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Selection regimes, not just cold environments, shape cold-active cellulases 选择机制，而不仅仅是寒冷的环境，塑造了冷活性纤维素酶。
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 Epub Date: 2026-09-10 DOI: 10.1016/j.tibs.2026.08.011
Caizhen Wang (王蔡真), Ming Gong (龚明), Gen Zou (邹根)
{"title":"Selection regimes, not just cold environments, shape cold-active cellulases","authors":"Caizhen Wang (王蔡真),&nbsp;Ming Gong (龚明),&nbsp;Gen Zou (邹根)","doi":"10.1016/j.tibs.2026.08.011","DOIUrl":"10.1016/j.tibs.2026.08.011","url":null,"abstract":"<div><div>Cold-active cellulases have traditionally been discovered in persistently cold environments, but examples from autolytic mushrooms, gut microbiomes, and biomass-decomposition systems suggest they are not exclusive adaptations to chronic cold. We propose that diverse ecological selection regimes may also favor enzymes that relieve catalytic bottlenecks.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 986-989"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148928746","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
Membrane lipid sensing during ERAD: coupling lipid composition to proteostatic fate ERAD期间的膜脂传感：脂质组成与蛋白抑制命运的耦合。
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 Epub Date: 2026-08-05 DOI: 10.1016/j.tibs.2026.07.006
Aikaterini Vrentzou, Alexander Stein
{"title":"Membrane lipid sensing during ERAD: coupling lipid composition to proteostatic fate","authors":"Aikaterini Vrentzou,&nbsp;Alexander Stein","doi":"10.1016/j.tibs.2026.07.006","DOIUrl":"10.1016/j.tibs.2026.07.006","url":null,"abstract":"<div><div>The endoplasmic reticulum (ER) membrane is both the central site of cellular lipid synthesis and the platform on which ER-associated degradation (ERAD) selects membrane proteins for ubiquitination and proteasomal destruction. ERAD shapes ER lipid composition by degrading biosynthetic enzymes and regulators of lipid metabolism, while the lipid environment in turn modulates each step of the pathway. In this review, we apply biophysical concepts of membrane protein dynamics to explain how changes in membrane composition shift conformational equilibria and bias proteostatic fate. We distinguish three modes through which lipid information reaches ERAD: substrate-intrinsic sensing, adaptor-mediated coupling, and lipid sensitivity of the ubiquitination machinery itself. These perspectives reframe ERAD as a lipid-responsive pathway integrating membrane composition with selective protein turnover.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 1038-1054"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148676708","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
Cell-free RNA fragmentomics: rethinking the biology of RNA liquid biopsies. 无细胞RNA片段组学：重新思考RNA液体活检的生物学。
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 DOI: 10.1016/j.tibs.2026.09.007
Valentina Blanco, Mauricio Castellano, Juan Pablo Tosar
{"title":"Cell-free RNA fragmentomics: rethinking the biology of RNA liquid biopsies.","authors":"Valentina Blanco, Mauricio Castellano, Juan Pablo Tosar","doi":"10.1016/j.tibs.2026.09.007","DOIUrl":"https://doi.org/10.1016/j.tibs.2026.09.007","url":null,"abstract":"<p><p>Cell-free RNA (cfRNA) is emerging as a promising analyte for liquid biopsy because it captures dynamic changes in gene expression across tissues and disease states. However, interpretation of cfRNA profiles remains limited by the lack of a unifying framework describing how extracellular RNAs are released, processed, and stabilized. Here, we propose that concepts from cell-free DNA fragmentomics provide a useful lens to interpret cfRNA biology and introduce the concept of cfRNA fragmentomics. We argue that many cfRNAs originate as intracellular ribonucleoprotein complexes that undergo extracellular ribonuclease processing, generating stable fragmented RNAs associated with proteins and other carriers. Under this framework, informative cfRNA signatures may arise not only from diseased tissues but also from indirect systemic responses to disease.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149102341","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
Subscription and Copyright Information 订阅及版权资料
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 DOI: 10.1016/S0968-0004(26)00291-4
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引用次数: 0
Science is always unfinished: rethinking the demand for complete stories 科学总是未完成的：重新考虑对完整故事的需求。
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 Epub Date: 2026-04-29 DOI: 10.1016/j.tibs.2026.04.010
Roberto Munita
{"title":"Science is always unfinished: rethinking the demand for complete stories","authors":"Roberto Munita","doi":"10.1016/j.tibs.2026.04.010","DOIUrl":"10.1016/j.tibs.2026.04.010","url":null,"abstract":"<div><div>The ‘complete story’ has become the standard in top journals. Narrative structure helps communicate science, but requiring mechanistic completeness for publication can exclude important discoveries, delay their dissemination, and push researchers to overfit their data to a narrative. This essay makes the case for making room for rigorous, unfinished stories.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 978-980"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147809025","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
Drugging the proteome via large-scale chemoproteomics 通过大规模化学蛋白质组学对蛋白质组进行药物治疗。
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 Epub Date: 2026-07-04 DOI: 10.1016/j.tibs.2026.06.005
Yushu Li (李玉书), Jiaqi Wang (王嘉琪), Tiantian Wang (王甜甜), Xisong Ke (柯细松), Yi Qu (屈祎)
{"title":"Drugging the proteome via large-scale chemoproteomics","authors":"Yushu Li (李玉书),&nbsp;Jiaqi Wang (王嘉琪),&nbsp;Tiantian Wang (王甜甜),&nbsp;Xisong Ke (柯细松),&nbsp;Yi Qu (屈祎)","doi":"10.1016/j.tibs.2026.06.005","DOIUrl":"10.1016/j.tibs.2026.06.005","url":null,"abstract":"<div><div>Genomic and proteomic initiatives have accelerated therapeutic target identification, yet many proteins remain difficult to drug, especially those lacking structural information, including those with intrinsically disordered regions. However, the conformational states of these proteins are shaped in living cells by chemical modifications, protein–protein interactions, oligomerization, and aggregation, offering new ligandable opportunities. In this article, we first discuss current approaches toward drugging the ‘undruggable’ proteins, in particular the advantages and limitations of structure-based drug design. We then describe the advantages of cellular protein-based strategies in identifying ligands for proteins that are hard to target, highlighting large-scale chemoproteomics approaches for drugging the proteome.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 1066-1078"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148387162","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
PABMB: connecting molecular biosciences across the Americas PABMB：连接整个美洲的分子生物科学
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 DOI: 10.1016/j.tibs.2026.08.012
José Sotelo-Silveira, Alexander de Luna Fors, Thomas Kislinger, Bianca Zingales, Alicia González-Manjarrez
{"title":"PABMB: connecting molecular biosciences across the Americas","authors":"José Sotelo-Silveira,&nbsp;Alexander de Luna Fors,&nbsp;Thomas Kislinger,&nbsp;Bianca Zingales,&nbsp;Alicia González-Manjarrez","doi":"10.1016/j.tibs.2026.08.012","DOIUrl":"10.1016/j.tibs.2026.08.012","url":null,"abstract":"<div><div>The Pan-American Association for Biochemistry and Molecular Biology (PABMB) has promoted scientific exchange, education, and research in the molecular biosciences across the Americas for more than five decades. By linking national societies operating in markedly different scientific environments, PABMB provides a regional framework for meetings, training, researcher mobility, and international collaboration, with particular emphasis on early-career scientists.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 975-977"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149094957","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
Subscription and Copyright Information 订阅及版权资料
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 DOI: 10.1016/S0968-0004(26)00291-4
{"title":"Subscription and Copyright Information","authors":"","doi":"10.1016/S0968-0004(26)00291-4","DOIUrl":"10.1016/S0968-0004(26)00291-4","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Page e1"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149094955","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
PABMB: connecting molecular biosciences across the Americas PABMB：连接整个美洲的分子生物科学
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 DOI: 10.1016/j.tibs.2026.08.012
José Sotelo-Silveira, Alexander de Luna Fors, Thomas Kislinger, Bianca Zingales, Alicia González-Manjarrez
{"title":"PABMB: connecting molecular biosciences across the Americas","authors":"José Sotelo-Silveira,&nbsp;Alexander de Luna Fors,&nbsp;Thomas Kislinger,&nbsp;Bianca Zingales,&nbsp;Alicia González-Manjarrez","doi":"10.1016/j.tibs.2026.08.012","DOIUrl":"10.1016/j.tibs.2026.08.012","url":null,"abstract":"<div><div>The Pan-American Association for Biochemistry and Molecular Biology (PABMB) has promoted scientific exchange, education, and research in the molecular biosciences across the Americas for more than five decades. By linking national societies operating in markedly different scientific environments, PABMB provides a regional framework for meetings, training, researcher mobility, and international collaboration, with particular emphasis on early-career scientists.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 975-977"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149094954","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
Minimal-alphabet proteins by evolution, engineering, and design 通过进化、工程和设计的最小字母蛋白质。
IF 14.4 1区 生物学
Trends in Biochemical Sciences Pub Date : 2026-10-01 Epub Date: 2026-08-29 DOI: 10.1016/j.tibs.2026.08.002
Filip Buchel, Valerio G. Giacobelli, Klára Hlouchová
{"title":"Minimal-alphabet proteins by evolution, engineering, and design","authors":"Filip Buchel,&nbsp;Valerio G. Giacobelli,&nbsp;Klára Hlouchová","doi":"10.1016/j.tibs.2026.08.002","DOIUrl":"10.1016/j.tibs.2026.08.002","url":null,"abstract":"<div><div>Research on the structural and functional potential of minimal amino acid alphabets is shifting from reductive ‘pruning’ of extant proteins to bottom-up exploration of combinatorial sequence space. This review highlights the experimental and computational toolkits driving this transition. We discuss how solid-phase peptide synthesis, genetically encoded libraries, and high-throughput selection and screening enable systematic exploration of vast, noncanonical landscapes largely inaccessible to traditional engineering. Integrating these approaches with generative machine learning and <em>de novo</em> protein design allows researchers to move beyond observing what evolution produced toward exploring what chemistry permits. Together, these advances are redirecting the field from simplifying extant proteins to uncovering the physicochemical principles governing protein foldability, while expanding the design space beyond the constraints imposed by biological evolution.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 10","pages":"Pages 1055-1065"},"PeriodicalIF":14.4,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148849638","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
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