Zobrazeno 1 - 6
of 6
pro vyhledávání: '"M A Lindorfer"'
Publikováno v:
Scopus-Elsevier
Protein splicing is the protein analogue of RNA splicing in which the central portion (spacer) of a protein precursor is excised and the amino- and carboxy-terminal portions of the precursor reconnected. The yeast Tfp1 protein undergoes a rapid prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e92d8df7aca6f033f78570f58c4cd391
https://doi.org/10.1002/j.1460-2075.1993.tb05913.x
https://doi.org/10.1002/j.1460-2075.1993.tb05913.x
Publikováno v:
Biochemistry. 30:4687-4696
Solid-state {sup 2}H NMR spectroscopy has been employed to study the channel conformation of gramicidin A (GA) in unoriented 1,2-dimyristoyl-sn-glycerol-3-phosphocholine (DMPC) multilayers. Quadrupolar echo spectra were obtained at 44{degree}C and 53
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59752e6f0e2d0e9e45e24931687b18d8
https://doi.org/10.1021/bi00233a008
https://doi.org/10.1021/bi00233a008
Publikováno v:
Immunological reviews. 183
Opsonization of particulate pathogens by antibodies and complement can lead to their binding to the complement receptor (CR1), specific for C3b, on primate erythrocytes (E). This process of immune adherence may play a role in immunologic defense by i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::20a32b43f1008db81c0acc4dd0b1b7c9
https://pubmed.ncbi.nlm.nih.gov/11782244
https://pubmed.ncbi.nlm.nih.gov/11782244
Publikováno v:
Molecular pharmacology. 50(6)
We investigated the coupling of A1 adenosine receptors to recombinant G proteins. Recombinant baculoviruses were used to express bovine A1 adenosine receptors in Sf9 insect cells that lack endogenous adenosine receptors. Binding parameters for recomb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eac7202720db7339bb603992544840cd
https://pubmed.ncbi.nlm.nih.gov/8967981
https://pubmed.ncbi.nlm.nih.gov/8967981
Publikováno v:
The Journal of biological chemistry. 268(17)
The yeast vacuolar membrane proton-translocating ATPase (V-ATPase) is a multisubunit complex comprised of peripheral catalytic, and integral membrane domains. At least eight proteins cofractionate with purified preparations of the enzyme including 10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2903cc43374b14a1bf24799a5554aea7
https://pubmed.ncbi.nlm.nih.gov/8509410
https://pubmed.ncbi.nlm.nih.gov/8509410
Publikováno v:
The Journal of biological chemistry. 268(1)
The vacuolar membrane H(+)-ATPase of the yeast Saccharomyces cerevisiae is a multisubunit enzyme complex composed of an integral membrane V0 sector, and a peripherally associated V1 sector. Deletion of one of several structural genes for vacuolar H(+
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::707d636c9096bf22eb57da457deb82c2
https://pubmed.ncbi.nlm.nih.gov/8416931
https://pubmed.ncbi.nlm.nih.gov/8416931