Zobrazeno 1 - 10
of 47
pro vyhledávání: '"H Cudny"'
Autor:
N. J. Tobkes, Nikos Panayotatos, Terence E Ryan, Wayne A. Hendrickson, James P. Fandl, Ann Acheson, N. Q. Mcdonald, H. Cudny, Somesh Nigam
Publikováno v:
Journal of Biological Chemistry. 269:755-759
Neurotrophin-4 (NT-4) is the most recently discovered member of the neurotrophin family. We have expressed, refolded, and purified recombinant human NT-4 from Escherichia coli and compared it with recombinant human NT-4 secreted into the culture medi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5694f5e0d338451c8e05d97de651e10a
https://doi.org/10.1016/s0021-9258(17)42414-8
https://doi.org/10.1016/s0021-9258(17)42414-8
Publikováno v:
Journal of Biological Chemistry. 256:5633-5637
The catalytic properties of purified RNase D were examined. The enzyme requires a divalent cation for activity, and this requirement can be satisfied by Mg2+, MN2+, or Co2+. RNase D is most active at pH 9.1-9.5, but this optimum may reflect an effect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fcb88dc9de894e8350d3f652b803d1b1
https://doi.org/10.1016/s0021-9258(19)69251-3
https://doi.org/10.1016/s0021-9258(19)69251-3
Autor:
H. Cudny, M P Deutscher
Publikováno v:
Journal of Biological Chemistry. 261:6450-6453
The cloned Escherichia coli cca gene, described in the accompanying paper (Cudny, H., Lupski, J. R., Godson, G. N., and Deutscher, M. P. (1986) J. Biol. Chem. 261, 6444-6449), has been used to construct strains that overproduce tRNA nucleotidyltransf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39bea7518ef3f42ec259bb60dc7b31ba
https://doi.org/10.1016/s0021-9258(19)84583-0
https://doi.org/10.1016/s0021-9258(19)84583-0
Publikováno v:
Journal of Biological Chemistry. 261:6444-6449
The Escherichia coli cca gene which encodes the enzyme tRNA nucleotidyltransferase has been cloned by taking advantage of its proximity to the previously cloned dnaG locus. A series of recombinant bacteriophages, spanning the chromosomal region betwe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91118245ce0c28ca07a2228809b60340
https://doi.org/10.1016/s0021-9258(19)84582-9
https://doi.org/10.1016/s0021-9258(19)84582-9
Publikováno v:
Journal of Biological Chemistry. 256:5627-5632
RNase D, a putative tRNa processing nuclease, has been purified about 1,000-fold from extracts of Escherichia coli to apparent homogeneity, as judged by acrylamide gel electrophoresis under nondenaturing and denaturing conditions and by gel electrofo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1a56e2f3837d7fd5d8ceacff2272601
https://doi.org/10.1016/s0021-9258(19)69250-1
https://doi.org/10.1016/s0021-9258(19)69250-1
Autor:
Murray P. Deutscher, H Cudny
Publikováno v:
Journal of Biological Chemistry. 263:1518-1523
In order to determine the mechanism and enzyme(s) responsible for 3' processing of tRNA precursors, we have developed an in vitro processing system that uses as substrates two SP6 RNA polymerase-generated transcripts of the gene for tRNA(Tyrsu3)+ tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1e57c7be2b616279a420f616217e2ed
https://doi.org/10.1016/s0021-9258(19)57334-3
https://doi.org/10.1016/s0021-9258(19)57334-3
Publikováno v:
Journal of Biological Chemistry. 261:14875-14877
Escherichia coli strain 5C15 contains a mutation in the cca gene that decreases AMP incorporation by tRNA nucleotidyltransferase while leaving CMP incorporation unaffected. Earlier studies of the purified mutant enzyme suggested that the mutation was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8fde4b78dbaedf31f21441e55c1dafa0
https://doi.org/10.1016/s0021-9258(18)66797-3
https://doi.org/10.1016/s0021-9258(18)66797-3
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 85(13)
Final trimming of the 3' terminus of tRNA precursors in Escherichia coli is thought to proceed by an exonucleolytic mechanism. However, mutant strains lacking as many as four exoribonucleases known to act on tRNA still grow normally and process tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b36275569f479df8ccf180262994efb0
https://pubmed.ncbi.nlm.nih.gov/2455297
https://pubmed.ncbi.nlm.nih.gov/2455297
Publikováno v:
The Journal of biological chemistry. 256(11)
RNase D, a putative tRNa processing nuclease, has been purified about 1,000-fold from extracts of Escherichia coli to apparent homogeneity, as judged by acrylamide gel electrophoresis under nondenaturing and denaturing conditions and by gel electrofo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ab52d2d8e3740c37a6c93e1cc3410e72
https://pubmed.ncbi.nlm.nih.gov/6263885
https://pubmed.ncbi.nlm.nih.gov/6263885
Autor:
H, Cudny, M P, Deutscher
Publikováno v:
The Journal of biological chemistry. 263(3)
In order to determine the mechanism and enzyme(s) responsible for 3' processing of tRNA precursors, we have developed an in vitro processing system that uses as substrates two SP6 RNA polymerase-generated transcripts of the gene for tRNA(Tyrsu3)+ tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::55da3b5646c38997e0d30c33ecc9e2ce
https://pubmed.ncbi.nlm.nih.gov/3275667
https://pubmed.ncbi.nlm.nih.gov/3275667