Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Eva-Maria Mayr"'
Publikováno v:
mSphere, Vol 5, Iss 2 (2020)
ABSTRACT The recently emerged pathogenic yeast Candida auris is a major concern for human health, because it is easily transmissible, difficult to eradicate from hospitals, and highly drug resistant. Most C. auris isolates are resistant to the widely
Externí odkaz:
https://doaj.org/article/52fa267fa7b3472580f15eb19d6f5c1d
Publikováno v:
Journal of Molecular Biology. 289:701-705
Globular proteins may be stabilized, either intrinsically, at the various levels of the structural hierarchy, or extrinsically, by ligand binding. In the case of the dormant all-β protein spherulin 3a (S3a) from the slime mold Physarum polycephalum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b7588ec4e486a3bbaddbdada24220bf
https://doi.org/10.1006/jmbi.1999.2833
https://doi.org/10.1006/jmbi.1999.2833
Publikováno v:
Journal of Molecular Biology. 286:989-994
βB2-Crystallin from vertebrate eye lens forms domain-swapped dimers, with subunits consisting of two all-β domains connected by an eight-residue extended linker peptide. Topologically, the two domains show great similarity; however, they differ wid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f79bca7989c55fc290454004bd5798e
https://doi.org/10.1006/jmbi.1999.2554
https://doi.org/10.1006/jmbi.1999.2554
Autor:
Tad A. Holak, Robert Huber, Martina Wenk, Eva-Maria Mayr, Rainer Jaenicke, Roland Baumgartner
Publikováno v:
Journal of Molecular Biology. 286:1533-1545
Protein S from Myxococcus xanthus is a member of the βγ-crystallin superfamily. Its N and C-terminal domains (NPS and CPS, respectively) show a high degree of structural similarity and possess the capacity to bind two calcium ions per domain. For N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e4cf975a2b483829910d37714ff3148
https://doi.org/10.1006/jmbi.1999.2582
https://doi.org/10.1006/jmbi.1999.2582
Autor:
Eva-Maria Mayr, Martina Wenk
Publikováno v:
European Journal of Biochemistry. 255:604-610
Protein S, a calcium-binding spore coat protein from the soil bacterium Myxococcus xanthus, belongs to a group of structurally related proteins, the betagamma-crystallin superfamily. Common features of this protein family are the Greek-key structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dbff4b05df290076f858dd81599090f
https://doi.org/10.1046/j.1432-1327.1998.2550604.x
https://doi.org/10.1046/j.1432-1327.1998.2550604.x
Publikováno v:
Journal of Molecular Biology. 271:645-655
Spherulin 3a is the most abundantly expressed cytosolic protein in spherulating plasmodia of the slime mold Physarum polycephalum. High yields of unlabeled, uniformly 15N and uniformly 13C/15N-labeled recombinant spherulin 3a from Escherichia coli co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6676d194470dccfcea38438254a30599
https://doi.org/10.1006/jmbi.1997.1184
https://doi.org/10.1006/jmbi.1997.1184
Publikováno v:
Journal of Molecular Biology. 269:260-269
gammaB-crystallin from vertebrate eye lens is an all beta-sheet two-domain protein with a high degree of intrachain symmetry. Its N and C-terminal domains show high levels of sequence similarity and structural identity. In natural gammaB-crystallin,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a745df5091cf592c327143c630cd48f
https://doi.org/10.1006/jmbi.1997.1033
https://doi.org/10.1006/jmbi.1997.1033
Autor:
Eva-Maria Mayr, Rudi Glockshuber, O. A. Bateman, Christine Slingsby, H.P.C. Driessen, B.V. Norledge, Rainer Jaenicke
Publikováno v:
Nature Structural Biology. 3:267-274
We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad5019d6cbec08e962b5bd9a0b2e1770
https://doi.org/10.1038/nsb0396-267
https://doi.org/10.1038/nsb0396-267
Publikováno v:
Journal of Molecular Biology. 235:84-88
beta B2- and gamma B-crystallin from bovine eye-lens are closely related proteins, topologically distinct mainly by virtue of the linker peptide connecting the two domains in each polypeptide chain. In homodimeric beta B2-crystallin, the extended con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76ec32d47c0ee94ad7d68de5a1142f10
https://doi.org/10.1016/s0022-2836(05)80017-8
https://doi.org/10.1016/s0022-2836(05)80017-8
Publikováno v:
Journal of molecular biology. 280(4)
The related vertebrate eye lens polypeptides, betaB2- and gammaB-crystallin, each fold into two similar beta-sheet domains. The main difference is the state of oligomerization resulting from intermolecular domain interactions in the oligomeric beta-c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db194bb37a5cecd54afb8e38e6bc2025
https://pubmed.ncbi.nlm.nih.gov/9677299
https://pubmed.ncbi.nlm.nih.gov/9677299