Zobrazeno 1 - 10
of 101
pro vyhledávání: '"Chanan, Angsuthanasombat"'
Autor:
Sathapat Charoenjotivadhanakul, Somsri Sakdee, Chompounoot Imtong, Hui-Chun Li, Chanan Angsuthanasombat
Publikováno v:
Biochemical and Biophysical Research Communications. 668:111-117
Autor:
Manussawee Dechkla, Sathapat Charoenjotivadhanakul, Chompounoot Imtong, Sarinporn Visitsattapongse, Hui-Chun Li, Chanan Angsuthanasombat
Publikováno v:
Toxins, Vol 14, Iss 10, p 652 (2022)
The three-domain Cry4Aa toxin produced from Bacillus thuringiensis subsp. israelensis was previously shown to be much more toxic to Culex mosquito larvae than its closely related toxin—Cry4Ba. The interaction of these two individual toxins with tar
Externí odkaz:
https://doaj.org/article/8262b46e40de49c285072c89899aea0b
Autor:
Anon Thammasittirong, Sutticha Na-Ranong Thammasittirong, Chompounoot Imtong, Sathapat Charoenjotivadhanakul, Somsri Sakdee, Hui-Chun Li, Siriporn Okonogi, Chanan Angsuthanasombat
Publikováno v:
Toxins, Vol 13, Iss 8, p 553 (2021)
In addition to the receptor-binding domain (DII), the C-terminal domain (DIII) of three-domain Cry insecticidal δ-endotoxins from Bacillus thuringiensis has been implicated in target insect specificity, yet its precise mechanistic role remains uncle
Externí odkaz:
https://doaj.org/article/78a3865ced004eafa98de3fad89a33bb
Autor:
Neeranuch Rukying, Ya’u Sabo Ajingi, Jiddah Nafiu Usman, Songsirin Ruengvisesh, Triwit Rattanarojpong, Patthra Pason, Chanan Angsuthanasombat, Nujarin Jongruja, Santi nokyod
Bacteria-derived antimicrobial peptides known as peptidic bacteriocins offer a promising alternative to traditional antibiotics in the face of the emergence of multidrug-resistant bacteria. Here, a nucleotide sequence of the gene encoding Lactococcus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::47146ed6a7fae2f66cdc395c73e608d8
https://doi.org/10.21203/rs.3.rs-2626969/v1
https://doi.org/10.21203/rs.3.rs-2626969/v1
Autor:
Chattip Kurehong, Chalermpol Kanchanawarin, Busaba Powthongchin, Gerd Katzenmeier, Chanan Angsuthanasombat
Publikováno v:
Toxins, Vol 7, Iss 5, Pp 1486-1496 (2015)
Previously, the 126-kDa Bordetella pertussis CyaA pore-forming/hemolysin (CyaA-Hly) domain was shown to retain its hemolytic activity causing lysis of susceptible erythrocytes. Here, we have succeeded in producing, at large quantity and high purity,
Externí odkaz:
https://doaj.org/article/d4150091bedc4a4bb805349f05dbf4a1
Autor:
Nitchakan Samainukul, Gerd Katzenmeier, Chonthicha Butnampetch, Aung Khine Linn, Somsri Sakdee, Hui-Chun Li, Chanan Angsuthanasombat
Publikováno v:
Protein & Peptide Letters. 28:643-650
Background: Gastric pathogen Helicobacter pylori secretes VacA cytotoxin displaying a high degree of polymorphic variations of which the highest VacA pathogenicity correlates with m1-type variant followed by VacA-m2. Objective: To comparatively evalu
Autor:
Ke Chen, Chompounoot Imtong, Aung Khine Linn, Charoensri Thonabulsombat, Hui-Chun Li, Chanan Angsuthanasombat, Suvash Chandra Ojha
Publikováno v:
Protein & Peptide Letters. 28:140-148
Background: Mature lysostaphin (~28-kDa Lss) from Staphylococcus simulans proves effective in killing methicillin-resistant Staphylococcus aureus (MRSA) which is endemic in hospitals worldwide. Lss is Zn2+-dependent endopeptidase, but its bacteriolyt
Autor:
Anon Thammasittirong, Chompounoot Imtong, Wilaiwan Sriwimol, Somsri Sakdee, Chanan Angsuthanasombat
Publikováno v:
Toxins, Vol 11, Iss 2, p 62 (2019)
Although the C-terminal domain (DIII) of three-domain Cry insecticidal toxins from Bacillus thuringiensis has been implicated in various biological functions, its exact role still remains to be elucidated. Here, the 21-kDa isolated DIII fragment of t
Externí odkaz:
https://doaj.org/article/3594cdb5e22f417d99119eaf7948f968
Autor:
Niramon Thamwiriyasati, Chalermpol Kanchanawarin, Chompounoot Imtong, Chun-Jung Chen, Hui-Chun Li, Chanan Angsuthanasombat
Publikováno v:
Biochemical and biophysical research communications. 620
The insecticidal nature of Cry δ-endotoxins produced by Bacillus thuringiensis is generally attributed to their ability to form transmembrane pores, causing lysis of target insect cells. Previously, the truncated tertiary structure of the chymotryps
Autor:
Somsri Sakdee, Siriporn Okonogi, Chompounoot Imtong, Sathapat Charoenjotivadhanakul, Anon Thammasittirong, Hui-Chun Li, Sutticha Na-Ranong Thammasittirong, Chanan Angsuthanasombat
Publikováno v:
Toxins
Toxins, Vol 13, Iss 553, p 553 (2021)
Volume 13
Issue 8
Toxins, Vol 13, Iss 553, p 553 (2021)
Volume 13
Issue 8
In addition to the receptor-binding domain (DII), the C-terminal domain (DIII) of three-domain Cry insecticidal δ-endotoxins from Bacillus thuringiensis has been implicated in target insect specificity, yet its precise mechanistic role remains uncle