Zobrazeno 1 - 7
of 7
pro vyhledávání: '"G A Barkocy-Gallagher"'
Publikováno v:
Journal of Biological Chemistry. 269:13609-13613
Signal peptidase I (also called leader peptidase) is the endopeptidase that removes the signal peptides of most secreted proteins during or after translocation in Escherichia coli. Precursor recognition is contingent in part on the presence of small,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e987e1872ae7d50cd62d2362287e050
https://doi.org/10.1016/s0021-9258(17)36873-4
https://doi.org/10.1016/s0021-9258(17)36873-4
Publikováno v:
Journal of Biological Chemistry. 267:1231-1238
The residues occupying the -3 and -1 positions relative to the cleavage site of secretory precursor proteins are usually amino acids with small, neutral side chains that are thought to constitute the recognition site for the processing enzyme, signal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3fc627aa5a83ea814df3ba8c3a8bcd40
https://doi.org/10.1016/s0021-9258(18)48419-0
https://doi.org/10.1016/s0021-9258(18)48419-0
Publikováno v:
Journal of Bacteriology. 176:3397-3399
Maltose-binding protein (MBP) is translocated across the cytoplasmic membrane of Escherichia coli; successful export depends on information in both the signal peptide and the mature moiety of the protein. To determine the shortest portion of the matu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f10225dea003eeab2e2e4fa440bcf5c
https://doi.org/10.1128/jb.176.11.3397-3399.1994
https://doi.org/10.1128/jb.176.11.3397-3399.1994
Publikováno v:
The Journal of biological chemistry. 269(18)
Signal peptidase I (also called leader peptidase) is the endopeptidase that removes the signal peptides of most secreted proteins during or after translocation in Escherichia coli. Precursor recognition is contingent in part on the presence of small,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7fad67fc79a5980cd0c879899728d8e1
https://pubmed.ncbi.nlm.nih.gov/8175796
https://pubmed.ncbi.nlm.nih.gov/8175796
DNA processing occurs in ciliates at autogamy and conjugation when new macronuclei are formed from micronuclei and old macronuclei degrade. Processing of micronuclear DNA consists of removal of certain internal sequences, chromosomal fragmentation, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02ac0c782fbad86fff04c9bda407043c
https://europepmc.org/articles/PMC43349/
https://europepmc.org/articles/PMC43349/
Autor:
G A, Barkocy-Gallagher, P J, Bassford
Publikováno v:
The Journal of biological chemistry. 267(2)
The residues occupying the -3 and -1 positions relative to the cleavage site of secretory precursor proteins are usually amino acids with small, neutral side chains that are thought to constitute the recognition site for the processing enzyme, signal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9f2cfd39db3f9bf68e7b41acd6a9d1ea
https://pubmed.ncbi.nlm.nih.gov/1730647
https://pubmed.ncbi.nlm.nih.gov/1730647
Publikováno v:
The Journal of biological chemistry. 265(6)
Comparative analyses of a number of secretory proteins processed by eukaryotic and prokaryotic signal peptidases have identified a strongly conserved feature regarding the residues positioned -3 and -1 relative to the cleavage site. These 2 residues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b5e04868dfe7c207264a37d033cbc95a
https://pubmed.ncbi.nlm.nih.gov/2406254
https://pubmed.ncbi.nlm.nih.gov/2406254