Zobrazeno 1 - 7
of 7
pro vyhledávání: '"S M, Mandala"'
Autor:
S M, Mandala, G H, Harris
Publikováno v:
Methods in enzymology. 311
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b00bdfdf1ac70c4cae79d75f9652cbb3
https://pubmed.ncbi.nlm.nih.gov/10563338
https://pubmed.ncbi.nlm.nih.gov/10563338
Autor:
S M Mandala, Carolyn W. Slayman
Publikováno v:
Journal of Biological Chemistry. 264:16276-16281
Based on hydropathy analysis, the P-type cation translocating ATPases are believed to have similar topological arrangements in the membrane, but little independent evidence exists for their precise pattern of transmembrane folding. As a first step to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7ce1889f92b314e36010b1fb9b82ce4
https://doi.org/10.1016/s0021-9258(18)71618-9
https://doi.org/10.1016/s0021-9258(18)71618-9
Autor:
L. R. Aaronson, David W. Speicher, Karl Hager, Amy Chang, J. W. Davenport, S M Mandala, Carolyn W. Slayman
Publikováno v:
Journal of Biological Chemistry. 263:14552-14558
The plasma membrane H+-ATPase of Neurospora is a 100-kDa integral membrane protein which appears, on the basis of hydropathy analysis of its amino acid sequence, to span the lipid bilayer at least eight times. To investigate the assembly and processi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6bca4ef5a4b1ff59c2b8fb5d15888cd
https://doi.org/10.1016/s0021-9258(18)68255-9
https://doi.org/10.1016/s0021-9258(18)68255-9
Autor:
S M Mandala, Carolyn W. Slayman
Publikováno v:
Journal of Biological Chemistry. 263:15122-15128
Previous work has shown that the tryptic degradation pattern of the Neurospora plasma membrane H+-ATPase varies with the presence and absence of ligands, thus providing information about conformational states of the enzyme (Addison, R., and Scarborou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03fd9659164d104b22ffb605ad4a8d3b
https://doi.org/10.1016/s0021-9258(18)68154-2
https://doi.org/10.1016/s0021-9258(18)68154-2
Autor:
S M, Mandala, C W, Slayman
Publikováno v:
The Journal of biological chemistry. 263(29)
Previous work has shown that the tryptic degradation pattern of the Neurospora plasma membrane H+-ATPase varies with the presence and absence of ligands, thus providing information about conformational states of the enzyme (Addison, R., and Scarborou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bd1f1ede968d238c29ff97a60e855dc9
https://pubmed.ncbi.nlm.nih.gov/2902089
https://pubmed.ncbi.nlm.nih.gov/2902089
Autor:
L R, Aaronson, K M, Hager, J W, Davenport, S M, Mandala, A, Chang, D W, Speicher, C W, Slayman
Publikováno v:
The Journal of biological chemistry. 263(28)
The plasma membrane H+-ATPase of Neurospora is a 100-kDa integral membrane protein which appears, on the basis of hydropathy analysis of its amino acid sequence, to span the lipid bilayer at least eight times. To investigate the assembly and processi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::838ef1fe0ab93270dc8d7fd461777fcb
https://pubmed.ncbi.nlm.nih.gov/2902084
https://pubmed.ncbi.nlm.nih.gov/2902084
Autor:
S M, Mandala, C W, Slayman
Publikováno v:
The Journal of biological chemistry. 264(27)
Based on hydropathy analysis, the P-type cation translocating ATPases are believed to have similar topological arrangements in the membrane, but little independent evidence exists for their precise pattern of transmembrane folding. As a first step to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8f473d3898fad62f959857859e58a300
https://pubmed.ncbi.nlm.nih.gov/2528544
https://pubmed.ncbi.nlm.nih.gov/2528544