cathelicidin-oa1 a novel antioxidant peptide identified

cathelicidin-oa1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from

1. Sci Rep. 2018 Jan 17;8(1):943. doi: 10.1038/s41598-018-19486-9. Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing.

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cathelicidin-oa1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a Novel Antioxidant Peptide Identified From

Cathelicidin-OA1, a Novel Antioxidant Peptide Identified From an Amphibian, Accelerates Skin Wound Healing Sci Rep . 2018 Jan 17;8(1):943. doi: 10.1038/s41598-018-19486-9.

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cathelicidin-oa1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from

In the present study, a novel cathelicidin-like peptide, cathelicidin-OA1, was identified from O. andersonii skin secretions. Our results demonstrated that this novel peptide could promote wound

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cathelicidin-oa1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing Xiaoqing Cao , # 1 Ying Wang , # 2 Chunyun Wu , # 3 Xiaojie Li , 4 Zhe Fu , 3 Meifeng Yang , 3 Wenxin Bian , 3 Siyuan Wang , 2 Yongli Song , 3 Jing Tang , 4 and Xinwang Yang 3

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author correction: cathelicidin-oa1, a novel antioxidant

Author Correction: Cathelicidin-OA1, a novel antioxidant

Author Correction: Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing Sci Rep . 2018 Oct 23;8(1):15906. doi: 10.1038/s41598-018-33558-w.

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cathelicidin-oa1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from

Cathelicidins play pivotal roles in host defense. The discovery of novel cathelicidins is important research; however, despite the identification of many cathelicidins in vertebrates, few have been reported in amphibians. Here we identified a novel cathelicidin (named cathelicidin-OA1) from the skin of an amphibian species, Odorrana andersonii. Produced by posttranslational processing of a 198

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author correction: cathelicidin-oa1, a novel antioxidant

Author Correction: Cathelicidin-OA1, a novel antioxidant

Author Correction: Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing Xiaoqing Cao 1 na1 , Ying Wang 2 na1 ,

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fm-cath, a novel cathelicidin from fejervarya multistriata

FM-CATH, A Novel Cathelicidin From Fejervarya Multistriata

Cathelicidin-OA1, a Novel Antioxidant Peptide Identified from an Amphibian, Accelerates Skin Wound Healing. Sci. Rep. 8 , 943. 10.1038/s41598-018-19486-9 [ PMC free article ] [ PubMed ] [ CrossRef ] [ Google Scholar ]

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cathelicidin-oa1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing By Xiaoqing Cao, Ying Wang, Chunyun Wu, Xiaojie Li, Zhe Fu, Meifeng Yang, Wenxin Bian, Siyuan Wang, Yongli Song, Jing Tang and Xinwang Yang

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derivatives of gecko cathelicidin-related antioxidant peptide

Derivatives of gecko cathelicidin-related antioxidant peptide

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing Sci. Rep. , 8 ( 2018 ) , p. 15 , 10.1038/s41598-018-19486-9

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a novel anionic cathelicidin lacking direct antimicrobial

A novel anionic cathelicidin lacking direct antimicrobial

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing. Here we identified a novel cathelicidin (named cathelicidin-OA1) from the skin of an

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[pdf] rich diversity and potency of skin antioxidant peptides

[PDF] Rich diversity and potency of skin antioxidant peptides

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing Xiaoqing Cao , Ying Wang , +8 authors Xinwang Yang Biology, Medicine

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frontiers | fm-cath, a novel cathelicidin from fejervarya

Frontiers | FM-CATH, A Novel Cathelicidin From Fejervarya

Sepsis is an exacerbated inflammatory reaction induced by severe infection. As important defensive molecules in innate immunity, several AMPs are reported to prevent septic shock. In this study, we characterized a novel cathelicidin, FM-CATH, from the frog skin of F. multistriata. FM-CATH was found to adopt an amphipathic α-helix structural in membrane-mimetic environments and possess

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cathelicidin-dm is an antimicrobial peptide from duttaphrynus

Cathelicidin-DM is an Antimicrobial Peptide from Duttaphrynus

A cathelicidin AMP was identified and named cathelicidin-DM, which is the first identified cathelicidin AMP from D. melanostictus. 50−52 According to the RT-PCR analysis results, the expression pattern of cathelicidin-DM is similar to the expression patterns of other amphibian cathelicidins. 21 − 23 , 28 Notably, the expression of

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the first identified cathelicidin from tree frogs possesses

The first identified cathelicidin from tree frogs possesses

The current work identified a novel defensive peptide (cathelicidin-PP) from the skin of the tree frog P. puerensis. The structural organization of cathelicidin-PP precursor (Fig. 2) is similar to other vertebrate cathelicidin Fig. 9 Effects of cathelicidinPP on LPS-induced inflammatory response pathways. a Western blot of phosphorylation of

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identification and characterization of a novel gene-encoded

Identification and Characterization of a Novel Gene-encoded

Here, we identified and named a novel gene-encoded antioxidant peptide from the skin secretions of an odorous frog species, which may assist in the development of potential antioxidant candidates. Conclusion: This study may help improve our understanding of the molecular basis of amphibians’ adaptation to environments experiencing long-term

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a novel anionic cathelicidin lacking direct antimicrobial

A novel anionic cathelicidin lacking direct antimicrobial

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing. Here we identified a novel cathelicidin (named cathelicidin-OA1) from the skin of an

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author correction: cathelicidin-oa1, a novel antioxidant

Author Correction: Cathelicidin-OA1, a novel antioxidant

Author Correction: Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing By Xiaoqing Cao, Ying Wang, Chunyun Wu, Xiaojie Li, Zhe Fu, Meifeng Yang, Wenxin Bian, Siyuan Wang, Yongli Song, Jing Tang and Xinwang Yang

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identification and polymorphism discovery of the

Identification and polymorphism discovery of the

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing This is the first cathelicidin antioxidant peptide identified from the lung which

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characterization and functional analysis of cathelicidin-mh

Characterization and functional analysis of cathelicidin-MH

The novel cathelicidin cathelicidin-MH was identified from the skin of M. heymonsivogt frog, which protects against lipopolysaccharide- and cecal ligation and puncture-induced sepsis, effectively ameliorates multi-organ pathology, especially in lung.

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egg white peptide kphaevvlr promotes skin fibroblasts

Egg White peptide KPHAEVVLR promotes skin fibroblasts

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing Xiaoqing Cao , Ying Wang , +8 authors Xinwang Yang Biology, Medicine

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anti-f4/80 antibody [sp115] ab111101 from abcam | biocompare.com

Anti-F4/80 antibody [SP115] ab111101 from Abcam | Biocompare.com

Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing. Sci Rep. 2018 Jan 17;8(1):943. Ghanem LY, Mansour IM, Abulata N, Akl MM, Demerdash ZA, El Baz HG, Mahmoud SS, Mohamed SH, Mahmoud FS, Hassan ASM.

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the first identified cathelicidin from tree frogs possesses

The first identified cathelicidin from tree frogs possesses

As of February 2017, approximately 7639 amphibian species have been described in the AmphibiaWeb database. However, only 20 cathelicidin-like antimicrobial peptides have been identified to date from 10 amphibian species. Half of these peptides were identified from genome sequences and have not yet been functionally characterized. In this study, a novel cathelicidin-like peptide designated

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the first identified cathelicidin from tree frogs possesses

The first identified cathelicidin from tree frogs possesses

The current work identified a novel defensive peptide (cathelicidin-PP) from the skin of the tree frog P. puerensis. The structural organization of cathelicidin-PP precursor (Fig. 2) is similar to other vertebrate cathelicidin Fig. 9 Effects of cathelicidinPP on LPS-induced inflammatory response pathways. a Western blot of phosphorylation of

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