Zobrazeno 1 - 10
of 10
pro vyhledávání: '"C A, Kumamoto"'
Publikováno v:
The Journal of biological chemistry. 275(31)
During localization to the periplasmic space or to the outer membrane of Escherichia coli some proteins are dependent on binding to the cytosolic chaperone SecB, which in turn is targeted to the membrane by specific interaction with SecA, a periphera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9621df498ef90d7a8414df92a4ca39bc
https://pubmed.ncbi.nlm.nih.gov/10807917
https://pubmed.ncbi.nlm.nih.gov/10807917
Autor:
P M, Gannon, C A, Kumamoto
Publikováno v:
The Journal of biological chemistry. 268(3)
SecB is a 16-kDa cytosolic chaperone protein that is required for efficient export of particular proteins in Escherichia coli. To identify regions of SecB that contribute to efficient protein export, we isolated secB point mutants that are defective
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::177ef30c1d52b05a2672c53558ad0ecc
https://pubmed.ncbi.nlm.nih.gov/8420934
https://pubmed.ncbi.nlm.nih.gov/8420934
Publikováno v:
Molecular microbiology. 5(1)
The rate of folding of the precursor of beta-lactamase is not influenced by the presence of SecB under conditions in which GroEL/ES retards the folding. Wild-type beta-lactamase and several mutants in the signal or the mature protein, affecting eithe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::064ac415e26a3b074d1ece0669606d08
https://pubmed.ncbi.nlm.nih.gov/2013998
https://pubmed.ncbi.nlm.nih.gov/2013998
Publikováno v:
The Journal of biological chemistry. 265(30)
In the accompanying paper (Altman, E., Bankaitis, V.A., and Emr, S.D. (1990) J. Biol. Chem. 265, 18148-18153) a putative SecB binding site was identified in the mature LamB protein. The export of wild-type LamB was unperturbed when this region was re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::31dd4ce93b89d03889c8e4cde78fbb5c
https://pubmed.ncbi.nlm.nih.gov/2211691
https://pubmed.ncbi.nlm.nih.gov/2211691
Publikováno v:
The Journal of biological chemistry. 256(18)
The biosynthesis and processing of type V procollagens was investigated in chick embryo blood vessels labeled with radioactive amino acids. Monomeric, pepsin-sensitive pro alpha 1 V and pro alpha 2 V chains are slowly assembled into triple helically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6a9c8cc286f388ce1cd11fb1178a5a69
https://pubmed.ncbi.nlm.nih.gov/7287701
https://pubmed.ncbi.nlm.nih.gov/7287701
Autor:
C A, Kumamoto, J H, Fessler
Publikováno v:
The Journal of biological chemistry. 256(13)
The biosynthesis of type V (A,B) collagens was recently found to proceed through the sequential forms pro alpha (A,B), p alpha (A,B), and f alpha (A,B). All these chains are larger than the A,B chains extracted from tissues after pepsin digestion. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bfb1db3818e9eec033c0bdbb9aa98ec9
https://pubmed.ncbi.nlm.nih.gov/6263929
https://pubmed.ncbi.nlm.nih.gov/6263929
Autor:
C A, Kumamoto, R D, Simoni
Publikováno v:
The Journal of biological chemistry. 262(7)
A mutation of the b subunit of the Escherichia coli proton-translocating ATPase and mutations in the gene for the a subunit that suppress its effects have been previously described (Kumamoto, C., and Simoni, R. D. (1986) J. Biol. Chem. 261, 10037-100
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::087219a4c9b8d587074c06460677fafc
https://pubmed.ncbi.nlm.nih.gov/2880846
https://pubmed.ncbi.nlm.nih.gov/2880846
Autor:
C A, Kumamoto, R D, Simoni
Publikováno v:
The Journal of biological chemistry. 261(22)
A mutation of the b subunit of the Escherichia coli proton translocating ATPase was previously described (Porter, A. C. G., Kumamoto, C., Aldape, K., and Simoni, R. D. (1985) J. Biol. Chem. 260, 8182-8187). This mutation, which causes substitution of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0753de1b29e5c2450c536457676a71a4
https://pubmed.ncbi.nlm.nih.gov/2874136
https://pubmed.ncbi.nlm.nih.gov/2874136
Autor:
C A, Kumamoto, P M, Gannon
Publikováno v:
The Journal of biological chemistry. 263(23)
Mutations affecting the secB gene of Escherichia coli cause a defect in protein export. This report presents the demonstration that the secB mutations caused a defect in co-translational processing of maltose binding protein (MBP). A significant amou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4a2722ac8aa846514ff4b99a0251306b
https://pubmed.ncbi.nlm.nih.gov/3042772
https://pubmed.ncbi.nlm.nih.gov/3042772
Publikováno v:
The Journal of biological chemistry. 264(4)
Mutations in the Escherichia coli secB gene lead to protein export defects in vivo (Kumamoto, C.A., and Beckwith, J. (1985) J. Bacteriol. 163, 267-274). To demonstrate directly the participation of the secB gene product (SecB) in protein export, SecB
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::03730964387930d106c6cdda53f32f9c
https://pubmed.ncbi.nlm.nih.gov/2644258
https://pubmed.ncbi.nlm.nih.gov/2644258