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  • 1
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2015. This is the author's version of the work. It is posted here by permission of John Wiley & Sons for personal use, not for redistribution. The definitive version was published in Natural Resource Modeling 28 (2015): 456-474, doi:10.1111/nrm.12075.
    Description: Marine reserves are an increasingly used and potentially contentious tool in fisheries management. Depending upon the way that individuals move, no-take marine reserves can be necessary for maximizing equilibrium rent in some simple mathematical models. The implementation of no-take marine reserves often generates a redistribution of fishing effort in space. This redistribution of effort, in turn, produces sharp spatial gradients in mortality rates for the targeted stock. Using a two-patch model, we show that the existence of such gradients is a sufficient condition for the evolution of an evolutionarily stable conditional dispersal strategy. Thus, the dispersal strategy of the fish depends upon the harvesting strategy of the manager and vice versa. We find that an evolutionarily stable optimal harvesting strategy (ESOHS)—one which maximizes equilibrium rent given that fish disperse in an evolutionarily stable manner– - never includes a no-take marine reserve. This strategy is economically unstable in the short run because a manager can generate more rent by disregarding the possibility of dispersal evolution. Simulations of a stochastic evolutionary process suggest that such a short-run, myopic strategy performs poorly compared to the ESOHS over the long run, however, as it generates rent that is lower on average and higher in variability.
    Description: This material is based upon work supported by funding from: The Woods Hole Oceanographic Institution's Investment in Science Fund to MGN; The Recruitment Program of Global Experts to YL; The University of Tennessee Center for Business and Economics Research to SL; and the U.S. National Science Foundation (NSF) through grants OCE-1031256, DEB-1257545, and DEB-1145017 to MGN, CNH-0707961 to GEH, DMS-1411476 to YL; and NSF Graduate Research Fellowships under Grant No. 1122374 to EAM and ES.
    Keywords: Evolution of dispersal ; Evolutionarily stable strategy ; Fisheries management ; Marine protected areas ; Optimal harvesting
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
    Format: application/pdf
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  • 2
    ISSN: 1573-5001
    Keywords: CD ; HDAg ; HDV ; RNA binding ; solution conformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Hepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus (HBV) which provides the surface antigen for the viral coat. Our results show that the N-terminal leucine-repeat region of hepatitis delta antigen (HDAg), encompassing residues 24–50, binds to the autolytic domain of HDV genomic RNA and attenuates its autolytic activity. The solution conformation of a synthetic peptide corresponding to residues 24–50 of HDAg as determined by two-dimensional 1H NMR and circular dichroism techniques is found to be an α-helix. The local helix content of this peptide was analyzed by NOEs and coupling constants. Mutagenesis studies indicate that Lys38, Lys39, and Lys40 within this α-helical peptide may be directly involved in RNA binding. A structural knowledge of the N-terminal leucine-repeat region of HDAg thus provides a molecular basis for understanding its role in the interaction with RNA.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5001
    Keywords: BTK ; peptide binding ; proline-rich peptide ; SH3 domain ; XLA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract X-linked agammaglobulinemia (XLA), an inherited disease, is caused by mutations in the Bruton's tyrosine kinase (BTK). The absence of functional BTK leads to failure of B cell differentiation which incapacitates antibody production in XLA patients leading to, sometimes lethal, bacterial infections. Point mutation in the BTK gene that leads to deletion of C-terminal 14 aa residues of BTK SH3 domain was found in one patient family. To understand the role of BTK in B cell development, we have determined the solution structure of BTK SH3 domain complexed with a proline-rich peptide from the protein product of c-cbl protooncogene (p120cbl). Like other SH3 domains, BTK SH3 domain consists of five β-strands packed in two β-sheets forming a β-barrel-like structure. The rmsd calculated from the averaged coordinates for the BTK SH3 domain residues 218–271 and the p120cbl peptide residues 6–12 of the complex was 0.87 Å (±0.16 Å) for the backbone heavy atoms (N, C, and Cα) and 1.64 Å (±0.16 Å) for all heavy atoms. Based on chemical shift changes and inter-molecular NOEs, we have found that the residues located in the RT loop, n-Src loop and helix-like loop between β4 and β5 of BTK SH3 domain are involved in ligand binding. We have also determined that the proline-rich peptide from p120cbl binds to BTK SH3 domain in a class I orientation. These results correlate well with our earlier observation that the truncated BTK SH3 domain (deletion of β4, β5 and the helix-like loop) exhibits weaker affinity for the p120cbl peptide. It is likely that the truncated SH3 domain fails to present to the ligand the crucial residues in the correct context and hence the weaker binding. These results delineate the importance of the C-terminus in the binding of SH3 domains and also indicate that improper folding and the altered binding behavior of mutant BTK SH3 domain likely lead to XLA.
    Type of Medium: Electronic Resource
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  • 4
    Publication Date: 2014-07-05
    Description: Environmental Science & Technology DOI: 10.1021/es502366g
    Print ISSN: 0013-936X
    Electronic ISSN: 1520-5851
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering
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  • 5
    Publication Date: 2015-06-23
    Description: Analytical Chemistry DOI: 10.1021/acs.analchem.5b01099
    Print ISSN: 0003-2700
    Electronic ISSN: 1520-6882
    Topics: Chemistry and Pharmacology
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