Ji She
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View article: Molecular basis for substrate recognition and transport of mammalian taurine transporters
Molecular basis for substrate recognition and transport of mammalian taurine transporters Open
The taurine transporter (TAUT) mediates cellular taurine uptake, playing a critical role in human health and longevity. In this study, we present cryogenic electron microscopy structures of both mouse and human TAUT in various conformation…
View article: Structure and function of human XPR1 in phosphate export
Structure and function of human XPR1 in phosphate export Open
Xenotropic and polytropic retrovirus receptor 1 (XPR1) functions as a phosphate exporter and is pivotal in maintaining human phosphate homeostasis. It has been identified as a causative gene for primary familial brain calcification. Here w…
View article: Structural insights into IL-6 signaling inhibition by therapeutic antibodies
Structural insights into IL-6 signaling inhibition by therapeutic antibodies Open
Antibody inhibitors of the interleukin-6 (IL-6) signaling pathway, such as tocilizumab and sarilumab, have been used to treat rheumatoid arthritis, chimeric antigen receptor T cell-induced cytokine storm, and severe COVID-19 pneumonia. Her…
View article: Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter
Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter Open
Vitamin C (L-ascorbic acid) is an essential nutrient for human health, and its deficiency has long been known to cause scurvy. Sodium-dependent vitamin C transporters (SVCTs) are responsible for vitamin C uptake and tissue distribution in …
View article: Structure of the human CLC-7/Ostm1 complex reveals a novel state
Structure of the human CLC-7/Ostm1 complex reveals a novel state Open
CLC-7 functions as a Cl−/H+ exchanger in lysosomes. Defects in CLC-7 and its β-subunit, Ostm1, result in osteopetrosis and neurodegeneration. Here, we present the cryogenic electron microscopy (cryo-EM) structure of t…
View article: Cryo-EM structure of the plant nitrate transporter AtCLCa reveals characteristics of the anion-binding site and the ATP-binding pocket
Cryo-EM structure of the plant nitrate transporter AtCLCa reveals characteristics of the anion-binding site and the ATP-binding pocket Open
Nitrate is one of the major nitrogen sources for most plants. Chloride channel (CLC) proteins mediate the transport and vacuole storage of nitrate in plants, but the structural basis of nitrate transport by plant CLC proteins remains unkno…
View article: Structural insights into the Ca2+-dependent gating of the human mitochondrial calcium uniporter
Structural insights into the Ca2+-dependent gating of the human mitochondrial calcium uniporter Open
Mitochondrial Ca 2+ uptake is mediated by an inner mitochondrial membrane protein called the mitochondrial calcium uniporter. In humans, the uniporter functions as a holocomplex consisting of MCU, EMRE, MICU1 and MICU2, among which MCU and…
View article: Author response: Structural insights into the Ca2+-dependent gating of the human mitochondrial calcium uniporter
Author response: Structural insights into the Ca2+-dependent gating of the human mitochondrial calcium uniporter Open
View article: Structural insights into the Ca<sup>2+</sup>-dependent gating of the human mitochondrial calcium uniporter
Structural insights into the Ca<sup>2+</sup>-dependent gating of the human mitochondrial calcium uniporter Open
Mitochondrial Ca 2+ uptake plays an important role in cellular physiology such as modulating ATP production, regulating cytoplasmic Ca 2+ dynamics, and triggering cell death, and is mediated by the mitochondrial calcium uniporter, a highly…
View article: Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter
Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter Open
View article: Structural and functional characterization of an otopetrin family proton channel
Structural and functional characterization of an otopetrin family proton channel Open
The otopetrin (OTOP) proteins were recently characterized as proton channels. Here we present the cryo-EM structure of OTOP3 from Xenopus tropicalis (XtOTOP3) along with functional characterization of the channel. XtOTOP3 forms a homodimer…
View article: Author response: Structural and functional characterization of an otopetrin family proton channel
Author response: Structural and functional characterization of an otopetrin family proton channel Open
View article: Structural mechanisms of phospholipid activation of the human TPC2 channel
Structural mechanisms of phospholipid activation of the human TPC2 channel Open
Mammalian two-pore channels (TPCs) regulate the physiological functions of the endolysosome. Here we present cryo-EM structures of human TPC2 (HsTPC2), a phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2)-activated, Na+ selective channel, i…
View article: Author response: Structural mechanisms of phospholipid activation of the human TPC2 channel
Author response: Structural mechanisms of phospholipid activation of the human TPC2 channel Open
View article: Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel
Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel Open
View article: Structures of the calcium-activated, non-selective cation channel TRPM4
Structures of the calcium-activated, non-selective cation channel TRPM4 Open
View article: Structure of mammalian endolysosomal TRPML1 channel in nanodiscs
Structure of mammalian endolysosomal TRPML1 channel in nanodiscs Open
View article: The lysosomal potassium channel TMEM175 adopts a novel tetrameric architecture
The lysosomal potassium channel TMEM175 adopts a novel tetrameric architecture Open