Magnetic Resonance Letters最新文献

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OFC: Outside Front Cover OFC:外封面
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-11-01 Epub Date: 2025-11-08 DOI: 10.1016/S2772-5162(25)00068-3
{"title":"OFC: Outside Front Cover","authors":"","doi":"10.1016/S2772-5162(25)00068-3","DOIUrl":"10.1016/S2772-5162(25)00068-3","url":null,"abstract":"","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 4","pages":"Article 200243"},"PeriodicalIF":1.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145468732","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
Extreme quadrupolar nuclei under control: Ultra-wideline solid-state NMR at 36 T 极端四极核控制:超宽线固态核磁共振在36t
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-11-01 Epub Date: 2025-07-25 DOI: 10.1016/j.mrl.2025.200238
Luming Peng
{"title":"Extreme quadrupolar nuclei under control: Ultra-wideline solid-state NMR at 36 T","authors":"Luming Peng","doi":"10.1016/j.mrl.2025.200238","DOIUrl":"10.1016/j.mrl.2025.200238","url":null,"abstract":"","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 4","pages":"Article 200238"},"PeriodicalIF":1.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145468739","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
NMR methods for investigating functionally relevant biomolecular dynamics 研究功能相关生物分子动力学的核磁共振方法
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-11-01 Epub Date: 2025-03-19 DOI: 10.1016/j.mrl.2025.200195
Yangzhuoyue Jin , Yingxian Cui , Tairan Yuwen
{"title":"NMR methods for investigating functionally relevant biomolecular dynamics","authors":"Yangzhuoyue Jin ,&nbsp;Yingxian Cui ,&nbsp;Tairan Yuwen","doi":"10.1016/j.mrl.2025.200195","DOIUrl":"10.1016/j.mrl.2025.200195","url":null,"abstract":"<div><div>The dynamics of biomolecules span across a wide range of timescales, reflecting the complexity of free energy landscapes of biomolecules. Among these, the microsecond-to-millisecond (μs–ms) timescale dynamics are particularly significant, offering detailed insights into the kinetic, thermodynamic, and structural aspects of biological function. Many critical biological processes, including enzyme catalysis, protein folding, ligand binding, and allosteric regulation, operate within this timescale. Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for probing molecular dynamics in this time window, commonly used NMR methods for investigating μs–ms timescale dynamics include Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion, chemical exchange saturation transfer (CEST), and rotating-frame longitudinal relaxation dispersion (<em>R</em><sub>1<em>ρ</em></sub> relaxation dispersion). This review provides a brief overview of the fundamental principles and some recent advances of these methods, highlighting their interrelationships and applications in elucidating biomolecular dynamics.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 4","pages":"Article 200195"},"PeriodicalIF":1.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145468733","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
Cryoporometry for short T2 samples: A T1 filter method applied to battery electrode characterization 短T2样品的低温孔隙法:一种用于电池电极表征的T1滤波方法
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2025-02-11 DOI: 10.1016/j.mrl.2025.200180
Marc Fleury , Thibaud Chevalier , Benjamin Nicot , Quentin Denoyelle , Julien Bernard
{"title":"Cryoporometry for short T2 samples: A T1 filter method applied to battery electrode characterization","authors":"Marc Fleury ,&nbsp;Thibaud Chevalier ,&nbsp;Benjamin Nicot ,&nbsp;Quentin Denoyelle ,&nbsp;Julien Bernard","doi":"10.1016/j.mrl.2025.200180","DOIUrl":"10.1016/j.mrl.2025.200180","url":null,"abstract":"<div><div>The pore size distribution is often an important parameter for transport processes in porous media. Cryoporometry experiments can provide such data in the meso and macropore size up to 1 μm providing the sample temperature is finely controlled. We use a Peltier based system inserted directly into the NMR probe to control the temperature within 0.05 °C and impose temperature ramps down to 0.002 °C/min, necessary to characterize the largest pore sizes. The pore size information in the macropore range cannot be obtained from gas adsorption techniques while mercury injection is questionable for the material considered here. For porous materials made of paramagnetic minerals such as lithium-iron phosphate (LiFePO<sub>4</sub>, LFP) or nickel-manganese-cobalt oxides (NMC) and saturated with octamethylcyclotetrasiloxane (OMCTS), the <em>T</em><sub>2</sub> relaxation times are very short such as protons from the liquid and frozen phases cannot be separated. Hence the usual cryoporometry experiment cannot be performed. Instead, we propose to use the <em>T</em><sub>1</sub> contrast to separate these phases. The method is studied in detail along with some temperature effects linked with the <em>T</em><sub>1</sub> variation of the bulk frozen OMCTS. We show an example on two cathode materials part of industrial battery product.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200180"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934274","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
Rigid and stable nitroxide spin label for high-resolution distance measurements on proteins by DEER experiments 刚性和稳定的氮氧化物自旋标签,用于高分辨率的距离测量蛋白质的DEER实验
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2025-02-28 DOI: 10.1016/j.mrl.2025.200194
Ya-Ting Chen , Xing Zhang , Jia-Liang Chen , Bin-Bin Pan , Daniella Goldfarb , Yin Yang , Xun-Cheng Su
{"title":"Rigid and stable nitroxide spin label for high-resolution distance measurements on proteins by DEER experiments","authors":"Ya-Ting Chen ,&nbsp;Xing Zhang ,&nbsp;Jia-Liang Chen ,&nbsp;Bin-Bin Pan ,&nbsp;Daniella Goldfarb ,&nbsp;Yin Yang ,&nbsp;Xun-Cheng Su","doi":"10.1016/j.mrl.2025.200194","DOIUrl":"10.1016/j.mrl.2025.200194","url":null,"abstract":"<div><div>The distance distributions between two site-specifically anchored spin labels in a protein, measured by pulsed electron-electron double resonance (PELDOR or DEER), provide rich sources of structural and conformational restraints on the proteins or their complexes. The rigid connection of the nitroxide spin label to the protein improves the accuracy and precision of distance measurement. We report a new spin labelling approach by formation of thioester bond between nitroxide (NO) spin label, NOAI (NO spin labels activated by acetylimidazole), and a protein thiol, and this spin labeling method has demonstrated high performance in DEER distance measurement on proteins. The results showed that NOAI has shorter connection to the protein ligation site than 2, 2, 5, 5-tetramethyl-pyrroline-1-oxyl methanethiosulfonate (MTSL) and 3-maleimido-proxyl (M-Prox) in the respective protein conjugate and produces narrower distance distributions for the tested proteins including ubiquitin (Ub), immunoglobulin-binding β1 domain of streptococcal protein G (GB1), and second mitochondria-derived activator of caspases (Smac). The NOAI protein conjugate connected by a thioester bond is resistant to reducing reagent and offers high-fidelity DEER distance measurements in cell lysates.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200194"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934216","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
Adaptive k-space learning and high-dimensional subsets embedding for parallel MRI reconstruction 自适应k空间学习和高维子集嵌入并行MRI重构
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2024-12-29 DOI: 10.1016/j.mrl.2024.200175
Zhonghui Wu , Yuxia Huang , Yu Guan, Qiegen Liu
{"title":"Adaptive k-space learning and high-dimensional subsets embedding for parallel MRI reconstruction","authors":"Zhonghui Wu ,&nbsp;Yuxia Huang ,&nbsp;Yu Guan,&nbsp;Qiegen Liu","doi":"10.1016/j.mrl.2024.200175","DOIUrl":"10.1016/j.mrl.2024.200175","url":null,"abstract":"<div><div>Magnetic resonance imaging (MRI) inherently requires considerable time for data acquisition, but obtaining multi-contrast MRI data further prolongs this process, thereby increasing susceptibility to motion artifacts. It is worth noting that the multi-contrast MR images have both structural similarities and unique contrast information. Therefore, to take advantage of their similarities while preserving their distinctive characteristics, we proposed a new method called high-dimensional subsets embedding (HDSE). This novel approach is based on the frame of low-rank modeling of local <em>k</em>-space neighborhoods with parallel imaging (P-LORAKS). Specifically, our approach utilizes the structural similarity of multi-contrast MR images to process different <em>k</em>-space data through two independent channels. In one channel, we individually separate the complementary <em>T</em><sub>1</sub>-<em>T</em><sub>2</sub> <em>k</em>-space data and directly construct a new subset of local <em>k</em>-space, allowing the model to better capture structural correlations between multiple contrasts. In another channel, we provide global under-sampled <em>T</em><sub>2</sub>-weighted <em>k</em>-space data further constrain image acquisition in high-dimensional space to maintain image consistency and reduce noise amplification. These two different channels information is fused together to form high-dimensional feature objects. Besides, we embed the constructed objects into P-LORAKS in various ways to enhance the reconstruction performance. Experimental results demonstrated that the aided reconstruction of local subsets fusion and the high-dimensional reconstruction of adaptive global constraints can improve the accuracy of image reconstruction and enhance the robustness of the model.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200175"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934213","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 rise of NMR-integrated fragment-based drug discovery in China 核磁共振整合碎片药物发现在中国的兴起
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2025-01-29 DOI: 10.1016/j.mrl.2025.200179
Zihuan Li, Lei Wang, Jia Gao, Ke Ruan
{"title":"The rise of NMR-integrated fragment-based drug discovery in China","authors":"Zihuan Li,&nbsp;Lei Wang,&nbsp;Jia Gao,&nbsp;Ke Ruan","doi":"10.1016/j.mrl.2025.200179","DOIUrl":"10.1016/j.mrl.2025.200179","url":null,"abstract":"<div><div>Nuclear magnetic resonance (NMR) spectroscopy is an indispensable tool to probe weak protein-ligand interactions, which are key to the hit identification and hit-to-lead evolution in fragment-based drug discovery (FBDD). The integration of NMR technology in FBDD has facilitated the development of a diverse array of candidate compounds and FDA-approved drugs. Here, we summarized the rapid advancement and application of NMR techniques in contemporary China, which serves as a catalyst for the ongoing prosperousness of fragment-derived inhibitors against various targets.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200179"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934217","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
A magnetically compatible, arbitrary positioning system for accurate spatial mapping of magnetic fields for shimming studies in MRI 一种磁兼容的任意定位系统,用于MRI中振荡研究的磁场精确空间映射
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2025-02-17 DOI: 10.1016/j.mrl.2025.200191
Yiqing Yin , Wenchen Wang , Shihe Zhao , Hui Wang , Junsheng Cheng , Shunzhong Chen , Wenhui Yang , Feng Liu , Yaohui Wang
{"title":"A magnetically compatible, arbitrary positioning system for accurate spatial mapping of magnetic fields for shimming studies in MRI","authors":"Yiqing Yin ,&nbsp;Wenchen Wang ,&nbsp;Shihe Zhao ,&nbsp;Hui Wang ,&nbsp;Junsheng Cheng ,&nbsp;Shunzhong Chen ,&nbsp;Wenhui Yang ,&nbsp;Feng Liu ,&nbsp;Yaohui Wang","doi":"10.1016/j.mrl.2025.200191","DOIUrl":"10.1016/j.mrl.2025.200191","url":null,"abstract":"<div><div>After the fabrication of magnetic resonance superconducting magnets, the magnetic field inhomogeneity needs to be accurately measured for subsequent shimming. However, conventional measurement methods are susceptible to magnetic fields, have poor compatibility, and are difficult to adapt to various types of magnets. This paper proposes a new field measuring system based on a three-axis movable platform. The system utilizes non-magnetic materials and an innovative hand-wheel lifting design that can be adapted to various aperture magnets, thus obviating the necessity for electrically driven equipment and addressing safety concerns in strong magnetic fields. In addition, the measurement system offers high accuracy up to 1 mm and a wide measurable range. The fields of 3 T and 7 T magnets were mapped using the designed system with diameter of spherical volume (DSV) of 160 mm and 130 mm, respectively. Experimental results demonstrate that the magnetic field measurement system has strong compatibility and can accurately map the magnetic field at arbitrary positions, which is critical for shimming studies.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200191"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934214","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
Dynamic nuclear polarization and chemically induced hyperpolarization: Progress, mechanisms, and opportunities 动态核极化和化学诱导的超极化:进展、机制和机会
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2025-01-29 DOI: 10.1016/j.mrl.2025.200178
Danhua Dai , Yangping Liu , Xiao He , Jiafei Mao
{"title":"Dynamic nuclear polarization and chemically induced hyperpolarization: Progress, mechanisms, and opportunities","authors":"Danhua Dai ,&nbsp;Yangping Liu ,&nbsp;Xiao He ,&nbsp;Jiafei Mao","doi":"10.1016/j.mrl.2025.200178","DOIUrl":"10.1016/j.mrl.2025.200178","url":null,"abstract":"<div><div>Nuclear magnetic resonance (NMR) spectroscopy is a powerful and broadly used spectroscopic technique for characterizing molecular structures and dynamics. Yet the power of NMR is restricted by its inherently low sensitivity due to the weak polarization of nuclear spins under conventional experiment conditions. Dynamic nuclear polarization (DNP) and chemically induced dynamic nuclear polarization (CIDNP) have been emerging as powerful <em>in-situ</em> hyperpolarization methods to boost NMR sensitivity. This review provides a brief overview of DNP mechanisms in the context of both solid-state and liquid-state. We delve into the molecular features of different polarizing agents and their impacts on DNP applications, which are now steadily progressing towards modern NMR magnetic field strengths and ambient temperatures. Furthermore, the progress of CIDNP, particularly photo-CIDNP as a potential alternative hyperpolarization technique of DNP, in studying protein dynamics and chemical reaction mechanisms, will be covered. This review also highlights the chemical diversity and experimental strategies crucial for these hyperpolarization techniques, showcasing their transformative role in NMR spectroscopy.</div></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200178"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934212","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
OFC: Outside Front Cover OFC:外封面
IF 1.7
Magnetic Resonance Letters Pub Date : 2025-08-01 Epub Date: 2025-09-02 DOI: 10.1016/S2772-5162(25)00055-5
{"title":"OFC: Outside Front Cover","authors":"","doi":"10.1016/S2772-5162(25)00055-5","DOIUrl":"10.1016/S2772-5162(25)00055-5","url":null,"abstract":"","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"5 3","pages":"Article 200230"},"PeriodicalIF":1.7,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144934272","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
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