Zobrazeno 1 - 10 of 39 pro vyhledávání: '"L H, Weaver"'
2
In Vitro Analysis of Transformation Potential Associated with Retroviral Vector Insertions
Autor: L. H. Weaver, Russette M. Lyons, Sharon K. Powell, Irina Burimski, Zhifeng Long, Edward Otto, Michele Kaloss, Gerard J. McGarrity
Publikováno v: Human Gene Therapy. 10:2123-2132
While replication-defective retroviral vectors provide excellent vehicles for the long-term expression of therapeutic genes, they also harbor the potential to induce undesired genetic changes by random insertions into the host genome. The rate of ins
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dafb0d95978ac0971a585951e728dc2
https://doi.org/10.1089/10430349950017112
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3
Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site
Autor: Brian W. Matthews, L. H. Weaver, Ryota Kuroki
Publikováno v: Proceedings of the National Academy of Sciences. 96:8949-8954
In contrast to hen egg-white lysozyme, which retains the β-configuration of the substrate in the product, T4 lysozyme (T4L) is an inverting glycosidase. The substitution Thr-26 → His, however, converts T4L from an inverting to a retaining enzyme.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0fb9e9778632c1a67502dda28cf7f87
https://doi.org/10.1073/pnas.96.16.8949
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4
Crystal Structure of Phosphatidylinositol-Specific Phospholipase C from Bacillus cereus in Complex with Glucosaminyl(α1→6)-d-myo-inositol, an Essential Fragment of GPI Anchors
Autor: M. P. Smith, J. F. W. Keana, Dirk W. Heinz, M. Ryan, L. H. Weaver, O. H. Griffith
Publikováno v: Biochemistry. 35:9496-9504
Numerous proteins on the external surface of the plasma membrane are anchored by glycosylated derivatives of phosphatidylinositol (GPI), rather than by hydrophobic amino acids embedded in the phospholipid bilayer. These GPI anchors are cleaved by pho
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4675d05698adb42b6c2b0d3cd0d63bee
https://doi.org/10.1021/bi9606105
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5
Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold
Autor: L H Weaver, Brian W. Matthews, S L Roderick, J F Bazan, Robert Huber
Publikováno v: Proceedings of the National Academy of Sciences. 91:2473-2477
Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) are related. A detailed comparison of the three-dimensiona
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4483f22d3321c540b7853b5ad4720c35
https://doi.org/10.1073/pnas.91.7.2473
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6
Three-dimensional structure of human basic fibroblast growth factor
Autor: L. H. Weaver, A E Eriksson, Brian W. Matthews, L S Cousens
Publikováno v: Proceedings of the National Academy of Sciences. 88:3441-3445
The three-dimensional structure of human basic fibroblast growth factor (bFGF) has been determined by x-ray crystallography and refined to a crystallographic residual of 17.4% at 2.2-A resolution. The structure was initially solved at a nominal resol
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f21b3a5c55234065aa3c3c5d49f40806
https://doi.org/10.1073/pnas.88.8.3441
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7
Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability
Autor: J W, Wray, W A, Baase, J D, Lindstrom, L H, Weaver, A R, Poteete, B W, Matthews
Publikováno v: Journal of molecular biology. 292(5)
The mutation Glu108--Val (E108V) in T4 lysozyme was previously isolated as a second-site revertant that specifically compensated for the loss of function associated with the destabilizing substitution Leu99--Gly (L99G). Surprisingly, the two sites ar
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5c2f94137e507428ea191b3a5818aa5e
https://pubmed.ncbi.nlm.nih.gov/10512706
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9
Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes
Autor: Richard L. Kendall, L. H. Weaver, Ralph A. Bradshaw, Albert E. Stewart, Brian W. Matthews, Stuart M. Arfin, Linda Hall
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 92(17)
Using partial amino acid sequence data derived from porcine methionyl aminopeptidase (MetAP; methionine aminopeptidase, peptidase M; EC 3.4.11.18), a full-length clone of the homologous human enzyme has been obtained. The cDNA sequence contains 2569
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e86bd288d413a0ddc61bb12f9dd2f440
https://pubmed.ncbi.nlm.nih.gov/7644482
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10
Improved methods of retroviral vector transduction and production for gene therapy
Autor: Shuyuan Zhang, Yawen L. Chiang, Hitoshi Kotani, Edward Otto, Gerard J. McGarrity, R. Michael Blaese, Perry Newton, W. French Anderson, L. H. Weaver
Publikováno v: Human gene therapy. 5(1)
To facilitate clinical applications of retroviral-mediated human gene transfer, retroviral vectors must be of high titer and free of detectable replication-competent retroviruses. The purpose of this study was to optimize methods of retroviral vector
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0d282d26caef375a5af7b9f4d350c9e
https://pubmed.ncbi.nlm.nih.gov/8155767
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