Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Nancy L. Scott"'
Autor:
Nancy L. Scott, Chase A. LaDue
Publikováno v:
Zoo biology. 38(5)
Population-level analyses suggest that habitat complexity, but not necessarily space availability, has important welfare outcomes for elephants in human care. At the Dallas Zoo, the opening of a new exhibit complex allowed us to measure the behavior
Autor:
Nancy L. Scott, Juliette T. J. Lecomte
Publikováno v:
Protein Science. 9:587-597
The genome of the unicellular cyanobacterium Synechocystis sp. PCC 6803 contains a gene (slr2097, glbN) encoding a 123 amino-acid product with sequence similarity to globins. Related proteins from cyanobacteria, ciliates, and green algae bind oxygen
Publikováno v:
Biochemistry. 40:6541-6552
The product of the cyanobacterium Synechocystis sp. PCC 6803 gene slr2097 is a 123 amino acid polypeptide chain belonging to the truncated hemoglobin family. Recombinant, ferric heme-reconstituted Synechocystis sp. PCC 6803 hemoglobin is a low-spin c
Autor:
Juliette T. J. Lecomte, Christopher J. Falzone, Shibani Bhattacharya, Nancy L. Scott, B.C. Vu, Y. Wang
Publikováno v:
Biochemistry. 40:4879-4891
The water-soluble domain of rat hepatic cytochrome b(5) undergoes marked structural changes upon heme removal. The solution structure of apocytochrome b(5) shows that the protein is partially folded in the absence of the heme group, exhibiting a stab
Autor:
Matthew P. Pond, Gaozhong Shen, David A. Vuletich, Juliette T. J. Lecomte, Donald A. Bryant, Christopher J. Falzone, Zhongkui Li, Matthew R. Preimesberger, Nancy L. Scott, Marcus Ludwig, Yu Xu
Publikováno v:
Biochemistry. 49(33)
Cyanobacterium Synechococcus sp. PCC 7002 contains a single gene (glbN) coding for GlbN, a protein of the 2/2 hemoglobin lineage. The precise function of GlbN is not known, but comparison to similar 2/2 hemoglobins suggests that reversible dioxygen b
Autor:
Nancy L. Scott, L. E. L. Rasmussen
Publikováno v:
Chemical Signals in Vertebrates 10 ISBN: 9780387251592
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::166c1cee65c95bcd4f9f86ecfdde1b93
https://doi.org/10.1007/0-387-25160-x_16
https://doi.org/10.1007/0-387-25160-x_16
Autor:
L.E.L. Rasmussen, Sarah M. Heineman, Amy Gray, Barbara E. Slade, Kathryn R. Bagley, Bruce A. Schulte, Michelle Malament, Nancy L. Scott, Maureen D. Correll, Lauren Stanley, Thomas E. Goodwin, Helen Loizi
Publikováno v:
Chemical Signals in Vertebrates 10 ISBN: 9780387251592
The study of chemical communication in elephants has resulted in startling and exciting new discoveries in the past decade (Rasmussen and Schulte, 1998; Rasmussen et al., 2003). To date, the highlight of this research has been the identification of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e459220874eb25e010440b96313092c0
https://doi.org/10.1007/0-387-25160-x_18
https://doi.org/10.1007/0-387-25160-x_18
Autor:
Juliette T. J. Lecomte, David A. Vuletich, Nancy L. Scott, Syna A. Kuriakose, B. Christie Vu, Christopher J. Falzone
Publikováno v:
Micron (Oxford, England : 1993). 35(1-2)
The truncated hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl sub
Publikováno v:
Journal of molecular biology. 324(5)
The product of the cyanobacterium Synechocystis sp. PCC 6803 gene slr2097 is a 123 amino acid polypeptide chain belonging to the truncated hemoglobin family. Recombinant, ferric heme-reconstituted Synechocystis sp. PCC 6803 hemoglobin displays bis-hi