Zobrazeno 1 - 8
of 8
pro vyhledávání: '"James G. McAfee"'
Autor:
Kalee Woody, Jessica Jewell, Vida Karimnia, Blaze Heckert, Tyler Shelby, Shoukath Sulthana, Santimukul Santra, James G. McAfee, Tuhina Banerjee
Publikováno v:
ACS Infectious Diseases. 2:667-673
Enterohemorrhagic Escherichia coli O157:H7 presents a serious threat to human health and sanitation and is a leading cause in many food- and waterborne ailments. While conventional bacterial detection methods such as PCR, fluorescent immunoassays and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ffb4cb2def2bac218b4a03921d4a1e0
https://doi.org/10.1021/acsinfecdis.6b00108
https://doi.org/10.1021/acsinfecdis.6b00108
Publikováno v:
Journal of Visualized Experiments.
Enterohemorrhagic Escherichia coli O157:H7 has been linked to both waterborne and foodborne illnesses, and remains a threat despite the food- and water-screening methods used currently. While conventional bacterial detection methods, such as polymera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6744840d02c2cb1d4a2c9b245c9af4ea
https://doi.org/10.3791/55821-v
https://doi.org/10.3791/55821-v
Publikováno v:
Biochemistry. 35:1212-1222
Proteins C1 and C2 together comprise about one-third the protein mass of mammalian core 40S heterogeneous nuclear ribonucleoprotein particles (40S hnRNP) and exist as heterotetramers of (C1)3C2. On the basis of nonequilibrium binding studies, it has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0bf73b38ad7469cf85660d94f7b1c49
https://doi.org/10.1021/bi951974k
https://doi.org/10.1021/bi951974k
Autor:
Lillian Shahied, Jia-huai Tan, Jun Li, Yuji Kajiwara, Wallace M. LeStourgeon, James G. McAfee
Publikováno v:
Journal of molecular biology. 305(4)
The hnRNP C protein tetramer cooperatively binds 230 nt increments of pre-mRNA in vitro in a salt-resistant manner and is located along the length of vertebrate transcripts in vivo . Based on these and other findings it has been suggested that hnRNP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9640fc4c1e9dd2df3d3b80450f511315
https://pubmed.ncbi.nlm.nih.gov/11162095
https://pubmed.ncbi.nlm.nih.gov/11162095
Publikováno v:
Biochemistry. 36(39)
Polypyrimidine tract binding protein (PTB) is a 57 kD hnRNP protein (hnRNP I) that binds to the pyrimidine tract typically found near the 3' end of introns. Primary sequence analysis suggests that PTB contains four RNA recognition motifs (RRMs). Data
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3218cecefe5edbd34caf7a3c412f1fb
https://pubmed.ncbi.nlm.nih.gov/9305981
https://pubmed.ncbi.nlm.nih.gov/9305981
Publisher Summary This chapter deals with identification of pre- messenger ribonucleic acids (mRNAs) splicing factors and analysis of RNA-protein interaction. Pre-mRNA splicing occurs in a large particle termed the “spliceosome,” composed of mult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36407e3116dd29f97bc4a5c8a59b9e1d
https://doi.org/10.1016/b978-012587545-5/50005-7
https://doi.org/10.1016/b978-012587545-5/50005-7
Publikováno v:
Biochemistry. 35(13)
The thermodynamics of the binding of the Sac7d protein of Sulfolobus acidocaldarius to double-stranded DNA has been characterized using spectroscopic signals arising from both the protein and the DNA. Ligand binding density function analysis has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e08f39450479d967ac713b1760226eb4
https://pubmed.ncbi.nlm.nih.gov/8672437
https://pubmed.ncbi.nlm.nih.gov/8672437
Publikováno v:
Biochemistry. 34(31)
The genes for two Sac7 DNA-binding proteins, Sac7d and Sac7e, from the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned into Escherichia coli and sequenced. The sac7d and sac7e open reading frames encode 66 amino acid (7608
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::654312eb0afa74c57b5e4f495517c66c
https://pubmed.ncbi.nlm.nih.gov/7632679
https://pubmed.ncbi.nlm.nih.gov/7632679