Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Michael P. Ready"'
Publikováno v:
EURASIP Journal on Advances in Signal Processing, Vol 2011 (2011)
Externí odkaz:
https://doaj.org/article/2ac10f420764464ba54260183cf059b2
Publikováno v:
The Plant Journal. 5:173-183
Pokeweed antiviral protein (PAP) and other ribosome-inactivating proteins (RIPs) had previously been thought to be incapable of attacking conspecific ribosomes, thus having no effect on endogenous processes. This assertion conflicts with a model for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d92d051df786e9703a44894b628a20e
https://doi.org/10.1046/j.1365-313x.1994.05020173.x
https://doi.org/10.1046/j.1365-313x.1994.05020173.x
Publikováno v:
Proteins: Structure, Function, and Genetics. 10:270-278
Ricin A-chain is an N-glycosidase that attacks ribosomal RNA at a highly conserved adenine residue. The enzyme is representative of a large family of medically significant proteins used in the design of anticancer agents and in the treatment of HIV i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25e2886cd62309e2408c33d32d780b26
https://doi.org/10.1002/prot.340100311
https://doi.org/10.1002/prot.340100311
Autor:
Jon D. Robertus, Youngsoo Kim, Art Frankel, Debra Mlsna, Arthur F. Monzingo, Michael P. Ready
Publikováno v:
Biochemistry. 31:3294-3296
Ricin A chain is an N-glycosidase which removes a single adenine base from a conservative loop of 28S rRNA, thereby inactivating eukaryotic ribosomes. The mechanism of action has been proposed to include transition-state stabilization of an oxycarbon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aed49fc739b09a5aa469fa4ade446eb
https://doi.org/10.1021/bi00127a035
https://doi.org/10.1021/bi00127a035
Publikováno v:
Journal of molecular biology. 229(1)
Higher plants contain multiple constitutively expressed proteins for defense against infection by viruses, bacteria, and fungi. One such class of proteins, the chitinases, are effective antifungal agents because they hydrolyze the insoluble β?1,4-li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42ec5487684df4b7e6be16d34ae6dad8
https://pubmed.ncbi.nlm.nih.gov/8421299
https://pubmed.ncbi.nlm.nih.gov/8421299
Publikováno v:
Journal of molecular biology. 225(2)
Higher plants contain several constitutively expressed proteins for protection against infections by viruses, bacteria and fungi. Here we report the crystallization of a polypeptide with antifungal activity, a 26,000 dalton endochitinase from barley
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bfaf0ad75b42e204818d4d36f5f53e6
https://pubmed.ncbi.nlm.nih.gov/1593638
https://pubmed.ncbi.nlm.nih.gov/1593638
Publikováno v:
Journal of Biological Chemistry. 259:15252-15256
A comparison has been made of the amino-terminal sequences of a number of ribosome-inhibiting proteins (RIPs) and cytotoxins. These include the monomeric enzymes PAP, PAP-S, PAP-II, and dodecandrin and the enzymatic A chains from the heterodimeric to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27c737ad6f6470441e015ec75d9fbd91
https://doi.org/10.1016/s0021-9258(17)42542-7
https://doi.org/10.1016/s0021-9258(17)42542-7
Publikováno v:
Proceedings of the National Academy of Sciences. 83:5053-5056
Pokeweed antiviral protein is an enzyme of Mr 29,000 known to inactivate a wide variety of eukaryotic ribosomes. We have used electron microscopy to show that the antibody specific for the protein is bound within the cell wall matrix of leaf mesophyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19d6bb05aad0c1e80b8b5d098496aae3
https://doi.org/10.1073/pnas.83.14.5053
https://doi.org/10.1073/pnas.83.14.5053
Autor:
Jon D. Robertus, Michael P. Ready
Publikováno v:
Journal of Biological Chemistry. 259:13953-13956
The galactoside-binding B chain of the cytotoxic protein ricin is apparently derived from a conservative exon-sized 40-residue peptide which is repeated four times in the molecule. A very similar peptide can also be seen in the amino acid sequence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cac30b68885a0094142a05917eb06ad
https://doi.org/10.1016/s0021-9258(18)89837-4
https://doi.org/10.1016/s0021-9258(18)89837-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 740:19-28
It has been known for some time that pokeweed antiviral protein acts by enzymatically inhibiting protein synthesis on eucaryotic ribosome systems. The site of this action is known to be the ribosome itself. In this paper we show that the pokeweed ant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fce1c3a206da6a93e0d3408d1bcd136
https://doi.org/10.1016/0167-4781(83)90116-1
https://doi.org/10.1016/0167-4781(83)90116-1