The Experts below are selected from a list of 12 Experts worldwide ranked by ideXlab platform

E Guoji - One of the best experts on this subject based on the ideXlab platform.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, ICTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. (C) 2015 Elsevier B.V. All rights reserved.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels.

Lei Zhang - One of the best experts on this subject based on the ideXlab platform.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, ICTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. (C) 2015 Elsevier B.V. All rights reserved.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels.

Wanxia Shi - One of the best experts on this subject based on the ideXlab platform.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, ICTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. (C) 2015 Elsevier B.V. All rights reserved.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels.

Xianchun Zeng - One of the best experts on this subject based on the ideXlab platform.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, ICTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. (C) 2015 Elsevier B.V. All rights reserved.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels.

Mingkun Yang - One of the best experts on this subject based on the ideXlab platform.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, ICTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels. (C) 2015 Elsevier B.V. All rights reserved.

  • unique diversity of the venom peptides from the Scorpion androctonus bicolor revealed by transcriptomic and proteomic analysis
    Journal of Proteomics, 2015
    Co-Authors: Lei Zhang, Wanxia Shi, Xianchun Zeng, Mingkun Yang, Yao Nie, Aorigele Bao, E Guoji
    Abstract:

    Androctonus bicolor is one of the most Poisonous Scorpion species in the world. However, little has been known about the venom composition of the Scorpion. To better understand the molecular diversity and medical significance of the venom from the Scorpion, we systematically analyzed the venom components by combining transcriptomic and proteomic surveys. Random sequencing of 1000 clones from a cDNA library prepared from the venom glands of the Scorpion revealed that 70% of the total transcripts code for venom peptide precursors. Our efforts led to a discovery of 103 novel putative venom peptides. These peptides include NaTx-like, KTx-like and CaTx-like peptides, putative antimicrobial peptides, defensin-like peptides, BPP-like peptides, BmKa2-like peptides, Kunitz-type toxins and some new-type venom peptides without disulfide bridges, as well as many new-type venom peptides that are cross-linked with one, two, three, five or six disulfide bridges, respectively. We also identified three peptides that are identical to known toxins from Scorpions. The venom was also analyzed using a proteomic technique. The presence of a total of 16 different venom peptides was confirmed by LC-MS/MS analysis. The discovery of a wide range of new and new-type venom peptides highlights the unique diversity of the venom peptides from A. bicolor. These data also provide a series of novel templates for the development of therapeutic drugs for treating ion channel-associated diseases and infections caused by antibiotic-resistant pathogens, and offer molecular probes for the exploration of structures and functions of various ion channels.