Nature Search

Revealing the aging process of solid electrolyte interphase on SiO_x anode

Observing the evolution of the solid electrolyte interphase on SiO_x-based electrodes in Li-ion batteries is challenging. Here, authors use three-dimensional tomography to visualize the growth of the interphase on single SiO_x particles and propose a mechanical confinement strategy to prevent aging.

Guoyu Qian
Yiwei Li
Feng Pan
ResearchOpen Access28 Sept 2023
Nature Communications

Volume: 14, P: 1-9
RING tetramerization is required for nuclear body biogenesis and PML sumoylation

Promyelocytic leukemia protein (PML) is a scaffolding protein that organizes PML nuclear bodies. Here the authors present the tetrameric crystal structure of the PML RING domain and show that RING tetramerization is functionally important for nuclear body formation and PML sumoylation.

Pengran Wang
Shirine Benhenda
Guoyu Meng
ResearchOpen Access29 Mar 2018
Nature Communications

Volume: 9, P: 1-10
Publisher Correction: RING tetramerization is required for nuclear body biogenesis and PML sumoylation

Pengran Wang
Shirine Benhenda
Guoyu Meng
Amendments and CorrectionsOpen Access04 May 2018
Nature Communications

Volume: 9, P: 1
HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells

The transcriptional repressor Blimp-1 has an important role in B-cell differentiation. Here the authors show that lymphoma-associated Blimp-1 mutants are selectively recognized by HSP70-Hrd1, which leads to their accelerated degradation and propose HSP70 inhibition as a therapeutic approach for certain lymphomas.

Wen-Fang Wang
Li Yan
Jiang Zhu
ResearchOpen Access25 Aug 2017
Nature Communications

Volume: 8, P: 1-16
Cellular hierarchy insights reveal leukemic stem-like cells and early death risk in acute promyelocytic leukemia

The cellular hierarchies in acute promyelocytic leukemia (APL) remain to be explored. Here, the authors perform single-cell RNA sequencing of 16 APL patients to characterise its cellular composition and develop an APL-specific stemness score for assessing the risk of early death in APL.

Wen Jin
Yuting Dai
Kankan Wang
ResearchOpen Access16 Feb 2024
Nature Communications

Volume: 15, P: 1-16
B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis

Promyelocytic leukemia protein (PML) is the scaffolding protein that organizes PML nuclear bodies. Here the authors determine the crystal structure of a PML B1-box multimer and characterise the oligomerisation behaviour of the PML RBCC construct and show that disrupting B1-B1 interactions precludes promyelocytic leukemia leukemogenesis in transgenic mice.

Yuwen Li
Xiaodan Ma
Guoyu Meng
ResearchOpen Access22 Aug 2019
Nature Communications

Volume: 10, P: 1-13
MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism

Microtubules regulate activation of the NLRP3 inflammasome, but the underlying molecular mechanism is unclear. Here the authors show that MARK4 binds NLRP3 and shuttles it to the microtubule-organizing centre to promote optimal inflammasome activation.

Xuan Li
Sarah Thome
Ziad Mallat
ResearchOpen Access28 Jun 2017
Nature Communications

Volume: 8, P: 1-13
Structural framework of fructosyl transfer in Bacillus subtilis levansucrase

Guoyu Meng
Klaus Fütterer
Research28 Sept 2003
Nature Structural & Molecular Biology

Volume: 10, P: 935-941
Functional and molecular features of the calmodulin-interacting protein IQCG required for haematopoiesis in zebrafish

NUP98–IQCG is a fusion protein found in acute leukaemia that functions as a regulator of transcriptional expression. Here, Chen et al. investigate IQCG-mediated calcium signalling in haematopoiesis, and propose a model where IQCG can store calmodulin, which once released, activates CaM-dependent kinase IV.

Li-Ting Chen
Wen-Xue Liang
Sai-Juan Chen
Research02 May 2014
Nature Communications

Volume: 5, P: 1-12
DUX4_HD2-DNA_ERG structure reveals new insight into DUX4-Responsive-Element

Xue Dong
Hao Zhang
Guoyu Meng
ResearchOpen Access12 Oct 2018
Leukemia

Volume: 33, P: 550-553
Exome sequencing identifies somatic mutations of DDX3X in natural killer/T-cell lymphoma

Zhu Chen, Sai-Juan Chen, Wei-Li Zhao and colleagues identify recurrent loss-of-function mutations in the RNA helicase gene DDX3X in 20% of subjects with natural killer/T-cell lymphoma (NKTCL) in their study. The results suggest that DDX3X acts as a tumor suppressor and that its inactivation leads to poor clinical outcome.

Lu Jiang
Zhao-Hui Gu
Sai-Juan Chen
Research20 Jul 2015
Nature Genetics

Volume: 47, P: 1061-1066
Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism

Yangxia Tan
Jiawei Li
Guoyu Meng
ResearchOpen Access25 Nov 2024
Cell Discovery

Volume: 10, P: 1-11
Structural basis of DUX4/IGH-driven transactivation

Xue Dong
Weina Zhang
Guoyu Meng
ResearchOpen Access15 Mar 2018
Leukemia

Volume: 32, P: 1466-1476

Search

Revealing the aging process of solid electrolyte interphase on SiO_x anode

RING tetramerization is required for nuclear body biogenesis and PML sumoylation

Publisher Correction: RING tetramerization is required for nuclear body biogenesis and PML sumoylation

HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells

Cellular hierarchy insights reveal leukemic stem-like cells and early death risk in acute promyelocytic leukemia

B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis

MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism

Structural framework of fructosyl transfer in Bacillus subtilis levansucrase

Functional and molecular features of the calmodulin-interacting protein IQCG required for haematopoiesis in zebrafish

DUX4_HD2-DNA_ERG structure reveals new insight into DUX4-Responsive-Element

Exome sequencing identifies somatic mutations of DDX3X in natural killer/T-cell lymphoma

Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism

Structural basis of DUX4/IGH-driven transactivation

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