Biomolecular NMR Assignments最新文献

Resonance assignments of the human receptor interacting protein kinase 1 (RIPK1) in its fibrillar conformation. 人受体相互作用蛋白激酶1 （RIPK1）在其纤维构象中的共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-09-15 DOI: 10.1007/s12104-025-10249-y

Paula Polonio, Miguel Mompeán

引用次数: 0

¹H, ¹⁵N, and ¹³C resonance assignment of human heat shock protein 10. 人热休克蛋白的1H， 15N和13C共振分配

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-09-13 DOI: 10.1007/s12104-025-10247-0

Abigail Page, Wyatt Hendricks, Marielle A Wälti

引用次数: 0

¹H, ¹³C and ¹⁵N backbone resonance assignment of the RNA binding motif 39 (RBM39) tandem RNA recognition motifs (RRM1-2). RNA结合基序39 （RBM39）串联RNA识别基序（RRM1-2）的1H， 13C和15N骨干共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-09-13 DOI: 10.1007/s12104-025-10248-z

Florian Malard, Léa Bouton, Sébastien Campagne

引用次数: 0

Resonance assignments of asymmetric tetrameric platelet factor 4 (PF4). 不对称四聚体血小板因子4 （PF4）的共振赋值。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-09-08 DOI: 10.1007/s12104-025-10246-1

Qiulin Ma, Jinfeng Huang, Stephen Boulton, Ellen Mak, Madoka Akimoto, Estefanía López Giraldo, Mikayla Truong, Mercy Daka, Angela Huynh, Sarah Kwok, Rumi Clare, Ishac Nazy, Woonghee Lee, Giuseppe Melacini

{"title":"Resonance assignments of asymmetric tetrameric platelet factor 4 (PF4).","authors":"Qiulin Ma, Jinfeng Huang, Stephen Boulton, Ellen Mak, Madoka Akimoto, Estefanía López Giraldo, Mikayla Truong, Mercy Daka, Angela Huynh, Sarah Kwok, Rumi Clare, Ishac Nazy, Woonghee Lee, Giuseppe Melacini","doi":"10.1007/s12104-025-10246-1","DOIUrl":"https://doi.org/10.1007/s12104-025-10246-1","url":null,"abstract":"Platelet Factor 4 (PF4), also known as CXCL4, is a CXC chemokine crucial for hemostasis, inflammation, and immune responses. Under physiological conditions PF4 assembles into asymmetric tetramers (31.2 kDa) that are dimers of dimers with highly flexible N-terminal regions. PF4 tetramers play a central role in prothrombotic autoimmune conditions, such as heparin-induced thrombocytopenia (HIT), as well as vaccine-induced immune thrombocytopenia and thrombosis (VITT). Here, we report the resonance assignments of 1H, 15N, and 13C nuclei for wild-type asymmetric PF4 tetramers using TROSY-based triple resonance NMR experiments. We also used Nz-exchange spectroscopy to identify peaks split by slow-exchange between two distinct conformational states caused by the asymmetry of PF4 tetramers. Our NMR assignments establish a foundation for future investigations into the structural dynamics and functional mechanisms of PF4 as well as its pathological role in anti-PF4 disorders.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.6,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145022595","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

¹H, ¹⁵N and ¹³C backbone resonance assignments of flap endonuclease from Plasmodium falciparum. 恶性疟原虫皮瓣内切酶的1H， 15N和13C骨干共振定位。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-08-09 DOI: 10.1007/s12104-025-10241-6

Rodolpho do Aido-Machado, Nicola J Baxter, Michelle L Rowe, Manoj B Pohare, Srdjan Vitovski, Jon R Sayers, Jonathan P Waltho

{"title":"1H, 15N and 13C backbone resonance assignments of flap endonuclease from Plasmodium falciparum.","authors":"Rodolpho do Aido-Machado, Nicola J Baxter, Michelle L Rowe, Manoj B Pohare, Srdjan Vitovski, Jon R Sayers, Jonathan P Waltho","doi":"10.1007/s12104-025-10241-6","DOIUrl":"https://doi.org/10.1007/s12104-025-10241-6","url":null,"abstract":"Flap endonuclease (FEN) enzymes are a group of metallonucleases that have essential roles in DNA repair and the maintenance of genomic resilience. They catalyse hydrolytic cleavage of a phosphodiester bond to remove 5'-flaps present on double-stranded DNA molecules formed during DNA replication. FEN locates a target scissile bond through the structural recognition of a pronounced bend in the double-stranded DNA substrate along with the presence of both a 5'-flap and a 1-nucleotide 3'-flap. FEN enzymes share a common structural architecture and are functionally conserved across all living organisms. In this work, we report the 1H, 15N and 13C backbone resonance assignments of residues 2-349 of FEN from Plasmodium falciparum (PfFEN349) in its substrate-free state. Using heteronuclear multidimensional NMR spectroscopy, 90% of all backbone resonances of PfFEN349 were assigned, with 298 backbone amide resonances out of 337 theoretically-detectible resonances (which exclude 10 prolines and the N-terminal glycine) identified in the 1H-15 N TROSY spectrum. Prediction of solution secondary structure content from a chemical shift analysis using the TALOS-N webserver is mostly in good agreement with an AlphaFold model of PfFEN349. The reported assignments provide a pathway for drug discovery as PfFEN349 is a potential target for the development of new inhibitors that could be utilised to control the incidence of malaria across the globe.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.6,"publicationDate":"2025-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144803192","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

¹H, ¹³C and ¹⁵N chemical shift assignment for stem-loop 5a from the 5'UTR of HCoV-229E. 从HCoV-229E的5'UTR中，茎环5a的1H， 13C和15N化学位移分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-31 DOI: 10.1007/s12104-025-10243-4

Nina M Krause, Anna Wacker, Christian Richter, Boris Fürtig, Ramakanth Madhugiri, John Ziebuhr, Harald Schwalbe

引用次数: 0

Backbone NMR assignments of the essential oxidoreductase tryparedoxin from the human pathogenic parasite Trypanosoma cruzi. 人类致病性克氏锥虫必需氧化还原酶tryparedoxin的核磁共振骨架分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-28 DOI: 10.1007/s12104-025-10244-3

Eric Schwegler, Ute A Hellmich

{"title":"Backbone NMR assignments of the essential oxidoreductase tryparedoxin from the human pathogenic parasite Trypanosoma cruzi.","authors":"Eric Schwegler, Ute A Hellmich","doi":"10.1007/s12104-025-10244-3","DOIUrl":"https://doi.org/10.1007/s12104-025-10244-3","url":null,"abstract":"Over 7 million people worldwide are affected with Chagas disease, a lifelong debilitating and potentially fatal Neglected Tropical Disease caused by the single cell protozoan parasite Trypanosoma cruzi. To maintain viability and to reproduce under the harsh conditions within a host organism, pathogens express a variety of protecting enzymes and virulence factors that can serve as potential drug targets. To protect itself from redox stress, T. cruzi takes advantage of a unique thiol metabolism. For instance, a cytosolic peroxide clearance cascade is centered on the conserved oxidoreductase Tryparedoxin (Tpx). Tpx efficiently distributes reducing equivalents across the parasitic cell through the promiscuous yet selective binding of numerous up- and downstream clients. However, the exact structure and binding interfaces of this central protein binding hub remain unknown. To study the redox-dependent structural dynamics of T. cruzi Tpx, and its interactions with binding partners, we determined the 1H, 13C, 15N-backbone NMR assignments of the enzyme in the reduced and oxidized state. In agreement with earlier NMR studies on Tpx from related protozoans, we report redox-dependent changes in the enzyme's dithiol active site that could play a crucial role in the recognition of physiological substrates and should be considered in the rational design of small molecule inhibitors.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.6,"publicationDate":"2025-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144726342","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

¹H, ¹³C, ¹⁵N backbone chemical shift assignment of P18ink4c from Danio rerio (zebrafish) using solution-state NMR spectroscopy. 利用溶液态核磁共振光谱分析斑马鱼P18ink4c的1H， 13C， 15N主链化学位移。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-28 DOI: 10.1007/s12104-025-10245-2

Aakriti Sethi, Pierre de Cordovez, Biswaranjan Mohanty, Vanessa K Morris, Christoph Göbl

引用次数: 0

Backbone assignment of a 28.5 kDa class A extended spectrum β-lactamase by high-field, carbon-detected solid-state NMR. 一个28.5 kDa的a类扩展光谱β-内酰胺酶的高场碳检测固体核磁共振骨架分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-27 DOI: 10.1007/s12104-025-10242-5

Christopher G Williams, Songlin Wang, Alexander F Thome, Owen A Warmuth, Varun Sakhrani, Leighton Coates, Chad M Rienstra, Leonard J Mueller

引用次数: 0

NMR chemical shift assignment of UEV domain of ubiquitin-conjugating enzyme E2 variant 3 lactate dehydrogenase (UEVLD). 泛素偶联酶E2变体3乳酸脱氢酶（UEVLD） UEV结构域的NMR化学位移赋值。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-26 DOI: 10.1007/s12104-025-10240-7

Jose G Vazquez, David A Nyenhuis, Marie-Paule Strub, Nico Tjandra

{"title":"NMR chemical shift assignment of UEV domain of ubiquitin-conjugating enzyme E2 variant 3 lactate dehydrogenase (UEVLD).","authors":"Jose G Vazquez, David A Nyenhuis, Marie-Paule Strub, Nico Tjandra","doi":"10.1007/s12104-025-10240-7","DOIUrl":"https://doi.org/10.1007/s12104-025-10240-7","url":null,"abstract":"UEV domains are catalytically dead variants of the E2 enzymes which play an intermediate role in ubiquitin signaling. UEV domain containing proteins, like the ESCRT-I factor Tsg101 often play critical roles in trafficking of ubiquitylated cargos or in modulating ubiquitin processivity, or in determining the type of signal that is transferred to a target protein. Ubiquitin-conjugating enzyme E2 variant (UEV) and lactate/malate dehydrogenase (UEVLD), also known as UEV3, is a human paralogue of Tsg101 with apparent associations to cancer, innate immunity, NF-κB signaling, and autophagy. It contains an N-terminal UEV domain with 56% identity to that of Tsg101 and a C-terminal lactate dehydrogenase domain. Here, we show the backbone assignments of the UEV domain from UEVLD and find that its Cα shifts are consistent with a UEV domain composition. Further experiments suggest that it may have regions corresponding to the known binding pockets of Tsg101, but further structural and functional work will be required to uncover critical determinants of UEV domain function, and the role of these domains in Ubiquitin signaling as a whole.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144504408","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