Zobrazeno 1 - 10 of 20 pro vyhledávání: '"J K Stoops"'
1
Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The 'breathing' core and its functional relationship to protein dynamics
Autor: Z H, Zhou, W, Liao, R H, Cheng, J E, Lawson, D B, McCarthy, L J, Reed, J K, Stoops
Publikováno v: The Journal of biological chemistry. 276(24)
Structural studies by three-dimensional electron microscopy of the Saccharomyces cerevisiae truncated dihydrolipoamide acetyltransferase (tE(2)) component of the pyruvate dehydrogenase complex reveal an extraordinary example of protein dynamics. The
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b508f75e521d6ced0c8f8c030bdb0764
https://pubmed.ncbi.nlm.nih.gov/11285267
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2
Three-Dimensional Structure of the Human Herpesvirus 8 Capsid
Autor: Z H Zhou, Pierrette Lo, Bagher Forghani, L Wu, Xuekui Yu, J K Stoops
Human herpesvirus 8 (HHV-8), or Kaposi's sarcoma-associated herpesvirus, is a gammaherpesvirus implicated in all forms of Kaposi's sarcoma and certain lymphomas. HHV-8 has been extensively characterized, both biochemically and immunologically, since
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::062758ad582897496dc27b93a49c9989
https://europepmc.org/articles/PMC112397/
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3
On the structural changes of native human alpha2-macroglobulin upon proteinase entrapment. Three-dimensional structure of the half-transformed molecule
Autor: U, Qazi, P G, Gettins, J K, Stoops
Publikováno v: The Journal of biological chemistry. 273(15)
The reconstructions of an intermediate form of human alpha2-macroglobulin (half-transformed alpha2M) in which two of its four bait regions and thiol ester sites were cleaved by chymotrypsin bound to Sepharose were obtained by three-dimensional electr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cf43a1552a0bc5bc5984f8960b42f8ac
https://pubmed.ncbi.nlm.nih.gov/9535885
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4
Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris. Roles of subunit equilibria, non-globin linker chains, and valence of the heme iron
Autor: H, Zhu, D W, Ownby, C K, Riggs, N J, Nolasco, J K, Stoops, A F, Riggs
Publikováno v: The Journal of biological chemistry. 271(47)
The extracellular hemoglobin of the earthworm Lumbricus terrestris has four major kinds of O2-binding chains: a, b, and c (forming a disulfide-linked trimer), and chain d. Non-heme, non-globin structural chains, "linkers," are also present. Light-sca
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::20a1351298677a11ff697b0e063d5810
https://pubmed.ncbi.nlm.nih.gov/8939947
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5
Structure-function relationships of the Saccharomyces cerevisiae fatty acid synthase. Three-dimensional structure
Autor: S J, Kolodziej, P A, Penczek, J P, Schroeter, J K, Stoops
Publikováno v: The Journal of biological chemistry. 271(45)
The three-dimensional structure of the Saccharomyces cerevisie fatty acid synthase was computed from electron microscopy of stain images. The barrel-shaped structure (point group symmetry 32) has major and minor axes of approximately 245 x 220 A, res
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3a9e61c0b9fb6f906e7cd1b8a92803da
https://pubmed.ncbi.nlm.nih.gov/8910467
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6
Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images
Autor: J K, Stoops, T S, Baker, J P, Schroeter, S J, Kolodziej, X D, Niu, L J, Reed
Publikováno v: The Journal of biological chemistry. 267(34)
Dihydrolipoamide acyltransferase (E2), a catalytic and structural component of the three functional classes of multienzyme complexes that catalyze the oxidative decarboxylation of alpha-keto acids, forms the central core to which the other components
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9c14fa0348f46e8a7fa076798f18ddbb
https://pubmed.ncbi.nlm.nih.gov/1280269
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7
The yeast fatty acid synthase. Pathway for transfer of the acetyl group from coenzyme A to the Cys-SH of the condensation site
Autor: J K, Stoops, N, Singh, S J, Wakil
Publikováno v: The Journal of biological chemistry. 265(28)
The reaction pathway of enzyme-catalyzed acetylation of the acyl-accepting sites of the yeast synthase, a Ser-OH at the acetyl transacylase site, a Cys-SH at the beta-ketoacyl synthase site, and the acyl carrier protein 4'-phosphopantetheine-SH (Pant
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4802e670b3c508b792906396e129a879
https://pubmed.ncbi.nlm.nih.gov/2211602
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10
The arrangement and role of some of the amino acid residues in the beta-ketoacyl synthetase site of chicken liver fatty acid synthetase
Autor: S J Wakil, J K Stoops, S J Henry
Publikováno v: Journal of Biological Chemistry. 258:12482-12486
The beta-ketoacyl synthetase site of eukaryotic fatty acid synthetases is comprised in part of a pantetheinyl residue on one subunit juxtapositioned with a cysteinyl residue on the adjacent subunit. The present study has confirmed this arrangement an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7ad9782ecb736195122c6a3113ef3fb7
https://doi.org/10.1016/s0021-9258(17)44201-3
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