packaging process and its place among other DNA machines.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"104 ","pages":"181-205"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7617512/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141499036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structure and Dynamics of Type 4a Pili and Type 2 Secretion System Endopili. 4a 型纤毛器和 2 型分泌系统内纤毛器的结构和动力学。

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-58843-3_21

Nadia Izadi-Pruneyre, Yasaman Karami, Michael Nilges

{"title":"Structure and Dynamics of Type 4a Pili and Type 2 Secretion System Endopili.","authors":"Nadia Izadi-Pruneyre, Yasaman Karami, Michael Nilges","doi":"10.1007/978-3-031-58843-3_21","DOIUrl":"10.1007/978-3-031-58843-3_21","url":null,"abstract":"Within the highly diverse type four filament (TFF or T4F) superfamily, the machineries of type IVa pili (T4aP) and the type 2 secretion system (T2SS) in diderm bacteria exhibit a substantial sequence similarity despite divergent functions and distinct appearances: T4aP can extend micrometers beyond the outer membrane, whereas the endopili in the T2SS are restricted to the periplasm. The determination of the structure of individual components and entire filaments is crucial to understand how their structure enables them to serve different functions. However, the dynamics of these filaments poses a challenge for their high-resolution structure determination. This review presents different approaches that have been used to study the structure and dynamics of T4aP and T2SS endopili by means of integrative structural biology, cryo-electron microscopy (cryo-EM), and molecular dynamics simulations. Their conserved features and differences are presented. The non-helical stretch in the long-conserved N-terminal helix which is characteristic of all members of the TFF and the impact of calcium on structure, function, and dynamics of these filaments are discussed in detail.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"104 ","pages":"549-563"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141499024","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 Copper Efflux Regulator (CueR). 铜外排调节器（CueR）。

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-58843-3_2

Yangbo Hu, Bin Liu

引用次数: 0

Oligomeric Structure of Yeast and Other Invertases Governs Specificity. 酵母和其他转化酶的低聚物结构决定其特异性

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-58843-3_19

Elena Jiménez-Ortega, Julia Sanz-Aparicio

{"title":"Oligomeric Structure of Yeast and Other Invertases Governs Specificity.","authors":"Elena Jiménez-Ortega, Julia Sanz-Aparicio","doi":"10.1007/978-3-031-58843-3_19","DOIUrl":"https://doi.org/10.1007/978-3-031-58843-3_19","url":null,"abstract":"Invertases, or β-fructofuranosidases, are metabolic enzymes widely distributed among plants and microorganisms that hydrolyze sucrose and release fructose from various substrates. Invertase was one of the earliest discovered enzymes, first investigated in the mid-nineteenth century, becoming a classical model used in the primary biochemical studies on protein synthesis, activity, and the secretion of glycoproteins. However, it was not until 20 years ago that a member of this family of enzymes was structurally characterized, showing a bimodular arrangement with a β-propeller catalytic domain, and a β-sandwich domain with unknown function. Since then, many studies on related plant and fungal enzymes have revealed them as basically monomeric. By contrast, all yeast enzymes in this family that have been characterized so far have shown sophisticated oligomeric structures mediated by the non-catalytic domain, which is also involved in substrate binding, and how this assembly determines the particular specificity of each enzyme. In this chapter, we will review the available structures of yeast invertases to elucidate the mechanism regulating oligomer formation and compare them with other reported dimeric invertases in which the oligomeric assembly has no apparent functional implications. In addition, recent work on a new family of invertases with absolute specificity for the α-(1,2)-bond of sucrose found in cyanobacteria and plant invertases is highlighted.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"104 ","pages":"503-530"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141499021","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

NAD⁺ Boosting Strategies. NAD+ 增强策略

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-66768-8_4

Jared Rice, Sofie Lautrup, Evandro F Fang

{"title":"NAD+ Boosting Strategies.","authors":"Jared Rice, Sofie Lautrup, Evandro F Fang","doi":"10.1007/978-3-031-66768-8_4","DOIUrl":"https://doi.org/10.1007/978-3-031-66768-8_4","url":null,"abstract":"Nicotinamide adenine dinucleotide (oxidized form, NAD+) serves as a co-substrate and co-enzyme in cells to execute its key roles in cell signalling pathways and energetic metabolism, arbitrating cell survival and death. It was discovered in 1906 by Arthur Harden and William John Young in yeast extract which could accelerate alcohol fermentation. NAD acts as an electron acceptor and cofactor throughout the processes of glycolysis, Tricarboxylic Acid Cycle (TCA), β oxidation, and oxidative phosphorylation (OXPHOS). NAD has two forms: NAD+ and NADH. NAD+ is the oxidising coenzyme that is reduced when it picks up electrons. NAD+ levels steadily decline with age, resulting in an increase in vulnerability to chronic illness and perturbed cellular metabolism. Boosting NAD+ levels in various model organisms have resulted in improvements in healthspan and lifespan extension. These results have prompted a search for means by which NAD+ levels in the body can be augmented by both internal and external means. The aim of this chapter is to provide an overview of NAD+, appraise clinical evidence of its importance and success in potentially extending health- and lifespan, as well as to explore NAD+ boosting strategies.","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"107 ","pages":"63-90"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142847754","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

Theoretical Studies on Assembly, Physical Stability, and Dynamics of Viruses. 病毒组装、物理稳定性和动力学的理论研究。

Sub-cellular biochemistry Pub Date : 2024-01-01 DOI: 10.1007/978-3-031-65187-8_19

Antoni Luque, David Reguera

引用次数: 0