Výsledky vyhledávání - "K L, Constantine"

Akademický článek

An assessment of the capacity and responsiveness of a national system to address the threat of invasive species: a systems approach

Autor: F. Williams, K. L. Constantine, A. A. Ali, T. W. Karanja, S. Kibet, E. K. Lingeera, G. Muthike, I. Rwomushana, J. Godwin, R. Day

Publikováno v: CABI Agriculture and Bioscience, Vol 2, Iss 1, Pp 1-17 (2021)

Abstract Background Invasive species affect the social, economic and health aspects of many farmers and are known to cause major losses with considerable costs spent on management. Several international agreements recognise the threat caused by invas

Externí odkaz: https://doaj.org/article/dec24acd7082437f9604b0543d1126c3

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An assessment of the capacity and responsiveness of a national system to address the threat of invasive species: a systems approach with examples from Kenya and Zambia

Autor: F. Williams, K. L. Constantine, A. A. Ali, J. Godwin, T. W. Karanja, S. Kibet, E. K. Lingeera, J. M. Mulila-Mitti, G. Muthike, I. Rwomushana, R. Day

Publikováno v: agriRxiv. 2021

Background: Invasive species affect the social, economic and health aspects of many farmers and are known to cause major losses with considerable costs spent on management. Several international agreements recognise the threat caused by invasive spec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::46391732ac9f325945c436c7de0f2767
https://doi.org/10.31220/agrirxiv.2021.00049

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Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern

Autor: W J, Metzler, K L, Constantine, M S, Friedrichs, A J, Bell, E G, Ernst, T B, Lavoie, L, Mueller

Publikováno v: Biochemistry. 32(50)

Human profilin is a 15-kDa protein that plays a major role in the signaling pathway leading to cytoskeletal rearrangement. Essentially complete assignment of the 1H, 13C, and 15N resonances of human profilin have been made by analysis of multidimensi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1a2d25878bc9daea4192b605ef5cd4a7
https://pubmed.ncbi.nlm.nih.gov/8268157

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Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain

Autor: K L, Constantine, V, Goldfarb, M, Wittekind, J, Anthony, S C, Ng, L, Mueller

Publikováno v: Biochemistry. 31(21)

A uniformly 15N-labeled recombinant light-chain variable (VL) domain from the anti-digoxin antibody 26-10 has been investigated by heteronuclear two-dimensional (2D) and three-dimensional (3D) NMR spectroscopy. Complementary homonuclear 2D NMR studie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::11da783b1ef5199ebaf0723fe87eeaa1
https://pubmed.ncbi.nlm.nih.gov/1318076

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Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain

Autor: K L, Constantine, M, Madrid, L, Bányai, M, Trexler, L, Patthy, M, Llinás

Publikováno v: Journal of molecular biology. 223(1)

We have determined, via 1H-n.m.r., the solution conformation of the collagen-binding b-domain of the bovine seminal fluid protein PDC-109 (PDC-109/b). The structure determination is based on 341 interproton distance estimates and 42 dihedral angle es

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7bc05f6ffea11a78f622d5f6f2de8d82
https://pubmed.ncbi.nlm.nih.gov/1731074

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Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b

Autor: K L, Constantine, V, Ramesh, L, Bányai, M, Trexler, L, Patthy, M, Llinás

Publikováno v: Biochemistry. 30(6)

Sequence-specific resonance assignments for the isolated second or b domain of the bovine seminal fluid protein PDC-109 have been obtained from analysis of two-dimensional 1H NMR experiments recorded at 500 MHz. These assignments include the identifi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b333a9ad574c7409b4cae4d43accee8d
https://pubmed.ncbi.nlm.nih.gov/1993183

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The solution conformations of ferrichrome and deferriferrichrome determined by 1H-NMR spectroscopy and computational modeling

Autor: K L, Constantine, A, De Marco, M, Madrid, C L, Brooks, M, Llinás

Publikováno v: Biopolymers. 30(3-4)

We have applied computational procedures that utilize nmr data to model the solution conformation of ferrichrome, a rigid microbial iron transport cyclohexapeptide of known x-ray crystallographic structure [D. van der Helm et al. (1980) J. Am. Chem.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::367730fbf3a58dfe6c2aec281fab405c
https://pubmed.ncbi.nlm.nih.gov/2279065

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