Jianlin Lei
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View article: A three-component signaling system plays multiple roles in the pathogenicity of Xanthomonas citri subsp. citri
A three-component signaling system plays multiple roles in the pathogenicity of Xanthomonas citri subsp. citri Open
Two-component signaling systems play crucial roles in bacteria by enabling them to sense and respond to environmental changes. These systems typically consist of a sensor kinase protein and a response regulator protein. The involvement of …
View article: Structural insights into human exon-defined spliceosome prior to activation
Structural insights into human exon-defined spliceosome prior to activation Open
Spliceosome is often assembled across an exon and undergoes rearrangement to span a neighboring intron. Most states of the intron-defined spliceosome have been structurally characterized. However, the structure of a fully assembled exon-de…
View article: Dynamic and multivalent engagement determines context-dependent nucleosomal deacetylation by the Rpd3S complex
Dynamic and multivalent engagement determines context-dependent nucleosomal deacetylation by the Rpd3S complex Open
Context-dependent dynamic histone modifications constitute a key epigenetic mechanism in gene regulation. The Rpd3S complex recognizes H3K36 trimethylation (H3K36me3) and deacetylates histones H3 and H4 at multiple sites across transcribed…
View article: Structural and functional insights of the human peroxisomal ABC transporter ALDP
Structural and functional insights of the human peroxisomal ABC transporter ALDP Open
Adrenoleukodystrophy protein (ALDP) is responsible for the transport of very-long-chain fatty acids (VLCFAs) and corresponding CoA-esters across the peroxisomal membrane. Dysfunction of ALDP leads to peroxisomal metabolic disorder exemplif…
View article: Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis
Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis Open
The voltage-gated potassium channel AKT1 is responsible for primary K + uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium channel α-subunit AtKC1. However, the molec…
View article: Structure of the cytoplasmic ring of the <i>Xenopus laevis</i> nuclear pore complex
Structure of the cytoplasmic ring of the <i>Xenopus laevis</i> nuclear pore complex Open
INTRODUCTION The nuclear pore complex (NPC) resides on the nuclear envelope (NE) and mediates nucleocytoplasmic cargo transport. As one of the largest cellular machineries, a vertebrate NPC consists of cytoplasmic filaments, a cytoplasmic …
View article: Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex
Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex Open
Nuclear pore complex (NPC) shuttles cargo across the nuclear envelope. Here we present single-particle cryo-EM structure of the nuclear ring (NR) subunit from Xenopus laevis NPC at an average resolution of 5.6 Å. The NR subunit comprises t…
View article: Near-atomic Structure of the Cytoplasmic Ring of the <i>Xenopus laevis</i> Nuclear Pore Complex
Near-atomic Structure of the Cytoplasmic Ring of the <i>Xenopus laevis</i> Nuclear Pore Complex Open
The nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-EM structure of the cytoplasmic ring (CR) from the Xenopus laevis NPC at 4.1-4.7 Å resolutions. The structure of an N-terminal domain…
View article: Cryo-EM structure of the Inner Ring from<i>Xenopus laevis</i>Nuclear Pore Complex
Cryo-EM structure of the Inner Ring from<i>Xenopus laevis</i>Nuclear Pore Complex Open
Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy (cryo-EM) structure of the inner ring (IR) subunit from Xenopus laevis NPC at an average resolution of 4.4 Å. The sym…
View article: Structure insights of the human peroxisomal ABC transporter ALDP
Structure insights of the human peroxisomal ABC transporter ALDP Open
Adrenoleukodystrophy protein (ALDP) is responsible for the transport of free very-long-chain fatty acids (VLCFAs) and corresponding CoA-esters across the peroxisomal membrane. ALDP belongs to the ATP-binding cassette sub-family D, which is…
View article: Structure of human Na <sub>v</sub> 1.5 reveals the fast inactivation-related segments as a mutational hotspot for the long QT syndrome
Structure of human Na <sub>v</sub> 1.5 reveals the fast inactivation-related segments as a mutational hotspot for the long QT syndrome Open
Significance Dysfunction of Na v 1.5, the primary cardiac Na v channel, is associated with multiple arrhythmia syndromes, exemplified by type 3 long QT syndrome (LQT3) and Brugada syndrome (BrS). Establishment of the structure-function rel…
View article: Comparative structural analysis of human Na <sub>v</sub> 1.1 and Na <sub>v</sub> 1.5 reveals mutational hotspots for sodium channelopathies
Comparative structural analysis of human Na <sub>v</sub> 1.1 and Na <sub>v</sub> 1.5 reveals mutational hotspots for sodium channelopathies Open
Significance Na v 1.1 is a major Na v subtype in the brain. Up to 900 nonsense and missense mutations in SCN1A , the coding gene for Na v 1.1, have been identified in patients with epilepsy syndromes. Here, we report the cryo-EM structure …
View article: Structure of human Na<sub>v</sub>1.5 reveals the fast inactivation-related segments as a mutational hotspot for the Long QT Syndrome
Structure of human Na<sub>v</sub>1.5 reveals the fast inactivation-related segments as a mutational hotspot for the Long QT Syndrome Open
Na v 1.5 is the primary voltage-gated Na + (Na v ) channel in the heart. Mutations of Na v 1.5 are associated with various cardiac disorders exemplified by the type 3 long QT syndrome (LQT3) and Brugada syndrome (BrS). E1784K is a common m…
View article: A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols
A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols Open
A cellular cholesterol sensor Cholesterol levels in cells are controlled by the sterol regulatory element–binding protein (SREBP) pathway. When the cell has sufficient cholesterol, the transcription factor that regulates cholesterol metabo…
View article: Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence
Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence Open
The human SLC26 transporter family exhibits various transport characteristics, and family member SLC26A9 performs multiple roles, including acting as Cl – /HCO 3 – exchangers, Cl – channels, and Na + transporters. Some mutations of SLC26A9…
View article: Molecular architecture of the SARS-CoV-2 virus
Molecular architecture of the SARS-CoV-2 virus Open
SUMMARY Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins and the complexes of the spike (…
View article: Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis
Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis Open
The nuclear pore complex (NPC) exhibits structural plasticity and has only been characterized at local resolutions of up to 15 Å for the cytoplasmic ring (CR). Here we present a single-particle cryo-electron microscopy (cryo-EM) structure …
View article: Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex
Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex Open
The nuclear pore complex (NPC) mediates the flow of substances between the nucleus and cytoplasm in eukaryotic cells. Here we report the cryo-electron tomography (cryo-ET) structure of the luminal ring (LR) of the NPC from Xenopus laevis o…
View article: Cryo-EM structure of the human heteromeric amino acid transporter b <sup>0,+</sup> AT-rBAT
Cryo-EM structure of the human heteromeric amino acid transporter b <sup>0,+</sup> AT-rBAT Open
Cryo-EM structures of the b 0,+ AT-rBAT complex are revealed, providing clues for the substrate recognition and transport mechanism.
View article: Molecular architecture of the luminal ring of the<i>Xenopus laevis</i>nuclear pore complex
Molecular architecture of the luminal ring of the<i>Xenopus laevis</i>nuclear pore complex Open
Nuclear pore complex (NPC) mediates the flow of substances between the nucleus and cytoplasm in eukaryotic cells. Here we report the cryo-electron tomography (cryo-ET) structure of the luminal ring (LR) of the NPC from Xenopus laevis oocyt…