Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Song-Ping Liang"'
Publikováno v:
Protein & Cell, Vol 8, Iss 2, Pp 140-143 (2016)
Externí odkaz:
https://doaj.org/article/5c58f7276b824480954ab6de7a51f803
An efficient strategy for heterologous expression and purification of active peptide hainantoxin-IV.
Autor:
Hui Zhang, Peng-Fei Huang, Er Meng, Wen-Ying Li, Lu Zhou, Ling-Yun Zhu, Lei Wu, Meng-Jie Li, Song-Ping Liang, Dong-Yi Zhang
Publikováno v:
PLoS ONE, Vol 10, Iss 2, p e0117099 (2015)
Hainantoxin-IV (HNTX-IV) from the venom of the spider Selenocosmia hainana is a potent antagonist that specifically inhibits the tetrodotoxin-sensitive (TTX-S) sodium channels. The toxin peptide consists of 35 amino acids and adopts a typical inhibit
Externí odkaz:
https://doaj.org/article/8cb461d659cc4d4590c9d968b12162e5
Autor:
Chun-Hua Yuan, Quan-Yuan He, Kuan Peng, Jian-Bo Diao, Li-Ping Jiang, Xing Tang, Song-Ping Liang
Publikováno v:
PLoS ONE, Vol 3, Iss 11 (2008)
Externí odkaz:
https://doaj.org/article/e276f8b1399f4b1c82e441424802dd7a
Autor:
Chun-Hua Yuan, Quan-Yuan He, Kuan Peng, Jian-Bo Diao, Li-Ping Jiang, Xing Tang, Song-Ping Liang
Publikováno v:
PLoS ONE, Vol 3, Iss 10, p e3414 (2008)
BACKGROUND: Kuntiz-type toxins (KTTs) have been found in the venom of animals such as snake, cone snail and sea anemone. The main ancestral function of Kunitz-type proteins was the inhibition of a diverse array of serine proteases, while toxic activi
Externí odkaz:
https://doaj.org/article/264c5e2be7cb445a81a281ae050a1626
Publikováno v:
Protein & Cell
Protein & Cell, Vol 8, Iss 2, Pp 140-143 (2016)
Protein & Cell, Vol 8, Iss 2, Pp 140-143 (2016)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e9a2b49917befad9e5757db9dea2c79
https://pubmed.ncbi.nlm.nih.gov/28032250
https://pubmed.ncbi.nlm.nih.gov/28032250
Publikováno v:
PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS. 36:1458-1468
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1bdac26bdeead2675e61e7850f1ddc58
https://doi.org/10.3724/sp.j.1206.2009.00276
https://doi.org/10.3724/sp.j.1206.2009.00276
Publikováno v:
Zoological Research. 30:381-388
The bioactivities and proteinous compositions of venoms collected by two different methods from Latrodectus tredecimguttatus were analyzed and compared. Most of proteinous venom components were high-molecular-mass acidic proteins (>104). Compared wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d2a932965fd42b9d771267645c9e5f2
https://doi.org/10.3724/sp.j.1141.2009.04381
https://doi.org/10.3724/sp.j.1141.2009.04381
Autor:
Li-Jun, Cai, De-Hong, Xu, Ji, Luo, Ren-Zhong, Chen, Yu-Peng, Chi, Xiong-Zhi, Zeng, Xian-Chun, Wang, Song-Ping, Liang
Publikováno v:
Sheng li xue bao : [Acta physiologica Sinica]. 62(3)
Kv4.3 channel is present in many mammalian tissues, predominantly in the heart and central nervous system. Its currents are transient, characterized by rapid activation and inactivation. In the hearts of most mammals, it is responsible for repolariza
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d07282d83b6b4a1d7e33eccfa4a7d176
https://pubmed.ncbi.nlm.nih.gov/20571743
https://pubmed.ncbi.nlm.nih.gov/20571743
Selenocosmia huwena and Selenocosmia hainana are two tarantula species found in southern China. Their venoms contain abundant peptide toxins. Two new neurotoxic peptides, huwentoxin-III (HWTX-III) and hainantoxin-VI (HNTX-VI), were obtained from the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9aafe9d214145dfb24e5eea686a29f75
https://europepmc.org/articles/PMC2880359/
https://europepmc.org/articles/PMC2880359/
Publikováno v:
Analytical Biochemistry. 197:163-167
A new method for immobilization of proteins purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) prior to sequencing is described. It utilizes a simple apparatus that permits the simultaneous electroelution of proteins fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d73d2bc89e3d392f1299f7e26999610
https://doi.org/10.1016/0003-2697(91)90373-2
https://doi.org/10.1016/0003-2697(91)90373-2