15 results on '"Rui Kai Zhang"'
Search Results
2. RABL4/IFT27 in a nucleotide‐independent manner promotes phospholipase D ciliary retrieval via facilitating BBSome reassembly at the ciliary tip
- Author
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Yan‐Xia Liu, Rui‐Kai Zhang, and Zhen‐Chuan Fan
- Subjects
Physiology ,Clinical Biochemistry ,Cell Biology - Published
- 2023
3. RABL2 promotes the outward transition zone passage of signaling proteins in cilia via ARL3.
- Author
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Rui-Kai Zhang, Wei-Yue Sun, Yan-Xia Liu, Zhang, Emma Y., and Zhen-Chuan Fan
- Subjects
- *
GUANINE nucleotide exchange factors , *CILIA & ciliary motion , *HEDGEHOG signaling proteins , *PHOSPHOLIPASE D , *LAURENCE-Moon-Biedl syndrome - Abstract
Certain transmembrane and membrane-tethered signaling proteins export from cilia as BBSome cargoes via the outward BBSome transition zone (TZ) diffusion pathway, indispensable for maintaining their ciliary dynamics to enable cells to sense and transduce extracellular stimuli inside the cell. Murine Rab-like 2 (Rabl2) GTPase resembles Chlamydomonas Arf-like 3 (ARL3) GTPase in promoting outward TZ passage of the signaling protein cargo-laden BBSome. During this process, ARL3 binds to and recruits the retrograde IFT train-dissociated BBSome as its effector to diffuse through the TZ for ciliary retrieval, while how RABL2 and ARL3 cross talk in this event remains uncertain. Here, we report that Chlamydomonas RABL2 in a GTP-bound form (RABL2GTP) cycles through cilia via IFT as an IFT-B1 cargo, dissociates from retrograde IFT trains at a ciliary region right above the TZ, and converts to RABL2GDP for activating ARL3GDP as an ARL3 guanine nucleotide exchange factor. This confers ARL3GTP to detach from the ciliary membrane and become available for binding and recruiting the phospholipase D (PLD)-laden BBSome, autonomous of retrograde IFT association, to diffuse through the TZ for ciliary retrieval. Afterward, RABL2GDP exits cilia by being bound to the ARL3GTP/BBSome entity as a BBSome cargo. Our data identify ciliary signaling proteins exported from cilia via the RABL2-ARL3 cascade-mediated outward BBSome TZ diffusion pathway. According to this model, hedgehog signaling defect-induced Bardet-Biedl syndrome caused by RABL2 mutations in humans could be well explained in a mutation-specific manner, providing us with a mechanistic understanding behind the outward BBSome TZ passage required for proper ciliary signaling. [ABSTRACT FROM AUTHOR]
- Published
- 2023
- Full Text
- View/download PDF
4. Unraveling the Intricate Cargo-BBSome Coupling Mechanism at the Ciliary Tip
- Author
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Yan-Xia Liu, Wen-Juan Li, Rui-Kai Zhang, Sheng-Nan Sun, and Zhen-Chuan Fan
- Subjects
Multidisciplinary - Abstract
Certain ciliary transmembrane and membrane-tethered signaling proteins migrate from the ciliary tip to base via retrograde intraflagellar transport (IFT), essential for maintaining their ciliary dynamics to enable cells to sense and transduce extracellular stimuli inside the cell. During this process, the BBSome functions as an adaptor between retrograde IFT trains and these signaling protein cargoes. The Arf-like 13 (ARL13) small GTPase resembles ARL6/BBS3 in facilitating these signaling cargoes to couple with the BBSome at the ciliary tip prior to loading onto retrograde IFT trains for transporting towards the ciliary base, while the molecular basis for how this intricate coupling event happens remains elusive. Here, we report thatChlamydomonasARL13 only in a GTP-bound form (ARL13GTP) anchors to the membrane for diffusing into cilia. Upon entering cilia, ARL13 undergoes GTPase cycle for shuttling between the ciliary membrane (ARL13GTP) and matrix (ARL13GDP). To achieve this goal, the ciliary membrane-anchored BBS3GTPbinds and activates the ciliary matrix-residing ARL13GDPas an ARL13 guanine nucleotide exchange factor. At the ciliary tip, ARL13GTPbinds and recruits the ciliary matrix-residing and post-remodeled BBSome as an ARL13 effector to anchor to the ciliary membrane. This makes the BBSome spatiotemporally become available for the ciliary membrane-tethered phospholipase D (PLD) to couple with. Afterward, ARL13GTPhydrolyzes GTP for releasing the PLD-laden BBSome to load onto retrograde IFT trains. According to this model, hedgehog signaling defects associated withARL13bandBBS3mutations in humans could be satisfactorily explained, providing us a mechanistic understanding behind BBSome-cargo coupling required for proper ciliary signaling.Significance statementCertain signaling proteins export in a BBSome-dependent manner from cilia via retrograde IFT. As IFT cargoes, their coupling with the BBSome is mediated by ARL13 and BBS3. Here, we report that ARL13 in a GTP-bound state binds the membrane for diffusing into cilia followed by running GTPase cycle with BBS3 acting as an ARL13-specific guanine nucleotide exchange factor. ARL13GTPrecruits the IFT-shed BBSome as its effector to anchor to the membrane of the ciliary tip, making it spatiotemporally available for the ciliary membrane-tethered PLD to bind. Afterward, ARL13 GTP hydrolysis releases the PLD-laden BBSome for retrograde IFT train loading. ARL13 and BBS3 facilitate the cargo-BBSome coupling in such a way providing a regulatory mechanism for signaling protein export from cilia.
- Published
- 2022
5. RABL2 Regulates Ciliation via Controlling IFT-B1 Basal Body Recruitment and ARL3-mediated BBSome Ciliary Retrieval
- Author
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Rui-Kai Zhang, Yan-Xia Liu, Wei-Yue Sun, Dong-Xue Bao, Rui-Qin Jia, Chan Zhang, and Zhen-Chuan Fan
- Abstract
Highly conserved intraflagellar transport (IFT) trains and certain small GTPases coordinate to direct ciliation and to maintain the ciliary dynamics of signaling molecules via the IFT cargo adaptor BBSome. Unlike murine Rab-like 2 (RABL2) GTPase that enters cilia to drive outward transition zone (TZ) passage of the BBSome, human orthologue fails to enter cilia but resides at the ciliary base, indispensable for ciliation. However, mechanisms underlying how RABL2 regulates ciliation and BBSome barrier passage remain elusive. Here, we show that Chlamydomonas RABL2 regulates basal body targeting of the IFT-B1 subcomplex component of IFT trains as a RABL2-specific effector, mediating ciliation via controlling IFT-B1 basal body amount available for assembling anterograde IFT trains. RABL2GTP binds IFT-B1 to perform IFT; sheds from retrograde IFT trains at the proximal ciliary region right above the TZ; and converts to RABL2GDP rapidly. Next, RABL2GDP activates the ciliary membrane anchored Arf-like 3 (ARL3) GTPase (ARL3GDP) as a ARL3-specific guanine nucleotide exchange factor. Upon detaching from the ciliary membrane, the active ARL3GTP recruits its BBSome effector, autonomous of retrograde IFT train association, to move cross the TZ for ciliary retrieval. This ensures proper BBSome ciliary turnover for maintaining phototactic response of Chlamydomonas cells. For finishing RABL2 ciliary cycle, RABL2GDP passes the TZ for ciliary retrieval by loading onto the ARL3GTP/BBSome as a BBSome cargo. Our data thus propose that RABL2 mediates ciliation and BBSome ciliary retrieval simultaneously but via distinct molecular pathways.Significance statementIntraflagellar transport (IFT) and its cargo adaptor BBSome are indispensable for ciliation and ciliary singling. Rab-like 2 (RABL2) GTPase mediates ciliation and outward transition zone (TZ) passage of BBSomes with mechanisms yet to be determined. Here, we report that RABL2 decides ciliation by controlling the basal body amount of its effector IFT-B1 available for the assembly of anterograde IFT trains. RABL2GTP cycles through cilia as an IFT-B1 cargo; sheds from IFT at the ciliary base; and undergoes nucleotide exchange for activating ARL3 as an ARL3-specfic guanine nucleotide exchange factor. ARLGTP recruits IFT-shed BBSomes to pass the TZ for ciliary retrieval. RABL2GDP exists cilia via ARL3GTP/BBSome as a BBSome cargo. Therefore, RABL2 functions both outside and inside cilia for initiating IFT and BBSome ciliary retrieval, respectively.
- Published
- 2022
6. Unraveling the intricate cargo-BBSome coupling mechanism at the ciliary tip.
- Author
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Yan-Xia Liu, Wen-Juan Li, Rui-Kai Zhang, Sheng-Nan Sun, and Zhen-Chuan Fan
- Subjects
GUANINE nucleotide exchange factors ,HEDGEHOG signaling proteins ,PHOSPHOLIPASE D ,CELLULAR signal transduction - Abstract
Certain ciliary transmembrane and membrane-tethered signaling proteins migrate from the ciliary tip to base via retrograde intraflagellar transport (IFT), essential for maintaining their ciliary dynamics to enable cells to sense and transduce extracellular stimuli inside the cell. During this process, the BBSome functions as an adaptor between retrograde IFT trains and these signaling protein cargoes. The Arf-like 13 (ARL13) small GTPase resembles ARL6/BBS3 in facilitating these signaling cargoes to couple with the BBSome at the ciliary tip prior to loading onto retrograde IFT trains for transporting towards the ciliary base, while the molecular basis for how this intricate coupling event happens remains elusive. Here, we report that Chlamydomonas ARL13 only in a GTP-bound form (ARL13
GTP ) anchors to the membrane for diffusing into cilia. Upon entering cilia, ARL13 undergoes GTPase cycle for shuttling between the ciliary membrane (ARL13GTP ) and matrix (ARL13GDP ). To achieve this goal, the ciliary membrane-anchored BBS3GTP binds the ciliary matrix-residing ARL13GDP to activate the latter as an ARL13 guanine nucleotide exchange factor. At the ciliary tip, ARL13GTP recruits the ciliary matrix-residing and post-remodeled BBSome as an ARL13 effector to anchor to the ciliary membrane. This makes the BBSome spatiotemporally become available for the ciliary membrane-tethered phospholipase D (PLD) to couple with. Afterward, ARL13GTP hydrolyzes GTP for releasing the PLD-laden BBSome to load onto retrograde IFT trains. According to this model, hedgehog signaling defects associated with ARL13b and BBS3 mutations in humans could be satisfactorily explained, providing us a mechanistic understanding behind BBSome-cargo coupling required for proper ciliary signaling. [ABSTRACT FROM AUTHOR]- Published
- 2023
- Full Text
- View/download PDF
7. ARL3 Mediates BBSome Ciliary Turnover by Promoting Its Outward Diffusion through the Transition Zone
- Author
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Yan-Xia Liu, Wen-Juan Li, Zhen-Chuan Fan, Bin Xue, Xixian Xie, Wei-Yue Sun, and Rui-Kai Zhang
- Subjects
BBSome ,biology ,Effector ,Chemistry ,Intraflagellar transport ,Phospholipase D ,Cilium ,Chlamydomonas ,GTPase ,biology.organism_classification ,Ciliary membrane ,Cell biology - Abstract
Ciliary receptors and their certain downstream signaling components undergo intraflagellar transport (IFT) as BBSome cargoes to maintain their ciliary dynamics for sensing and transducing extracellular stimuli inside the cell. Cargo laden BBSomes shed from retrograde IFT at the proximal ciliary region above the transition zone (TZ) followed by diffusing through the TZ for ciliary retrieval, while how the BBSome barrier passage is controlled remains elusive. Here, we show that the BBSome is a major effector of the Arf-like 3 (ARL3) GTPase in Chlamydomonas. Under physiological condition, ARL3GDP binds the membrane for diffusing into and residing in cilia. Following a nucleotide conversion, ARL3GTP dissociates with the ciliary membrane and binds and recruits the IFT-detached and cargo (phospholipase D, PLD)-laden BBSome at the proximal ciliary region to diffuse through the TZ and out of cilia. ARL3 deficiency impairs ciliary signaling, e.g. phototaxis of Chlamydomonas cells, by disrupting BBSome ciliary retrieval, providing a mechanistic understanding behind BBSome ciliary turnover required for ciliary signaling.
- Published
- 2021
8. ARL3 mediates BBSome ciliary turnover by promoting its outward movement across the transition zone
- Author
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Yan-Xia Liu, Wei-Yue Sun, Bin Xue, Rui-Kai Zhang, Wen-Juan Li, Xixian Xie, and Zhen-Chuan Fan
- Subjects
Protein Transport ,ADP-Ribosylation Factors ,Nucleotides ,Chlamydomonas ,Phospholipase D ,Cell Biology ,Cilia ,GTP Phosphohydrolases - Abstract
Ciliary receptors and their certain downstream signaling components undergo intraflagellar transport (IFT) as BBSome cargoes to maintain their ciliary dynamics for sensing and transducing extracellular stimuli inside the cell. Cargo-laden BBSomes pass the transition zone (TZ) for ciliary retrieval, but how this passage is controlled remains elusive. Here, we show that phospholipase D (PLD)-laden BBSomes shed from retrograde IFT trains at the proximal ciliary region right above the TZ to act as Arf-like 3 (ARL3) GTPase-specific effectors in Chlamydomonas cilia. Under physiological condition, ARL3GDP binds to the membrane for diffusing into cilia. Following nucleotide exchange, ARL3GTP detaches from the ciliary membrane, binds to retrograde IFT train-shed and PLD-laden BBSomes at the proximal ciliary region right above the TZ, and recruits them to pass the TZ for ciliary retrieval likely via diffusion. ARL3 mediates the ciliary dynamics of certain signaling molecules through facilitating BBSome ciliary retrieval, providing a mechanistic understanding behind why ARL3-related Joubert syndrome shares overlapping phenotypes with Bardet-Biedl syndrome.
- Published
- 2021
9. Chlamydomonas LZTFL1 mediates phototaxis via controlling BBSome recruitment to the basal body and its reassembly at the ciliary tip
- Author
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Yan-Xia Liu, Mingfu Wu, Wen Xin, Bin Xue, Rong-Chao Li, Zhen-Chuan Fan, Wei-Yue Sun, and Rui-Kai Zhang
- Subjects
Multidisciplinary ,BBSome ,biology ,Chemistry ,Cilium ,Chlamydomonas ,GTPase ,Biological Sciences ,biology.organism_classification ,Cell biology ,Intraflagellar transport ,Basal body ,Ciliary tip ,Ciliary membrane - Abstract
Many G protein–coupled receptors and other signaling proteins localize to the ciliary membrane for regulating diverse cellular processes. The BBSome composed of multiple Bardet–Biedl syndrome (BBS) proteins is an intraflagellar transport (IFT) cargo adaptor essential for sorting signaling proteins in and/or out of cilia via IFT. Leucine zipper transcription factor-like 1 (LZTFL1) protein mediates ciliary signaling by controlling BBSome ciliary content, reflecting how LZTFL1 mutations could cause BBS. However, the mechanistic mechanism underlying this process remains elusive thus far. Here, we show that LZTFL1 maintains BBSome ciliary dynamics by finely controlling BBSome recruitment to the basal body and its reassembly at the ciliary tip simultaneously in Chlamydomonas reinhardtii. LZTFL1 directs BBSome recruitment to the basal body via promoting basal body targeting of Arf-like 6 GTPase BBS3, thus deciding the BBSome amount available for loading onto anterograde IFT trains for entering cilia. Meanwhile, LZTFL1 stabilizes the IFT25/27 component of the IFT-B1 subcomplex in the cell body so as to control its presence and amount at the basal body for entering cilia. Since IFT25/27 promotes BBSome reassembly at the ciliary tip for loading onto retrograde IFT trains, LZTFL1 thus also directs BBSome removal out of cilia. Therefore, LZTFL1 dysfunction deprives the BBSome of ciliary presence and generates Chlamydomonas cells defective in phototaxis. In summary, our data propose that LZTFL1 maintains BBSome dynamics in cilia by such a dual-mode system, providing insights into how LZTFL1 mediates ciliary signaling through maintaining BBSome ciliary dynamics and the pathogenetic mechanism of the BBS disorder as well.
- Published
- 2021
10. Safety assessment of external defects in the nozzle-head intersection of a nuclear steam generator
- Author
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Jian-Ping Tan, Rui-Kai Zhang, Yue Li, Xin Zeng, Pan Liu, Da-Sheng Wang, and Ting Jin
- Subjects
Mechanics of Materials ,Mechanical Engineering ,General Materials Science - Published
- 2022
11. Chlamydomonas LZTFL1 mediates phototaxis via controlling BBSome recruitment to the basal body and its reassembly at the ciliary tip.
- Author
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Wei-Yue Sun, Bin Xue, Yan-Xia Liu, Rui-Kai Zhang, Rong-Chao Li, Wen Xin, Mingfu Wu, and Zhen-Chuan Fan
- Subjects
CILIARY body ,PHOTOTAXIS ,CHLAMYDOMONAS ,G protein coupled receptors ,IMMOBILIZED proteins ,LABOR demand ,COMMERCIAL products - Abstract
Many G protein-coupled receptors and other signaling proteins localize to the ciliary membrane for regulating diverse cellular processes. The BBSome composed of multiple Bardet-Biedl syndrome (BBS) proteins is an intraflagellar transport (IFT) cargo adaptor essential for sorting signaling proteins in and/or out of cilia via IFT. Leucine zipper transcription factor-like 1 (LZTFL1) protein mediates ciliary signaling by controlling BBSome ciliary content, reflecting how LZTFL1 mutations could cause BBS. However, the mechanistic mechanism underlying this process remains elusive thus far. Here, we show that LZTFL1 maintains BBSome ciliary dynamics by finely controlling BBSome recruitment to the basal body and its reassembly at the ciliary tip simultaneously in Chlamydomonas reinhardtii. LZTFL1 directs BBSome recruitment to the basal body via promoting basal body targeting of Arf-like 6 GTPase BBS3, thus deciding the BBSome amount available for loading onto anterograde IFT trains for entering cilia. Meanwhile, LZTFL1 stabilizes the IFT25/27 component of the IFT-B1 subcomplex in the cell body so as to control its presence and amount at the basal body for entering cilia. Since IFT25/27 promotes BBSome reassembly at the ciliary tip for loading onto retrograde IFT trains, LZTFL1 thus also directs BBSome removal out of cilia. Therefore, LZTFL1 dysfunction deprives the BBSome of ciliary presence and generates Chlamydomonas cells defective in phototaxis. In summary, our data propose that LZTFL1 maintains BBSome dynamics in cilia by such a dualmode system, providing insights into how LZTFL1 mediates ciliary signaling through maintaining BBSome ciliary dynamics and the pathogenetic mechanism of the BBS disorder as well. [ABSTRACT FROM AUTHOR]
- Published
- 2021
- Full Text
- View/download PDF
12. Cadmium induces cell centrosome amplification via reactive oxygen species as well as endoplasmic reticulum stress pathway
- Author
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Shao Chin Lee, Yu Cheng Lu, Rui Kai Zhang, Lan Wang, Lang Lang, and Pu Wang
- Subjects
inorganic chemicals ,0301 basic medicine ,Proteomics ,Small interfering RNA ,Physiology ,MAP Kinase Signaling System ,Clinical Biochemistry ,03 medical and health sciences ,0302 clinical medicine ,Downregulation and upregulation ,Cell Line, Tumor ,Humans ,ASK1 ,Phosphorylation ,chemistry.chemical_classification ,Centrosome ,Reactive oxygen species ,Endoplasmic reticulum ,JNK Mitogen-Activated Protein Kinases ,Cell Biology ,Endoplasmic Reticulum Stress ,HCT116 Cells ,Cell biology ,Up-Regulation ,030104 developmental biology ,chemistry ,030220 oncology & carcinogenesis ,Unfolded protein response ,Reactive Oxygen Species ,Cadmium ,Signal Transduction - Abstract
There is evidence that cadmium can initiate carcinogenesis. However, the underlying mechanisms remain unknown. There is also evidence that moderate centrosome amplification can initiate tumorigenesis. The present study investigated whether cadmium could trigger cell centrosome amplification, and examined the underlying molecular mechanisms. We found that cadmium was able to cause cell centrosome amplification at the subtoxic concentrations, in a dose-dependent manner. It could cause centrosome amplification via the signaling of reactive oxygen species (ROS). Proteomic analysis revealed that cadmium caused differential expressions of three proteins, which included HSPA1A which is associated with endoplasmic reticulum (ER) stress. Western blot analysis confirmed that cadmium upregulated HSPA1A. Further analyses showed that cadmium upregulated Bip and decreased the phosphorylation of ASK1 as well as increased the phosphorylation of MKK7 and c-Jun N-terminal kinases (JNK). Knockdown of JNK2 using small interfering RNA inhibited the cadmium-induced centrosome amplification but not the level of ROS. N-acetylcysteine did not inhibit the cadmium-activated ER stress pathway. In conclusion, our results suggest that cadmium can induce cell centrosome amplification via ROS as well as ER stress through the Bip-TRAF2-ASK1-MKK7-JNK signaling route, in parallel. More studies are required to clarify whether centrosome amplification underlies cadmium-induced carcinogenesis.
- Published
- 2018
13. Hsp74/14-3-3σ Complex Mediates Centrosome Amplification by High Glucose, Insulin, and Palmitic Acid
- Author
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Yu Cheng Lu, Pu Wang, Rui Kai Zhang, Yuan Fei Li, Qi Gui Wu, Shao Chin Lee, and Alice Kong
- Subjects
medicine.medical_treatment ,Blotting, Western ,Palmitic Acid ,Biochemistry ,Ribosome ,Mass Spectrometry ,Palmitic acid ,Mitochondrial Proteins ,03 medical and health sciences ,chemistry.chemical_compound ,Biosynthesis ,medicine ,Humans ,Insulin ,ROCK1 ,HSP70 Heat-Shock Proteins ,Molecular Biology ,030304 developmental biology ,chemistry.chemical_classification ,Centrosome ,0303 health sciences ,Gene knockdown ,Microscopy, Confocal ,030302 biochemistry & molecular biology ,Computational Biology ,HCT116 Cells ,Amino acid ,Molecular Docking Simulation ,Glucose ,chemistry ,14-3-3 Proteins ,Carrier Proteins ,Protein Binding - Abstract
It has been reported recently that type 2 diabetes promotes centrosome amplification via 14-3-3σ/ROCK1 complex. In the present study, 14-3-3σ interacting proteins are characterized and their roles in the centrosome amplification by high glucose, insulin, and palmitic acid are investigated. Co-immunoprecipitation in combination with MS analysis identified 134 proteins that interact with 14-3-3σ, which include heat shock 70 kDa protein 4 (Hsp74). Gene ontology analyses reveal that many of them are enriched in binding activity. Kyoto Encyclopedia of Genes and Genomes analysis shows that the top three enriched pathways are ribosome, carbon metabolism, and biosynthesis of amino acids. Molecular and functional investigations show that the high glucose, insulin, and palmitic acid increase the expression and binding of 14-3-3σ and Hsp74 as well as centrosome amplification, all of which are inhibited by knockdown of 14-3-3σ or Hsp74. Moreover, molecular docking analysis shows that the interaction between the 14-3-3σ and the Hsp74 is mainly through hydrophobic contacts and a lesser degree ionic interactions and hydrogen bond by different amino acids residues. In conclusion, the results suggest that the experimental treatment triggers centrosome amplification via upregulations of expression and binding of 14-3-3σ and Hsp74.
- Published
- 2018
14. A Comparative Study on the Self Diffusion of N-Octadecane with Crystal and Amorphous Structure by Molecular Dynamics Simulation
- Author
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Zhonghao Rao, Yimin Li, Xinjian Liu, Chang-Xing Wei, Xiang Li, Hao-Dong Wang, and Rui-Kai Zhang
- Subjects
Crystal ,Self-diffusion ,chemistry.chemical_compound ,Phase change ,Molecular dynamics ,Materials science ,Octadecane ,chemistry ,General Physics and Astronomy ,Thermodynamics ,Diffusion (business) ,Thermal energy storage ,Amorphous solid - Abstract
The straight chain n-alkanes and their mixture, which can be used as phase change materials (PCM) for thermal energy storage, have attracted much attention in recent years. We employ the molecular dynamics (MD) simulation to investigate their thermophysical properties, including self diffusion and melting of n-octadecane with crystal and amorphous structures. Our results show that, although the initial and melted structures of n-octadecane with crystal and amorphous are different, the melting behaviors of n-octadecane judged by the self diffusion behavior are consistent. The MD simulation indicates that both the crystal and amorphous structures are effective for the property investigation of n-octadecane and the simulated conclusion can be used as reference for modeling the alkanes-based PCM system.
- Published
- 2014
15. A Comparative Study on the Self Diffusion of N-Octadecane with Crystal and Amorphous Structure by Molecular Dynamics Simulation.
- Author
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Zhong-Hao, Rao, Xin-Jian, Liu, Rui-Kai, Zhang, Xiang, Li, Chang-Xing, Wei, Hao-Dong, Wang, and Yi-Min, Li
- Subjects
PHASE change materials ,HEAT storage devices ,MOLECULAR dynamics ,THERMOPHYSICAL properties ,THERMAL properties of condensed matter ,ALKANES - Abstract
The straight chain n-alkanes and their mixture, which can be used as phase change materials (PCM) for thermal energy storage, have attracted much attention in recent years. We employ the molecular dynamics (MD) simulation to investigate their thermophysical properties, including self diffusion and melting of n-octadecane with crystal and amorphous structures. Our results show that, although the initial and melted structures of n-octadecane with crystal and amorphous are different, the melting behaviors of n-octadecane judged by the self diffusion behavior are consistent. The MD simulation indicates that both the crystal and amorphous structures are effective for the property investigation of n-octadecane and the simulated conclusion can be used as reference for modeling the alkanes-based PCM system. [ABSTRACT FROM AUTHOR]
- Published
- 2014
- Full Text
- View/download PDF
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