ChemBioChem最新文献_第3页

Glycoproteins, Glycolipids, or Both: Why do Glycosyltransferases Recognize Different Acceptors? 糖蛋白，糖脂，或两者：为什么糖基转移酶识别不同的受体？

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-06 DOI: 10.1002/cbic.202500212

Krzysztof Mikołajczyk, Marcin Czerwinski, Radoslaw Kaczmarek

引用次数: 0

Preorganized Electric Fields in Voltage-Gated Sodium Channels. 电压门控钠通道中的预组织电场。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-06 DOI: 10.1002/cbic.202500314

Yi Zheng, Taoyi Chen, Valerie Vaissier Welborn

引用次数: 0

Selective [9-15N] Guanosine for NMR Studies of Large RNAs. 选择性[9-15N]鸟苷用于大rna的核磁共振研究。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-04 DOI: 10.1002/cbic.202500206

Solomon K Attionu, Rita Dill, Michael F Summers, David A Case, Jan Marchant, Theodore Kwaku Dayie

引用次数: 0

Clade III Synthases Add Cyclic And Linear Terpenoids To The Psilocybe Metabolome. Clade III合酶在裸盖菇代谢组中添加环状和线性萜类。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-03 DOI: 10.1002/cbic.202500167

Nick Zschoche, Sebastian Schober, Karl Walther, Andrew R Chadeayne, Markus Gressler, Stefan Bartram, Sarah E O'Connor, Dirk Hoffmeister

{"title":"Clade III Synthases Add Cyclic And Linear Terpenoids To The Psilocybe Metabolome.","authors":"Nick Zschoche, Sebastian Schober, Karl Walther, Andrew R Chadeayne, Markus Gressler, Stefan Bartram, Sarah E O'Connor, Dirk Hoffmeister","doi":"10.1002/cbic.202500167","DOIUrl":"https://doi.org/10.1002/cbic.202500167","url":null,"abstract":"Psilocybe \"magic mushrooms\" are best known for their indolethylamine psilocybin, yet they encode enzymes for a much more diverse arsenal of small and potentially bioactive molecules. Here, we report on four Psilocybe cubensis clade III sesquiterpene synthases, CubB-CubE, whose genes are differently expressed in fruiting bodies compared to vegetative mycelium. CubB-CubE were functionally characterized in vitro by product formation assays with heterologously produced enzymes and in vivo by transgene expression in Aspergillus niger, followed by extensive GC-MS analyses. CubB was identified as a single product (3R,6E)-(-)-nerolidol synthase. CubC is a multi-product enzyme producing β-caryophyllene, β-elemene, α-humulene, and β-farnesene. CubD and CubE catalyzed (near-)exclusively sterpurene formation. P. cubensis young fruiting bodies and vegetative mycelium were analyzed for sesquiterpenes which verified the presence of the CubB product α-(3R,6E)-(-)-nerolidol. As various Psilocybe species encode highly similar enzymes, this study contributes generally to the as yet little understood secondary metabolome of the genus.","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202500167"},"PeriodicalIF":2.6,"publicationDate":"2025-05-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143960755","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Development of a Peptide Inhibitor Targeting the C-SH2 Domain of the SHP2 Phosphatase. 一种靶向SHP2磷酸酶C-SH2结构域的肽抑制剂的研制

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-02 DOI: 10.1002/cbic.202400938

Azin Kiani, Catia L Pierotti, Franziska Schedel, Thomas Kokot, Judith Weyershaeuser, Mario Brehm, Pablo Rios, Kerstin Fehrenbach, Bettina Warscheid, Susana Minguet, Wolfgang W Schamel, Maja Köhn

{"title":"Development of a Peptide Inhibitor Targeting the C-SH2 Domain of the SHP2 Phosphatase.","authors":"Azin Kiani, Catia L Pierotti, Franziska Schedel, Thomas Kokot, Judith Weyershaeuser, Mario Brehm, Pablo Rios, Kerstin Fehrenbach, Bettina Warscheid, Susana Minguet, Wolfgang W Schamel, Maja Köhn","doi":"10.1002/cbic.202400938","DOIUrl":"10.1002/cbic.202400938","url":null,"abstract":"Src homology 2 (SH2) domain-containing phosphatase 2 (SHP2) mediates important signal transduction upon cell surface receptor stimulation, regulating multiple cellular functions. In addition to the catalytically active phosphotyrosine (pTyr) phosphatase domain, SHP2 contains two regulatory pTyr-binding domains: the N-SH2 and C-SH2 domains. While the role of the N-SH2 domain is well understood, the role of the C-SH2 domain is less clear. To support studies on the involvement of the domains in SHP2 function, herein, the development of a peptide inhibitor containing a nonhydrolysable pTyr mimetic, which selectively binds to the C-SH2 domain of SHP2 and blocks its protein-protein interactions, is described. Incorporation of the pTyr mimetic l-O-malonyltyrosine (l-OMT) results in robust binding affinity to the C-SH2 domain, while the widely used pTyr mimetic phosphonodifluoromethyl phenylalanine (F2Pmp) abolishes binding, showing that this mimetic is not a general binder of SH2 domains, which challenges existing notions. The C-SH2 inhibitor peptide (CSIP) is stable, selective, cell permeable, and noncytotoxic. CSIP enriches the toolbox of inhibitors with different modes of action targeting SHP2, and will support studies to better understand SHP2 regulation and interactions, which can ultimately inform new drug discovery efforts.","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e2400938"},"PeriodicalIF":2.6,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143955901","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Hijacking the MDM2 E3 Ligase with novel BRD4-Targeting PROTACs in Pancreatic Cancer Cells. 胰腺癌细胞中新型靶向brd4的PROTACs劫持MDM2 E3连接酶

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-02 DOI: 10.1002/cbic.202500133

Mihaela Ficu, Dan Niculescu-Duvaz, Mohammed Aljarah, Caroline Springer, Christopher S Kershaw

引用次数: 0

Chemically Synthesized Fluorescence based Kinase Sensing Systems for Signaling in Cancer. 基于化学合成荧光的肿瘤信号激酶传感系统。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-02 DOI: 10.1002/cbic.202500175

Anindita Roy, Monisha Singha, Subhankar Singha

{"title":"Chemically Synthesized Fluorescence based Kinase Sensing Systems for Signaling in Cancer.","authors":"Anindita Roy, Monisha Singha, Subhankar Singha","doi":"10.1002/cbic.202500175","DOIUrl":"https://doi.org/10.1002/cbic.202500175","url":null,"abstract":"Kinases are an essential class of enzymes that regulate cellular processes through phosphorylation, influencing signal transduction, cell cycle progression, and apoptosis. Dysregulation of kinase activity is a hallmark of cancer, contributing to tumorigenesis, metastasis, and therapeutic resistance. Therefore, precise detection and monitoring of kinase activity are essential for understanding cancer biology and advancing diagnostics and therapeutics. Among various detection methods, fluorescence-based kinase sensing systems have emerged as highly sensitive, real-time tools for investigating kinase function. These systems leverage fluorescent moieties, either genetically encoded or chemically synthesized, to provide spatial and temporal insights into kinase activity in complex biological environments. This review focuses on chemically synthesized fluorescence-based kinase sensing systems, which offer unique advantages, including precise control over concentrations and compatibility with in vitro and in vivo applications. We have classified the chemically synthesized sensing systems into three categories: specific peptide substrate-based, ATP/ADP-recognition-based, and inhibitor-based sensing systems, each tailored to specific kinase activities. Compared to genetically encoded systems, chemically synthesized sensors demonstrate greater versatility and are better suited for quantitative high-throughput applications. This review explores the design, mechanisms, and applications of these systems in cancer biology, highlighting their potential for identifying kinase biomarkers, optimizing targeted therapies, and advancing personalized medicine.","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202500175"},"PeriodicalIF":2.6,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143957525","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Synthesis of 2-substituted ATP derivatives and their use in enzymatic synthesis and postsynthetic labelling of RNA. 2-取代ATP衍生物的合成及其在酶促合成和RNA合成后标记中的应用。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-02 DOI: 10.1002/cbic.202500241

Ugnė Šinkevičiūtė, Tania Sanchez-Quirante, Samanta Rožánková, Lenka Poštová Slavětínská, Veronika Raindlová, Michal Hocek

引用次数: 0

Biosynthesis of Ephedrine is Initiated by Pyridoxal Phosphate-Dependent Formation of Cathinone. 由磷酸吡哆醛依赖性形成卡西酮引发麻黄碱的生物合成。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-05-01 DOI: 10.1002/cbic.202500279

Karina Witte, Anne Behrens, Hannes M Schwelm, Volker Auwärter, Michael Müller

{"title":"Biosynthesis of Ephedrine is Initiated by Pyridoxal Phosphate-Dependent Formation of Cathinone.","authors":"Karina Witte, Anne Behrens, Hannes M Schwelm, Volker Auwärter, Michael Müller","doi":"10.1002/cbic.202500279","DOIUrl":"https://doi.org/10.1002/cbic.202500279","url":null,"abstract":"Ephedra alkaloids possess some of the most basic structures of alkaloids. Despite their importance for human use and their commercial relevance, the biosynthesis of ephedra alkaloids has remained enigmatic. The predominant biosynthetic pathway in the literature proposes a thiamine-dependent caboligation followed by a transaminase, although no candidate enzymes have yet been identified in ephedra alkaloid producers. In this work, an alternative pathway in plants to ephedra alkaloids via (S)-cathinone was investigated that circumvents the formation of 1-phenylpropane-1,2-dione as an intermediate and is in full agreement with previous biosynthetic studies. This alternative pathway involves the pyridoxal phosphate (PLP)-dependent carboligation of benzoyl-CoA and l-alanine in a single step. The PLP-dependent formation of labeled and unlabeled (S)-cathinone was detected in plant lysate of young stem tissue of various Ephedra species that contained Ephedra alkaloids, as well as in young leaf tissue of Catha edulis. The incorporation of labeled nitrogen from l-alanine into (S)-cathinone supports the hypothesis that an α-oxoamine synthase (AOS) catalyzes the formation of (S)-cathinone, bypassing the dione as an intermediate. These results demonstrate the involvement of a PLP-dependent AOS as a pivotal step in the biosynthesis of ephedra alkaloids.","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202500279"},"PeriodicalIF":2.6,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143953685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

Fluorescence Lifetime Multiplexing with Environment-Sensitive Chemigenetic Probes. 荧光寿命复用与环境敏感的化学探针。

IF 2.6 4区生物学

ChemBioChem Pub Date : 2025-04-30 DOI: 10.1002/cbic.202500174

Sarah Emmert, Anna Rovira, Pablo Rivera-Fuentes

引用次数: 0