@misc{watson1968the14,
    author = "Watson, J. D",
    title = "The Double Helix",
    year = "1968",
    howpublished = "New York, Antheneum",
    note = "talkorigins\_source = {true}; raw\_reference = {Watson, J. D., 1968, The Double Helix: New York, Antheneum.}"
}

@incollection{doi101016b9781483232119500097,
    author = "Jukes, Thomas H. and Cantor, Charles R.",
    title = "Evolution of Protein Molecules",
    year = "1969",
    booktitle = "Elsevier eBooks",
    url = "https://doi.org/10.1016/b978-1-4832-3211-9.50009-7",
    doi = "10.1016/b978-1-4832-3211-9.50009-7",
    openalex = "W1525734744",
    references = "doi101001jama196603100230164053, doi101016s0021925818969450, doi101016s002192581897184x, doi101021bi00872a016, doi101038171737a0, doi101038202147a0, doi101073pnas316153, doi101073pnas504672, doi101126science147365368, doi101126science1553760279, doi101126science15838051200, doi1023072412074, openalexw2565219170, sarich1967immunological"
}

@article{kohne1972evolution9,
    author = "Kohne, D. E. and Chiscon, J. A. and Hoyer, B. H",
    title = "Evolution of primate DNA sequences",
    year = "1972",
    journal = "Journal of Human Evolution, v. 1, p. 627-644",
    note = "talkorigins\_source = {true}; raw\_reference = {Kohne, D. E., Chiscon, J. A., and Hoyer, B. H., 1972, Evolution of primate DNA sequences: Journal of Human Evolution, v. 1, p. 627-644.}"
}

@phdthesis{crick1976a4,
    author = "Crick, F. H. C. and Brenner, S. and Klug, A. and Pieczenik, G",
    title = "A speculation on the origin of protein systhesis",
    year = "1976",
    publisher = "Origins Life, v. 7, p. 389-397",
    note = "talkorigins\_source = {true}; raw\_reference = {Crick, F. H. C., Brenner, S., Klug, A., and Pieczenik, G., 1976, A speculation on the origin of protein systhesis: Origins Life, v. 7, p. 389-397.}"
}

@misc{crick1981life5,
    author = "Crick, F. J",
    title = "Life Itself",
    year = "1981",
    howpublished = "Its Origin and Nature: New York, Simon and Schuster",
    note = "talkorigins\_source = {true}; raw\_reference = {Crick, F. J., 1981, Life Itself: Its Origin and Nature: New York, Simon and Schuster.}"
}

@phdthesis{fox1981a7,
    author = "Fox, S. W",
    title = "A model for protocellular coordination of nucleic acid and protein synthesis, in Kageyama, M., Nakamura, K., Oshima, T., and Uchida, T., eds., Science and Scientists",
    year = "1981",
    publisher = "Tokyo, Japan Science Society Press, p. 39-45",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., 1981, A model for protocellular coordination of nucleic acid and protein synthesis, in Kageyama, M., Nakamura, K., Oshima, T., and Uchida, T., eds., Science and Scientists: Tokyo, Japan Science Society Press, p. 39-45.}"
}

@misc{crick1982life3,
    author = "Crick, F",
    title = "Life Itself",
    year = "1982",
    howpublished = "Its Origin and Nature: New York, W.W. Norton, 192 p",
    note = "talkorigins\_source = {true}; raw\_reference = {Crick, F., 1982, Life Itself: Its Origin and Nature: New York, W.W. Norton, 192 p.}"
}

@phdthesis{follmann1982deoxyribonucleotide6,
    author = "Follmann, H",
    title = "Deoxyribonucleotide systhesis and the emergence of DNA in molecular evolution",
    year = "1982",
    publisher = "Naturwissenschaften, v. 69, p. 75-81",
    note = "talkorigins\_source = {true}; raw\_reference = {Follmann, H., 1982, Deoxyribonucleotide systhesis and the emergence of DNA in molecular evolution: Naturwissenschaften, v. 69, p. 75-81.}"
}

@misc{stebbins1982darwin13,
    author = "Stebbins, G. L",
    title = "Darwin to DNA, Molecules to Humanity",
    year = "1982",
    howpublished = "San Francisco, W. H. Freeman, 491 p",
    note = "talkorigins\_source = {true}; raw\_reference = {Stebbins, G. L., 1982, Darwin to DNA, Molecules to Humanity: San Francisco, W. H. Freeman, 491 p.}"
}

@misc{lewin1984dna10,
    author = "Lewin, R",
    title = "DNA reveals surprises in human family tree",
    year = "1984",
    howpublished = "Science, v. 226, p. 1179-1182",
    note = "talkorigins\_source = {true}; raw\_reference = {Lewin, R., 1984, DNA reveals surprises in human family tree: Science, v. 226, p. 1179-1182.}"
}

@misc{lewin1984first11,
    author = "Lewin, R",
    title = "First true DNA catalyst found",
    year = "1984",
    howpublished = "Science, v. 223, p. 266-267",
    note = "talkorigins\_source = {true}; raw\_reference = {Lewin, R., 1984, First true DNA catalyst found: Science, v. 223, p. 266-267.}"
}

@article{sibley1984the12,
    author = "Sibley, C. and Ahlquist, J",
    title = "The phylogeny of the homonid primates as indicated by DNA-DNA hybridization",
    year = "1984",
    journal = "Journal of Molecular Evolution, v. 20, p. 2-15",
    note = "talkorigins\_source = {true}; raw\_reference = {Sibley, C., and Ahlquist, J., 1984, The phylogeny of the homonid primates as indicated by DNA-DNA hybridization: Journal of Molecular Evolution, v. 20, p. 2-15.}"
}

@misc{britten1986rates1,
    author = "Britten, R. J",
    title = "Rates of DNA sequence evolution differ between taxonomic groups",
    year = "1986",
    howpublished = "Science, v. 231, p. 1393-1398",
    note = "talkorigins\_source = {true}; raw\_reference = {Britten, R. J., 1986, Rates of DNA sequence evolution differ between taxonomic groups: Science, v. 231, p. 1393-1398.}"
}

@article{ghiselin1986we8,
    author = "Ghiselin, M. T",
    title = "We Are All Contraptions",
    year = "1986",
    journal = "New York Times Book Review, p. 18-19",
    note = "talkorigins\_source = {true}; raw\_reference = {Ghiselin, M. T., 1986, We Are All Contraptions: New York Times Book Review, p. 18-19.}"
}

@misc{cann1987mitochondrial2,
    author = "Cann, R. L. and Stoncking, M. and Wilson, A. C",
    title = "Mitochondrial DNA and human evolution",
    year = "1987",
    howpublished = "Nature, v. 325, p. 31-36",
    note = "talkorigins\_source = {true}; raw\_reference = {Cann, R. L., Stoncking, M., and Wilson, A. C., 1987, Mitochondrial DNA and human evolution: Nature, v. 325, p. 31-36.}"
}

@article{petkov1989effects,
    author = "Petkov, A. and Todorov, N. and Enev, E. and Oblakov, N. and Demeyer, D.",
    title = "Effects of Defaunation on Degradability and Protein Systhesis in the Rumen of Sheep",
    year = "1989",
    journal = "Asian-Australasian Journal of Animal Sciences",
    url = "https://doi.org/10.5713/ajas.1989.469",
    doi = "10.5713/ajas.1989.469",
    number = "3",
    openalex = "W2088633493",
    pages = "469-470",
    volume = "2"
}

@article{doi101038351652a0,
    author = "McDonald, John H. and Kreitman, Martin",
    title = "Adaptive protein evolution at the Adh locus in Drosophila",
    year = "1991",
    journal = "Nature",
    url = "https://doi.org/10.1038/351652a0",
    doi = "10.1038/351652a0",
    openalex = "W1982603712",
    references = "doi101007bf02984069, doi107312nei92038"
}

@article{doi101093oxfordjournalsmolbeva040153,
    author = "Goldman, Nick and Yang, Zefeng",
    title = "A codon-based model of nucleotide substitution for protein-coding DNA sequences.",
    year = "1994",
    journal = "Molecular Biology and Evolution",
    abstract = "A codon-based model for the evolution of protein-coding DNA sequences is presented for use in phylogenetic estimation. A Markov process is used to describe substitutions between codons. Transition/transversion rate bias and codon usage bias are allowed in the model, and selective restraints at the protein level are accommodated using physicochemical distances between the amino acids coded for by the codons. Analyses of two data sets suggest that the new codon-based model can provide a better fit to data than can nucleotide-based models and can produce more reliable estimates of certain biologically important measures such as the transition/transversion rate ratio and the synonymous/nonsynonymous substitution rate ratio.",
    url = "https://doi.org/10.1093/oxfordjournals.molbev.a040153",
    doi = "10.1093/oxfordjournals.molbev.a040153",
    openalex = "W1920973730",
    references = "doi101007bf02407308, doi101093oxfordjournalsmolbeva040343, doi101093oxfordjournalsmolbeva040410"
}

@article{doi101046j1365313x1999t01100606x,
    author = "Meyers, Blake C. and Dickerman, Allan W. and Michelmore, Richard W. and Sivaramakrishnan, S. and Sobral, Bruno and Young, Nevin D.",
    title = "Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily",
    year = "1999",
    journal = "The Plant Journal",
    abstract = "The nucleotide binding site (NBS) is a characteristic domain of many plant resistance gene products. An increasing number of NBS-encoding sequences are being identified through gene cloning, PCR amplification with degenerate primers, and genome sequencing projects. The NBS domain was analyzed from 14 known plant resistance genes and more than 400 homologs, representing 26 genera of monocotyledonous, dicotyle-donous and one coniferous species. Two distinct groups of diverse sequences were identified, indicating divergence during evolution and an ancient origin for these sequences. One group was comprised of sequences encoding an N-terminal domain with Toll/Interleukin-1 receptor homology (TIR), including the known resistance genes, N, M, L6, RPP1 and RPP5. Surprisingly, this group was entirely absent from monocot species in searches of both random genomic sequences and large collections of ESTs. A second group contained monocot and dicot sequences, including the known resistance genes, RPS2, RPM1, I2, Mi, Dm3, Pi-B, Xa1, RPP8, RPS5 and Prf. Amino acid signatures in the conserved motifs comprising the NBS domain clearly distinguished these two groups. The Arabidopsis genome is estimated to contain approximately 200 genes that encode related NBS motifs; TIR sequences were more abundant and outnumber non-TIR sequences threefold. The Arabidopsis NBS sequences currently in the databases are located in approximately 21 genomic clusters and 14 isolated loci. NBS-encoding sequences may be more prevalent in rice. The wide distribution of these sequences in the plant kingdom and their prevalence in the Arabidopsis and rice genomes indicate that they are ancient, diverse and common in plants. Sequence inferences suggest that these genes encode a novel class of nucleotide-binding proteins.",
    url = "https://doi.org/10.1046/j.1365-313x.1999.t01-1-00606.x",
    doi = "10.1046/j.1365-313x.1999.t01-1-00606.x",
    openalex = "W1989581558"
}

@article{doi101093bioinformatics157563,
    author = "Hertz, Gerald Z. and Stormo, Gary D.",
    title = "Identifying DNA and protein patterns with statistically significant alignments of multiple sequences.",
    year = "1999",
    journal = "Bioinformatics",
    abstract = "MOTIVATION: Molecular biologists frequently can obtain interesting insight by aligning a set of related DNA, RNA or protein sequences. Such alignments can be used to determine either evolutionary or functional relationships. Our interest is in identifying functional relationships. Unless the sequences are very similar, it is necessary to have a specific strategy for measuring-or scoring-the relatedness of the aligned sequences. If the alignment is not known, one can be determined by finding an alignment that optimizes the scoring scheme. RESULTS: We describe four components to our approach for determining alignments of multiple sequences. First, we review a log-likelihood scoring scheme we call information content. Second, we describe two methods for estimating the P value of an individual information content score: (i) a method that combines a technique from large-deviation statistics with numerical calculations; (ii) a method that is exclusively numerical. Third, we describe how we count the number of possible alignments given the overall amount of sequence data. This count is multiplied by the P value to determine the expected frequency of an information content score and, thus, the statistical significance of the corresponding alignment. Statistical significance can be used to compare alignments having differing widths and containing differing numbers of sequences. Fourth, we describe a greedy algorithm for determining alignments of functionally related sequences. Finally, we test the accuracy of our P value calculations, and give an example of using our algorithm to identify binding sites for the Escherichia coli CRP protein. AVAILABILITY: Programs were developed under the UNIX operating system and are available by anonymous ftp from ftp://beagle.colorado.edu/pub/consensus.",
    url = "https://doi.org/10.1093/bioinformatics/15.7.563",
    doi = "10.1093/bioinformatics/15.7.563",
    openalex = "W2003967338"
}

@article{dubertret2001dynamics,
    author = "Dubertret, Benoit and Liu, Shumo and Ouyang, Qi and Libchaber, Albert",
    title = "Dynamics of DNA-Protein Interaction Deduced from in vitro DNA Evolution",
    year = "2001",
    journal = "Physical Review Letters",
    url = "https://doi.org/10.1103/physrevlett.86.6022",
    doi = "10.1103/physrevlett.86.6022",
    number = "26",
    openalex = "W1980609565",
    pages = "6022-6025",
    volume = "86",
    references = "doi101006jmbi19960406, doi101016s0022283661800727, doi10103873317, doi101073pnas5661891, doi101073pnas581217, doi101073pnas70123581, doi101073pnas80226785, doi101093nar18133739, doi101126science2200121, doi101126science27152531247"
}

@article{creevey2003crann,
    author = "Creevey, C.J. and McInerney, J.O.",
    title = "CRANN: detecting adaptive evolution in protein-coding DNA sequences",
    year = "2003",
    journal = "Bioinformatics",
    abstract = "Summary: A software program CRANN has been developed in order to detect adaptive evolution in protein-coding DNA sequences. Availability: CRANN is available from http://bioinf.may.ie/crann/ Supplementary Information: CRANN has been written in the C programming language. Source code is available on request.",
    url = "https://doi.org/10.1093/bioinformatics/btg225",
    doi = "10.1093/bioinformatics/btg225",
    number = "13",
    openalex = "W2104540125",
    pages = "1726-1726",
    volume = "19",
    references = "doi101007bf02407308, doi101016s0378111902010399, doi101038385151a0, doi101093oxfordjournalsmolbeva040343, doi101093oxfordjournalsmolbeva040454"
}

@article{doi101146annurevgenom4020303162528,
    author = "Fay, Justin C. and Wu, Chung‐I",
    title = "Sequence Divergence, Functional Constraint, and Selection in Protein Evolution",
    year = "2003",
    journal = "Annual Review of Genomics and Human Genetics",
    abstract = "The genome sequences of multiple species has enabled functional inferences from comparative genomics. A primary objective is to infer biological functions from the conservation of homologous DNA sequences between species. A second, more difficult, objective is to understand what functional DNA sequences have changed over time and are responsible for species' phenotypic differences. The neutral theory of molecular evolution provides a theoretical framework in which both objectives can be explicitly tested. Development of statistical tests within this framework has provided insight into the evolutionary forces that constrain and in some cases change DNA sequences and the resulting patterns that emerge. In this article, we review recent work on how functional constraint and changes in protein function are inferred from protein polymorphism and divergence data. We relate these studies to our understanding of the neutral theory and adaptive evolution.",
    url = "https://doi.org/10.1146/annurev.genom.4.020303.162528",
    doi = "10.1146/annurev.genom.4.020303.162528",
    openalex = "W2115759361",
    references = "doi101016s0378111902010399"
}

@article{doi101093nargkl315,
    author = "Suyama, Mikita and Torrents, David and Bork, Peer",
    title = "PAL2NAL: robust conversion of protein sequence alignments into the corresponding codon alignments",
    year = "2006",
    journal = "Nucleic Acids Research",
    abstract = "PAL2NAL is a web server that constructs a multiple codon alignment from the corresponding aligned protein sequences. Such codon alignments can be used to evaluate the type and rate of nucleotide substitutions in coding DNA for a wide range of evolutionary analyses, such as the identification of levels of selective constraint acting on genes, or to perform DNA-based phylogenetic studies. The server takes a protein sequence alignment and the corresponding DNA sequences as input. In contrast to other existing applications, this server is able to construct codon alignments even if the input DNA sequence has mismatches with the input protein sequence, or contains untranslated regions and polyA tails. The server can also deal with frame shifts and inframe stop codons in the input models, and is thus suitable for the analysis of pseudogenes. Another distinct feature is that the user can specify a subregion of the input alignment in order to specifically analyze functional domains or exons of interest. The PAL2NAL server is available at http://www.bork.embl.de/pal2nal.",
    url = "https://doi.org/10.1093/nar/gkl315",
    doi = "10.1093/nar/gkl315",
    openalex = "W2046183549",
    references = "doi101093oxfordjournalsmolbeva026334"
}

@article{doi101126science1123539,
    author = "Weinreich, Daniel and Delaney, Nigel F. and DePristo, Mark A. and Hartl, Daniel L.",
    title = "Darwinian Evolution Can Follow Only Very Few Mutational Paths to Fitter Proteins",
    year = "2006",
    journal = "Science",
    abstract = "Five point mutations in a particular beta-lactamase allele jointly increase bacterial resistance to a clinically important antibiotic by a factor of approximately 100,000. In principle, evolution to this high-resistance beta-lactamase might follow any of the 120 mutational trajectories linking these alleles. However, we demonstrate that 102 trajectories are inaccessible to Darwinian selection and that many of the remaining trajectories have negligible probabilities of realization, because four of these five mutations fail to increase drug resistance in some combinations. Pervasive biophysical pleiotropy within the beta-lactamase seems to be responsible, and because such pleiotropy appears to be a general property of missense mutations, we conclude that much protein evolution will be similarly constrained. This implies that the protein tape of life may be largely reproducible and even predictable.",
    url = "https://doi.org/10.1126/science.1123539",
    doi = "10.1126/science.1123539",
    openalex = "W2016666153",
    references = "doi101016jdrup200402003, doi101016s002228360200400x, doi101038370389a0, doi101038nrg1523, doi101038nrg1672, doi101042bj2760269, doi101093clinids24supplement1s19, doi101111j155856461984tb00380x, doi1011289781555817886, doi10155404272"
}

@article{doi101371journalpone0004809,
    author = "Ansong, Charles and Yoon, Hyunjin and Porwollik, Steffen and Mottaz-Brewer, Heather M. and Petritis, Brianne and Jaitly, Navdeep and Adkins, Joshua and McClelland, Michael and Heffron, Fred and Smith, Richard",
    title = "Global Systems-Level Analysis of Hfq and SmpB Deletion Mutants in Salmonella: Implications for Virulence and Global Protein Translation",
    year = "2009",
    journal = "PLoS ONE",
    abstract = "Using sample-matched transcriptomics and proteomics measurements it is now possible to begin to understand the impact of post-transcriptional regulatory programs in Enterobacteria. In bacteria post-transcriptional regulation is mediated by relatively few identified RNA-binding protein factors including CsrA, Hfq and SmpB. A mutation in any one of these three genes, csrA, hfq, and smpB, in Salmonella is attenuated for mouse virulence and unable to survive in macrophages. CsrA has a clearly defined specificity based on binding to a specific mRNA sequence to inhibit translation. However, the proteins regulated by Hfq and SmpB are not as clearly defined. Previous work identified proteins regulated by hfq using purification of the RNA-protein complex with direct sequencing of the bound RNAs and found binding to a surprisingly large number of transcripts. In this report we have used global proteomics to directly identify proteins regulated by Hfq or SmpB by comparing protein abundance in the parent and isogenic hfq or smpB mutant. From these same samples we also prepared RNA for microarray analysis to determine if alteration of protein expression was mediated post-transcriptionally. Samples were analyzed from bacteria grown under four different conditions; two laboratory conditions and two that are thought to mimic the intracellular environment. We show that mutants of hfq and smpB directly or indirectly modulate at least 20\% and 4\% of all possible Salmonella proteins, respectively, with limited correlation between transcription and protein expression. These proteins represent a broad spectrum of Salmonella proteins required for many biological processes including host cell invasion, motility, central metabolism, LPS biosynthesis, two-component regulatory systems, and fatty acid metabolism. Our results represent one of the first global analyses of post-transcriptional regulons in any organism and suggest that regulation at the translational level is widespread and plays an important role in virulence regulation and environmental adaptation for Salmonella.",
    url = "https://doi.org/10.1371/journal.pone.0004809",
    doi = "10.1371/journal.pone.0004809",
    openalex = "W2076696121",
    references = "doi10103835101614, doi101046j13652958200303313x, doi101073pnas120163297, doi101073pnas83145189, doi101126science2715251990, doi101128mmbr5344504901989, doi101128mr5344504901989, doi101146annurevbiochem691183, doi101146annurevmicro58030603123841, doi101371journalpgen1000163"
}

@article{doi101038nrg3927,
    author = "Packer, Michael S. and Liu, David R.",
    title = "Methods for the directed evolution of proteins",
    year = "2015",
    journal = "Nature Reviews Genetics",
    url = "https://doi.org/10.1038/nrg3927",
    doi = "10.1038/nrg3927",
    openalex = "W1954202239",
    references = "doi101073pnas91156808, doi101093nar18133739"
}

@article{doi101093gbeevw036,
    author = "Kusch, Stefan and Pesch, Lina and Panstruga, Ralph",
    title = "Comprehensive Phylogenetic Analysis Sheds Light on the Diversity and Origin of the MLO Family of Integral Membrane Proteins",
    year = "2016",
    journal = "Genome Biology and Evolution",
    abstract = "Mildew resistanceLocusO(MLO) proteins are polytopic integral membrane proteins that have long been considered as plant-specific and being primarily involved in plant-powdery mildew interactions. However, research in the past decade has revealed that MLO proteins diverged into a family with several clades whose members are associated with different physiological processes. We provide a largely increased dataset of MLO amino acid sequences, comprising nearly all major land plant lineages. Based on this comprehensive dataset, we defined seven phylogenetic clades and reconstructed the likely evolution of the MLO family in embryophytes. We further identified several MLO peptide motifs that are either conserved in all MLO proteins or confined to one or several clades, supporting the notion that clade-specific diversification of MLO functions is associated with particular sequence motifs. In baker's yeast, some of these motifs are functionally linked to transmembrane (TM) transport of organic molecules and ions. In addition, we attempted to define the evolutionary origin of the MLO family and found that MLO-like proteins with highly diverse membrane topologies are present in green algae, but also in the distinctly related red algae (Rhodophyta), Amoebozoa, and Chromalveolata. Finally, we discovered several instances of putative fusion events between MLO proteins and different kinds of proteins. Such Rosetta stone-type hybrid proteins might be instructive for future analysis of potential MLO functions. Our findings suggest that MLO is an ancient protein that possibly evolved in unicellular photosynthetic eukaryotes, and consolidated in land plants with a conserved topology, comprising seven TM domains and an intrinsically unstructured C-terminus.",
    url = "https://doi.org/10.1093/gbe/evw036",
    doi = "10.1093/gbe/evw036",
    openalex = "W2294763389",
    references = "doi101016jgene200710031"
}

@misc{madru2022dnabinding,
    author = "Madru, Clément and Martinez-Carranza, Markel and Laurent, Sébastien and Alberti, Alessandra C. and Chevreuil, Maelenn and Raynal, Bertrand and Haouz, Ahmed and Le Meur, Rémy A. and Delarue, Marc and Flament, Didier and Krupovic, Mart and Legrand, Pierre and Sauguet, Ludovic",
    title = "DNA-binding mechanism and evolution of Replication Protein A",
    year = "2022",
    abstract = "Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair, in both eukaryotic and archaeal cells. By using an integrative approach that combines three crystal structures, four cryo-EM structures in complex with single-stranded DNA (ssDNA) of different lengths, we extensively characterized RPA from Pyrococcus abyssi in different states. These structures show two essential features conserved in eukaryotes: a trimeric core and a module that promotes cooperative binding to ssDNA, as well as a newly identified archaeal-specific domain. These structures reveal for the first time how ssDNA is handed over from one RPA complex to the other, and uncover an unanticipated mechanism of self-association on ssDNA tracts. This work constitutes a significant step forward in the molecular understanding of the structure and DNA-binding mechanism of RPA, with far-reaching implications for the evolution of this primordial replication factor in Archaea and Eukarya.",
    url = "https://doi.org/10.1101/2022.07.20.500673",
    doi = "10.1101/2022.07.20.500673",
    openalex = "W4286007468",
    references = "doi101002pro3943, doi101016jjmb200705022, doi101038nmeth4169, doi101038s41586021038192, doi101093nargkaa913, doi101107s0021889807021206, doi101107s0108767307043930, doi101107s0907444904019158, doi101107s0907444909047337, doi101107s0907444910007493"
}