发布求助
文献互助 智能选刊 最新文献

Annual review of biochemistry最新文献

筛选
英文 中文
Driving E3 Ligase Substrate Specificity for Targeted Protein Degradation: Lessons from Nature and the Laboratory. 驱动E3连接酶底物特异性靶向蛋白降解:从自然界和实验室的经验教训。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 Epub Date: 2022-03-23 DOI: 10.1146/annurev-biochem-032620-104421
Angus D Cowan, Alessio Ciulli
{"title":"Driving E3 Ligase Substrate Specificity for Targeted Protein Degradation: Lessons from Nature and the Laboratory.","authors":"Angus D Cowan,&nbsp;Alessio Ciulli","doi":"10.1146/annurev-biochem-032620-104421","DOIUrl":"https://doi.org/10.1146/annurev-biochem-032620-104421","url":null,"abstract":"<p><p>Methods to direct the degradation of protein targets with proximity-inducing molecules that coopt the cellular degradation machinery are advancing in leaps and bounds, and diverse modalities are emerging. The most used and well-studied approach is to hijack E3 ligases of the ubiquitin-proteasome system. E3 ligases use specific molecular recognition to determine which proteins in the cell are ubiquitinated and degraded. This review focuses on the structural determinants of E3 ligase recruitment of natural substrates and neo-substrates obtained through monovalent molecular glues and bivalent proteolysis-targeting chimeras. We use structures to illustrate the different types of substrate recognition and assess the basis for neo-protein-protein interactions in ternary complex structures. The emerging structural and mechanistic complexity is reflective of the diverse physiological roles of protein ubiquitination. This molecular insight is also guiding the application of structure-based design approaches to the development of new and existing degraders as chemical tools and therapeutics.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"295-319"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40316865","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: 26
Sensory TRP Channels in Three Dimensions. 三维感官 TRP 通道
IF 12.1 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 Epub Date: 2022-03-14 DOI: 10.1146/annurev-biochem-032620-105738
Melinda M Diver, John V Lin King, David Julius, Yifan Cheng
{"title":"Sensory TRP Channels in Three Dimensions.","authors":"Melinda M Diver, John V Lin King, David Julius, Yifan Cheng","doi":"10.1146/annurev-biochem-032620-105738","DOIUrl":"10.1146/annurev-biochem-032620-105738","url":null,"abstract":"<p><p>Transient receptor potential (TRP) ion channels are sophisticated signaling machines that detect a wide variety of environmental and physiological signals. Every cell in the body expresses one or more members of the extended TRP channel family, which consists of over 30 subtypes, each likely possessing distinct pharmacological, biophysical, and/or structural attributes. While the function of some TRP subtypes remains enigmatic, those involved in sensory signaling are perhaps best characterized and have served as models for understanding how these excitatory ion channels serve as polymodal signal integrators. With the recent resolution revolution in cryo-electron microscopy, these and other TRP channel subtypes are now yielding their secrets to detailed atomic analysis, which is beginning to reveal structural underpinnings of stimulus detection and gating, ion permeation, and allosteric mechanisms governing signal integration. These insights are providing a framework for designing and evaluating modality-specific pharmacological agents for treating sensory and other TRP channel-associated disorders.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"91 ","pages":"629-649"},"PeriodicalIF":12.1,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9233036/pdf/nihms-1809634.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9702300","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The Purinosome: A Case Study for a Mammalian Metabolon. 嘌呤酶:哺乳动物代谢物的案例研究。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 DOI: 10.1146/annurev-biochem-032620-105728
Anthony M Pedley, Vidhi Pareek, Stephen J Benkovic
{"title":"The Purinosome: A Case Study for a Mammalian Metabolon.","authors":"Anthony M Pedley,&nbsp;Vidhi Pareek,&nbsp;Stephen J Benkovic","doi":"10.1146/annurev-biochem-032620-105728","DOIUrl":"https://doi.org/10.1146/annurev-biochem-032620-105728","url":null,"abstract":"<p><p>Over the past fifteen years, we have unveiled a new mechanism by which cells achieve greater efficiency in de novo purine biosynthesis. This mechanism relies on the compartmentalization of de novo purine biosynthetic enzymes into a dynamic complex called the purinosome. In this review, we highlight our current understanding of the purinosome with emphasis on its biophysical properties and function and on the cellular mechanisms that regulate its assembly. We propose a model for functional purinosomes in which they consist of at least ten enzymes that localize near mitochondria and carry out de novo purine biosynthesis by metabolic channeling. We conclude by discussing challenges and opportunities associated with studying the purinosome and analogous metabolons.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"91 ","pages":"89-106"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9531488/pdf/nihms-1837650.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9701464","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 15
Better, Faster, Cheaper: Recent Advances in Cryo-Electron Microscopy. 更好，更快，更便宜:冷冻电子显微镜的最新进展。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 DOI: 10.1146/annurev-biochem-032620-110705
Eugene Y D Chua, Joshua H Mendez, Micah Rapp, Serban L Ilca, Yong Zi Tan, Kashyap Maruthi, Huihui Kuang, Christina M Zimanyi, Anchi Cheng, Edward T Eng, Alex J Noble, Clinton S Potter, Bridget Carragher
{"title":"Better, Faster, Cheaper: Recent Advances in Cryo-Electron Microscopy.","authors":"Eugene Y D Chua,&nbsp;Joshua H Mendez,&nbsp;Micah Rapp,&nbsp;Serban L Ilca,&nbsp;Yong Zi Tan,&nbsp;Kashyap Maruthi,&nbsp;Huihui Kuang,&nbsp;Christina M Zimanyi,&nbsp;Anchi Cheng,&nbsp;Edward T Eng,&nbsp;Alex J Noble,&nbsp;Clinton S Potter,&nbsp;Bridget Carragher","doi":"10.1146/annurev-biochem-032620-110705","DOIUrl":"https://doi.org/10.1146/annurev-biochem-032620-110705","url":null,"abstract":"<p><p>Cryo-electron microscopy (cryo-EM) continues its remarkable growth as a method for visualizing biological objects, which has been driven by advances across the entire pipeline. Developments in both single-particle analysis and in situ tomography have enabled more structures to be imaged and determined to better resolutions, at faster speeds, and with more scientists having improved access. This review highlights recent advances at each stageof the cryo-EM pipeline and provides examples of how these techniques have been used to investigate real-world problems, including antibody development against the SARS-CoV-2 spike during the recent COVID-19 pandemic.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"91 ","pages":"1-32"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10393189/pdf/nihms-1916146.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10286487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 19
Evolutionary Dynamics and Molecular Mechanisms of HORMA Domain Protein Signaling. HORMA结构域蛋白信号的进化动力学和分子机制。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 Epub Date: 2022-01-18 DOI: 10.1146/annurev-biochem-090920-103246
Yajie Gu, Arshad Desai, Kevin D Corbett
{"title":"Evolutionary Dynamics and Molecular Mechanisms of HORMA Domain Protein Signaling.","authors":"Yajie Gu,&nbsp;Arshad Desai,&nbsp;Kevin D Corbett","doi":"10.1146/annurev-biochem-090920-103246","DOIUrl":"https://doi.org/10.1146/annurev-biochem-090920-103246","url":null,"abstract":"<p><p>Controlled assembly and disassembly of multi-protein complexes is central to cellular signaling. Proteins of the widespread and functionally diverse HORMA family nucleate assembly of signaling complexes by binding short peptide motifs through a distinctive safety-belt mechanism. HORMA proteins are now understood as key signaling proteins across kingdoms, serving as infection sensors in a bacterial immune system and playing central roles in eukaryotic cell cycle, genome stability, sexual reproduction, and cellular homeostasis pathways. Here, we describe how HORMA proteins' unique ability to adopt multiple conformational states underlies their functions in these diverse contexts. We also outline how a dedicated AAA+ ATPase regulator, Pch2/TRIP13, manipulates HORMA proteins' conformational states to activate or inactivate signaling in different cellular contexts. The emergence of Pch2/TRIP13 as a lynchpin for HORMA protein action in multiple genome-maintenance pathways accounts for its frequent misregulation in human cancers and highlights TRIP13 as a novel therapeutic target.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"541-569"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39829358","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: 15
Encapsulins. 密封剂。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 DOI: 10.1146/annurev-biochem-040320-102858
Tobias W Giessen
{"title":"Encapsulins.","authors":"Tobias W Giessen","doi":"10.1146/annurev-biochem-040320-102858","DOIUrl":"https://doi.org/10.1146/annurev-biochem-040320-102858","url":null,"abstract":"<p><p>Subcellular compartmentalization is a defining feature of all cells. In prokaryotes, compartmentalization is generally achieved via protein-based strategies. The two main classes of microbial protein compartments are bacterial microcompartments and encapsulin nanocompartments. Encapsulins self-assemble into proteinaceous shells with diameters between 24 and 42 nm and are defined by the viral HK97-fold of their shell protein. Encapsulins have the ability to encapsulate dedicated cargo proteins, including ferritin-like proteins, peroxidases, and desulfurases. Encapsulation is mediated by targeting sequences present in all cargo proteins. Encapsulins are found in many bacterial and archaeal phyla and have been suggested to play roles in iron storage, stress resistance, sulfur metabolism, and natural product biosynthesis. Phylogenetic analyses indicate that they share a common ancestor with viral capsid proteins. Many pathogens encode encapsulins, and recent evidence suggests that they may contribute toward pathogenicity. The existing information on encapsulin structure, biochemistry, biological function, and biomedical relevance is reviewed here.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"91 ","pages":"353-380"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9944552/pdf/nihms-1869567.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10750512","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 14
The Structural Dynamics of Translation. 翻译的结构动力学。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 DOI: 10.1146/annurev-biochem-071921-122857
Andrei A Korostelev
{"title":"The Structural Dynamics of Translation.","authors":"Andrei A Korostelev","doi":"10.1146/annurev-biochem-071921-122857","DOIUrl":"https://doi.org/10.1146/annurev-biochem-071921-122857","url":null,"abstract":"<p><p>Accurate protein synthesis (translation) relies on translation factors that rectify ribosome fluctuations into a unidirectional process. Understanding this process requires structural characterization of the ribosome and translation-factor dynamics. In the 2000s, crystallographic studies determined high-resolution structures of ribosomes stalled with translation factors, providing a starting point for visualizing translation. Recent progress in single-particle cryogenic electron microscopy (cryo-EM) has enabled near-atomic resolution of numerous structures sampled in heterogeneous complexes (ensembles). Ensemble and time-resolved cryo-EM have now revealed unprecedented views of ribosome transitions in the three principal stages of translation: initiation, elongation, and termination. This review focuses on how translation factors help achieve high accuracy and efficiency of translation by monitoring distinct ribosome conformations and by differentially shifting the equilibria of ribosome rearrangements for cognate and near-cognate substrates.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"91 ","pages":"245-267"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10389292/pdf/nihms-1920330.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9890319","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 13
Ribonucleotide Incorporation by Eukaryotic B-Family Replicases and Its Implications for Genome Stability. 真核生物b家族复制酶与核糖核苷酸的结合及其对基因组稳定性的影响。
IF 12.1 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 Epub Date: 2022-03-14 DOI: 10.1146/annurev-biochem-032620-110354
Jessica S Williams, Thomas A Kunkel
{"title":"Ribonucleotide Incorporation by Eukaryotic B-Family Replicases and Its Implications for Genome Stability.","authors":"Jessica S Williams, Thomas A Kunkel","doi":"10.1146/annurev-biochem-032620-110354","DOIUrl":"10.1146/annurev-biochem-032620-110354","url":null,"abstract":"<p><p>Our current view of how DNA-based genomes are efficiently and accurately replicated continues to evolve as new details emerge on the presence of ribonucleotides in DNA. Ribonucleotides are incorporated during eukaryotic DNA replication at rates that make them the most common noncanonical nucleotide placed into the nuclear genome, they are efficiently repaired, and their removal impacts genome integrity. This review focuses on three aspects of this subject: the incorporation of ribonucleotides into the eukaryotic nuclear genome during replication by B-family DNA replicases, how these ribonucleotides are removed, and the consequences of their presence or removal for genome stability and disease.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"1 1","pages":"133-155"},"PeriodicalIF":12.1,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9384702/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41923596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The Initiation of Eukaryotic DNA Replication. 真核生物DNA复制的起始。
IF 16.6 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 Epub Date: 2022-03-23 DOI: 10.1146/annurev-biochem-072321-110228
Alessandro Costa, John F X Diffley
{"title":"The Initiation of Eukaryotic DNA Replication.","authors":"Alessandro Costa,&nbsp;John F X Diffley","doi":"10.1146/annurev-biochem-072321-110228","DOIUrl":"https://doi.org/10.1146/annurev-biochem-072321-110228","url":null,"abstract":"<p><p>DNA replication in eukaryotic cells initiates from large numbers of sites called replication origins. Initiation of replication from these origins must be tightly controlled to ensure the entire genome is precisely duplicated in each cell cycle. This is accomplished through the regulation of the first two steps in replication: loading and activation of the replicative DNA helicase. Here we describe what is known about the mechanism and regulation of these two reactions from a genetic, biochemical, and structural perspective, focusing on recent progress using proteins from budding yeast.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":" ","pages":"107-131"},"PeriodicalIF":16.6,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40316866","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: 35
Lipoproteins in the Central Nervous System: From Biology to Pathobiology. 中枢神经系统中的脂蛋白：从生物学到病理生物学
IF 12.1 1区 生物学
Annual review of biochemistry Pub Date : 2022-06-21 Epub Date: 2022-03-18 DOI: 10.1146/annurev-biochem-032620-104801
Ana-Caroline Raulin, Yuka A Martens, Guojun Bu
{"title":"Lipoproteins in the Central Nervous System: From Biology to Pathobiology.","authors":"Ana-Caroline Raulin, Yuka A Martens, Guojun Bu","doi":"10.1146/annurev-biochem-032620-104801","DOIUrl":"10.1146/annurev-biochem-032620-104801","url":null,"abstract":"<p><p>The brain, as one of the most lipid-rich organs, heavily relies on lipid transport and distribution to maintain homeostasis and neuronal function. Lipid transport mediated by lipoprotein particles, which are complex structures composed of apolipoproteins and lipids, has been thoroughly characterized in the periphery. Although lipoproteins in the central nervous system (CNS) were reported over half a century ago, the identification of <i>APOE4</i> as the strongest genetic risk factor for Alzheimer's disease has accelerated investigation of the biology and pathobiology of lipoproteins in the CNS. This review provides an overview of the different components of lipoprotein particles, in particular apolipoproteins, and their involvements in both physiological functions and pathological mechanisms in the CNS.</p>","PeriodicalId":7980,"journal":{"name":"Annual review of biochemistry","volume":"91 ","pages":"731-759"},"PeriodicalIF":12.1,"publicationDate":"2022-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9634960/pdf/nihms-1844218.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9743352","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
首页 上一页 下一页 尾页
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整，为了账户安全，请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们：info@booksci.cn Book学术提供免费学术资源搜索服务，方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号：604180095
Book学术官方微信