Annual review of biochemistry最新文献

DLK, NMNAT2, and SARM1: Judge, Jury, and Executioner in Axon Degeneration. DLK、NMNAT2和SARM1：轴突退化中的法官、陪审团和刽子手。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-20 DOI: 10.1146/annurev-biochem-051424-045840

Flora I Hinz, Casper C Hoogenraad

{"title":"DLK, NMNAT2, and SARM1: Judge, Jury, and Executioner in Axon Degeneration.","authors":"Flora I Hinz, Casper C Hoogenraad","doi":"10.1146/annurev-biochem-051424-045840","DOIUrl":"10.1146/annurev-biochem-051424-045840","url":null,"abstract":"Axon degeneration is a tightly regulated process that plays a central role in the pathogenesis of many neurodegenerative diseases. Three core mediators, DLK (dual leucine zipper kinase), NMNAT2 (nicotinamide mononucleotide adenylyltransferase 2), and SARM1 (sterile alpha and Toll/interleukin-1 receptor motif-containing 1) form a molecular axis that orchestrates axonal self-destruction. Upon stress, DLK initiates mitogen-activated protein kinase signaling, which triggers the expression of prodegenerative genes. NMNAT2, an essential nicotinamide adenine dinucleotide biosynthetic enzyme, is rapidly depleted following injury. Loss of NMNAT2 leads to the accumulation of its substrate, nicotinamide mononucleotide, which in turn activates SARM1, a central executioner of axon degeneration. Together, these proteins constitute a coordinated signaling axis that monitors cellular stress and metabolic cues to regulate axonal integrity. In this review, we provide an overview of the biochemical and cellular mechanisms of DLK, NMNAT2, and SARM1 signaling and discuss how targeting these factors offers opportunities for therapeutic intervention in a broad range of neurodegenerative disorders.","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"595-624"},"PeriodicalIF":24.9,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147490342","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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

Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles. 单链RNA在病毒和病毒样颗粒中的包装。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-04-08 DOI: 10.1146/annurev-biochem-080525-105928

Rees F Garmann, William M Gelbart

引用次数: 0

Radical Chemistry in Metalloenzymes: Bridging Inorganic Centers and Biological Catalysis. 金属酶的自由基化学：桥接无机中心和生物催化。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-30 DOI: 10.1146/annurev-biochem-051024-013029

Maximilian Böhm, Fikret Mamedov, Gustav Berggren, Martin Högbom

{"title":"Radical Chemistry in Metalloenzymes: Bridging Inorganic Centers and Biological Catalysis.","authors":"Maximilian Böhm, Fikret Mamedov, Gustav Berggren, Martin Högbom","doi":"10.1146/annurev-biochem-051024-013029","DOIUrl":"10.1146/annurev-biochem-051024-013029","url":null,"abstract":"Radical chemistry, once deemed too reactive for biological systems, is delicately controlled within metalloenzymes to catalyze challenging chemical transformations under physiological conditions. This review explores the diverse strategies employed by metalloenzymes to generate, stabilize, and utilize highly reactive radical intermediates. We discuss amino acid-based radicals (tyrosyl, tryptophan, cysteinyl, glycyl, and DOPA), radicals derived from molecular oxygen (in heme, manganese, copper, and nonheme iron enzymes), and cofactor-based radicals (specifically adenosylcobalamin and radical S-adenosylmethionine enzymes). We devote special attention to ribonucleotide reductases as a prime example of evolutionary convergence of radical mechanisms. The interplay among redox-active cofactors, metal ions, and protein scaffolds highlights nature's ingenuity in generating, controlling, and utilizing radicals. We also discuss emerging themes and open questions, emphasizing how advances in structural and spectroscopic techniques continue to deepen our understanding of these complex and vital enzymatic processes.","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"81-114"},"PeriodicalIF":24.9,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147580343","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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

Natural Products from the Oral Microbiome. 口腔微生物群的天然产物。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-20 DOI: 10.1146/annurev-biochem-051024-050248

McKenna Loop Yao, Yitao Dai, Wenjun Zhang

引用次数: 0

The Great Escape: Protein Trafficking from the Bacterial Cytosol to the Outer Membrane. 大逃亡：蛋白质从细菌细胞质转运到外膜。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-20 DOI: 10.1146/annurev-biochem-051024-011856

William J Allen, Sophie L Williams, Ian Collinson

{"title":"The Great Escape: Protein Trafficking from the Bacterial Cytosol to the Outer Membrane.","authors":"William J Allen, Sophie L Williams, Ian Collinson","doi":"10.1146/annurev-biochem-051024-011856","DOIUrl":"10.1146/annurev-biochem-051024-011856","url":null,"abstract":"To protect their delicate, carefully curated contents from the world, bacteria encase themselves within a protective envelope made up of sugars, lipids, and proteins. Cell envelopes give bacteria their characteristic shapes, provide rigidity and mechanical stability, and form a selective antechamber-granting access only to a desirable subset of environmental substances. Yet this protective layer is a double-edged sword: Its effectiveness at keeping things out also makes it difficult for things to leave, including the proteins required to interface with the outside world and form the envelope itself. Bacteria have solved this problem by constructing an array of proteinaceous nanomachines that expend energy to selectively shuttle proteins and other building blocks to their intended destinations. Here, we present an overview of our current understanding of how these transporters work, focusing on the major, conserved machines that ferry proteins across the cell envelope throughout the domain Bacteria. The emphasis is on recent discoveries and open questions, with the hope that answering these will provide new avenues to help combat the rising threat of antimicrobial resistance and the rapidly expanding list of diseases linked to human microbiome composition.","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"431-454"},"PeriodicalIF":24.9,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147490375","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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

Cotranslational Assembly of Oligomeric Proteins. 低聚蛋白的共翻译组装。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-25 DOI: 10.1146/annurev-biochem-051024-124747

Jaime Santos, Sander J Tans, Nenad Ban, Günter Kramer, Bernd Bukau

引用次数: 0

Proteostasis Deregulation by Metabolism Drives the Hallmarks of Cancer. 代谢导致的蛋白质平衡失调驱动癌症的特征。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-04-03 DOI: 10.1146/annurev-biochem-051424-052148

Ashok R Venkitaraman

{"title":"Proteostasis Deregulation by Metabolism Drives the Hallmarks of Cancer.","authors":"Ashok R Venkitaraman","doi":"10.1146/annurev-biochem-051424-052148","DOIUrl":"10.1146/annurev-biochem-051424-052148","url":null,"abstract":"Cancer cells acquire hallmark behaviors through adaptations that extend beyond genetic and epigenetic changes. Proteostasis-the biochemical network governing protein synthesis, folding, trafficking, and degradation-is a fundamental, yet underappreciated, mediator of these adaptations that merits consideration as a hallmark-enabling mechanism. Metabolic alterations impose proteotoxic stress, globally rewire protein homeostasis, and selectively modulate key oncogenic and tumor suppressive proteins. A unifying framework is proposed wherein metabolic deregulation of proteostasis operates throughout carcinogenesis: early, by enhancing accumulation of premalignant clones bearing cancer-driving somatic mutations in response to environmental and systemic metabolic stress, and later, by buffering proteotoxic stress to sustain malignant growth in hostile tissue environments. This perspective connects cancer risk with genetic background, diet, microbiome-derived metabolites, and metabolic disease, introduces metabolic bypass of tumor suppression as an alternative to classical genetic models, and highlights the metabolism-proteostasis interface as a promising target for cancer prevention and therapy.","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"483-506"},"PeriodicalIF":24.9,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147615671","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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

The Dynamics of Chromatin Replication. 染色质复制动力学。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-20 DOI: 10.1146/annurev-biochem-082525-050024

Leonie Kollenstart, Sebastian Jespersen Charlton, Anja Groth

引用次数: 0

Cellular Repair and Removal of Protein-Damage Modifications. 细胞修复和去除蛋白质损伤修饰。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 Epub Date: 2026-03-24 DOI: 10.1146/annurev-biochem-051024-045733

Abigail K D Porter, Christina M Woo

{"title":"Cellular Repair and Removal of Protein-Damage Modifications.","authors":"Abigail K D Porter, Christina M Woo","doi":"10.1146/annurev-biochem-051024-045733","DOIUrl":"10.1146/annurev-biochem-051024-045733","url":null,"abstract":"Protein aging, stress, or metabolism can lead to the accumulation of numerous nonenzymatic chemical alterations that can threaten protein stability and function, particularly in long-lived proteins. Eukaryotic cells recognize these protein-damage events through repair and removal pathways, whose loss can lead to adverse effects and contribute to age-related disease pathogenesis. Here, we review recent advances in understanding the formation, repair, and removal mechanisms of posttranslational modifications arising from protein damage, including dehydroamino acids, early-stage glycation, isoaspartate, C-terminal cyclic imides, and C-terminal amides. We emphasize the emerging role of E3 ubiquitin ligases in facilitating the degradation of proteins bearing these modifications, highlight the approaches used to make these discoveries, and discuss the potential functions of these modifications beyond protein damage. Mounting evidence that protein-damage events influence cellular signaling and metabolism suggests the existence of vast undiscovered regulatory networks, creating opportunities to uncover tissue-specific repair mechanisms and their roles in development, aging, and stress responses across diverse biological contexts.","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"455-481"},"PeriodicalIF":24.9,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147508848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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

Lactate as a Chemical Modification on Proteins and Metabolites. 乳酸作为蛋白质和代谢物的化学修饰。

IF 24.9 1区生物学

Annual review of biochemistry Pub Date : 2026-06-01 DOI: 10.1146/annurev-biochem-051024-015746

Shuke Xiao, Andrew L Markhard, Jonathan Z Long

引用次数: 0