Zobrazeno 1 - 10
of 11
pro vyhledávání: '"J D, Schrag"'
Autor:
M, Cygler, J D, Schrag
Publikováno v:
Biochimica et biophysica acta. 1441(2-3)
Three-dimensional structures of a number of lipases determined in the past decade have provided a solid structural foundation for our understanding of lipase function. The structural studies of Candida rugosa lipase summarized here have addressed man
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::df103d7d34fb4a697aa450ec49eb8eb7
https://pubmed.ncbi.nlm.nih.gov/10570248
https://pubmed.ncbi.nlm.nih.gov/10570248
Autor:
J D, Schrag, M, Cygler
Publikováno v:
Methods in enzymology. 284
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a6afc45752bbede97a41875271d5b094
https://pubmed.ncbi.nlm.nih.gov/9379946
https://pubmed.ncbi.nlm.nih.gov/9379946
Autor:
M, Cygler, J D, Schrag
Publikováno v:
Methods in enzymology. 284
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c7c6935a2c77769ddc068d8546f61dbb
https://pubmed.ncbi.nlm.nih.gov/9379943
https://pubmed.ncbi.nlm.nih.gov/9379943
Publikováno v:
European journal of biochemistry. 228(3)
Despite tremendous progress in the elucidation of three-dimensional structures of lipases, the molecular basis for their observed substrate preference is not well understood. In an effort to correlate the lipase structure with its substrate preferenc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8e173f01f05d90aaa5cb7b2ab0c49279
https://pubmed.ncbi.nlm.nih.gov/7737187
https://pubmed.ncbi.nlm.nih.gov/7737187
Autor:
T, Vernet, E, Ziomek, A, Recktenwald, J D, Schrag, C, de Montigny, D C, Tessier, D Y, Thomas, M, Cygler
Publikováno v:
The Journal of biological chemistry. 268(35)
The three-dimensional structure of lipase II of Geotrichum candidum strain ATCC34614 (GCL II) has provided insights with respect to the nature of the catalytic machinery of lipases. To support these structural observations, we have carried out an ana
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dfb7ea0499decde7f490ec4018b0a872
https://pubmed.ncbi.nlm.nih.gov/7902836
https://pubmed.ncbi.nlm.nih.gov/7902836
Autor:
P, Grochulski, Y, Li, J D, Schrag, F, Bouthillier, P, Smith, D, Harrison, B, Rubin, M, Cygler
Publikováno v:
The Journal of biological chemistry. 268(17)
The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site. Comparison with the crystal structure of the homologous lipase from Geotrichum candidum, in which the active site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9f177c34d7ad013efb45047717c0aaf7
https://pubmed.ncbi.nlm.nih.gov/8509417
https://pubmed.ncbi.nlm.nih.gov/8509417
Publikováno v:
Protein science : a publication of the Protein Society. 2(3)
Based on the recently determined X-ray structures of Torpedo californica acetylcholinesterase and Geotrichum candidum lipase and on their three-dimensional superposition, an improved alignment of a collection of 32 related amino acid sequences of oth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a0f3937ca813d20e215a1c160c99460a
https://pubmed.ncbi.nlm.nih.gov/8453375
https://pubmed.ncbi.nlm.nih.gov/8453375
Publikováno v:
The Journal of biological chemistry. 267(7)
Comparison of the fold of lipases from Geotrichum candidum and from human pancreas identified a high degree of similarity which was not expected on the basis of their amino acid sequences. Although both enzymes utilize a serine protease-like catalyti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0482d655cab85cfd31eb5db3c8d5469a
https://pubmed.ncbi.nlm.nih.gov/1537823
https://pubmed.ncbi.nlm.nih.gov/1537823
Publikováno v:
Journal of Biological Chemistry. 263:9795-9800
The 11 S form of acetylcholinesterase from Electrophorus electricus was purified by affinity chromatography. The protein was crystallized from polyethylene glycol solutions. One crystal form proved suitable for x-ray diffraction studies. Preliminary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e56f9fa9ef5433476fba2c2cb146405
https://doi.org/10.1016/s0021-9258(19)81588-0
https://doi.org/10.1016/s0021-9258(19)81588-0
Publikováno v:
The Journal of biological chemistry. 263(20)
The 11 S form of acetylcholinesterase from Electrophorus electricus was purified by affinity chromatography. The protein was crystallized from polyethylene glycol solutions. One crystal form proved suitable for x-ray diffraction studies. Preliminary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::75b054fdf4330eaf2f18996f20f0b6fa
https://pubmed.ncbi.nlm.nih.gov/3384821
https://pubmed.ncbi.nlm.nih.gov/3384821