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1

Eble, Johannes A., and Klaus Kühn. Integrin-Ligand Interaction. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-4064-6.

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2

Roterman-Konieczna, Irena, ed. Identification of Ligand Binding Site and Protein-Protein Interaction Area. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5285-6.

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3

Kozik, Andrzej. Thiamine-protein interaction: Chemical mechanism of ligand-binding and bioanalytical application of thiamine-binding proteins from seeds. Kraków: Nakł. Uniwersytetu Jagiellońskiego, 1996.

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4

Russo, Nino, and Dennis R. Salahub, eds. Metal-Ligand Interactions. Dordrecht: Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-0155-1.

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5

Guschlbauer, Wilhelm, and Wolfram Saenger, eds. DNA—Ligand Interactions. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5383-6.

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6

Gohlke, Holger, ed. Protein-Ligand Interactions. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527645947.

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7

Williams, Mark A., and Tina Daviter, eds. Protein-Ligand Interactions. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-398-5.

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8

Russo, Nino, Dennis R. Salahub, and Malgorzata Witko, eds. Metal-Ligand Interactions. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0191-5.

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9

Nienhaus, G. Ulrich. Protein-Ligand Interactions. New Jersey: Humana Press, 2005. http://dx.doi.org/10.1385/1592599125.

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10

Daviter, Tina, Christopher M. Johnson, Stephen H. McLaughlin, and Mark A. Williams, eds. Protein-Ligand Interactions. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1197-5.

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11

Protein-ligand interactions: Methods and applications. 2nd ed. New York: Humana Press, 2013.

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12

Press, Humana, ed. Protein-ligand interactions: Methods and applications. Totowa: Humana Press, 2010.

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13

Roque, Ana Cecília A., ed. Ligand-Macromolecular Interactions in Drug Discovery. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-244-5.

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14

Pellizzari, Andrew. Studies into glycolipid receptor-ligand interactions. Ottawa: National Library of Canada, 1992.

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15

Ballante, Flavio, ed. Protein-Ligand Interactions and Drug Design. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1209-5.

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16

NATO ASI/FEBS Course on DNA-Ligand Interactions: From Drugs to Proteins (1986 Abbey of Fontevraud). DNA-ligand interactions: From drugs to proteins. New York: Plenum Press, 1987.

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17

Introduction to biomolecular energetics: Including ligand-receptor interactions. Orlando [Fla.]: Academic Press, 1986.

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18

Russo, Nino, and Dennis R. Salahub, eds. Metal-Ligand Interactions in Chemistry, Physics and Biology. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-011-4245-8.

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19

Russo, Nino. Metal-Ligand Interactions in Chemistry, Physics and Biology. Dordrecht: Springer Netherlands, 2000.

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20

Daëron, M. Techniques d'études des interactions ligands-récepteurs. Paris: Société française d'immunologie, 1989.

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21

Ligand-macromolecular interactions in drug discovery: Methods and protocols. New York: Springer, 2009.

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22

Salahub, Dennis R., and Nino Russo, eds. Metal-Ligand Interactions: From Atoms, to Clusters, to Surfaces. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2822-3.

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23

Asamitsu, Sefan. Development of Selective DNA-Interacting Ligands. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-7716-1.

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24

Martin, Patrick N. Design, synthesis, kinetics and biological evaluation of acridine baseed DNA intercalators. Dublin: University College Dublin, 1996.

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25

Neidle, Stephen. DNA structure and recognition. Oxford, Eng: IRL Press at Oxford University Press, 1994.

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26

Rahman, Masoud. Protein-Nanoparticle Interactions: The Bio-Nano Interface. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013.

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27

Phoenix, Robert Michael. Characterisation of multiple metal ion-ligand interactions of biological significance using diffusion parameters. Wolverhampton: University of Wolverhampton, 1997.

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28

Elbe, Johannes A. Integrin-Ligand Interaction. Springer, 2013.

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29

Eble. Iinegrin-ligand Interaction. Springer-Verlag Telos, 1998.

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30

Elbe, Johannes A. Integrin-Ligand Interaction. Springer, 1997.

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31

1964-, Eble Johannes A., and Kühn Klaus 1927-, eds. Integrin-ligand interaction. New York: Springer, 1997.

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32

Integrin-Ligand Interaction: Special Edition (Molecular biology intellignece unit). R G Landes Co, 1997.

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33

Wang, Bing, Peng Chen, and Jun Zhang. Computational Intelligence in Protein-Ligand Interaction Analysis. Elsevier Science & Technology Books, 2021.

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34

Identification Of Ligand Binding Site And Proteinprotein Interaction Area. Springer, 2012.

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35

Roterman-Konieczna, Irena. Identification of Ligand Binding Site and Protein-Protein Interaction Area. Springer, 2012.

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36

Harlan, John E. Solution structure and function of ligand interaction of prostaglandin H₂ synthase. 1993.

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37

Ren, Ke, and Ronald Dubner. The first crystal structure of an ionotropic glutamate receptor ligand-binding core. Edited by Paul Farquhar-Smith, Pierre Beaulieu, and Sian Jagger. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198834359.003.0032.

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The known functional ionotropic glutamate receptors (iGluRs) are composed of three major subtypes: AMPA, NMDA, and kainate. In 1998, in the landmark paper discussed in this chapter, Armstrong et al. provided the first crystal structure of an iGluR-subunit ligand-binding core, the S1S2 region of the rat GluA2 ‘flop’ isoform. They solved its structure with X-ray crystallography from selenomethonine crystals. They also identified residues involved in kainate binding, analysed allosteric sites that regulate affinity and specificity of the agonist, and mapped potential subunit–subunit interaction sites. They also proposed that binding of different agonists may result in variable degrees of domain closure. This work has profound impact on the field and it has been importantly cited. Subsequently, numerous high-resolution crystal structures of ligand-binding domains of iGluRs in complex with ligands, both agonists and antagonists, have been solved.
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38

Sardinia, Michael Francis. AT₄ receptor binding characteristics: A study of the structural requirements of the angiotensin IV peptide requisite for high affinity, specific ligand-receptor interaction. 1994.

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39

Proteinligand Interactions. Wiley-VCH Verlag GmbH, 2012.

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40

Folkers, Gerd, Raimund Mannhold, Hugo Kubinyi, and Holger Gohlke. Protein-Ligand Interactions. Wiley & Sons, Limited, John, 2012.

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41

DNA-ligand interactions. Plenum published in cooperation with NATO Scientific Affairs Division, 1987.

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42

Folkers, Gerd, Raimund Mannhold, Hugo Kubinyi, and Holger Gohlke. Protein-Ligand Interactions. Wiley & Sons, Incorporated, John, 2012.

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43

W, Celander Daniel, and Abelson John, eds. RNA-ligand interactions. San Diego, CA: Academic Press, 2000.

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44

Folkers, Gerd, Raimund Mannhold, Hugo Kubinyi, and Holger Gohlke. Protein-Ligand Interactions. Wiley & Sons, Incorporated, John, 2012.

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45

Böhm, H. ‐J, and G. Schneider, eds. Protein‐Ligand Interactions. Wiley, 2003. http://dx.doi.org/10.1002/3527601813.

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46

Folkers, Gerd, Raimund Mannhold, Hugo Kubinyi, and Holger Gohlke. Protein-Ligand Interactions. Wiley & Sons, Incorporated, John, 2012.

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47

E, Harding S., and Chowdhry Babur Z, eds. Protein-ligand interactions, structure and spectroscopy: A practical approach. Oxford: Oxford University Press, 2001.

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48

Knaggs, Roger D. The molecular structure of the μ‎-opioid receptor. Edited by Paul Farquhar-Smith, Pierre Beaulieu, and Sian Jagger. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198834359.003.0038.

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The landmark paper discussed in this chapter describes the crystal structure of the μ‎-opioid receptor (also known as MOP-1). Opioids are some of the oldest known drugs and have been used for over 4,000 years; however, in addition to having beneficial analgesic effects, they are associated with a myriad of side effects that can minimize their use. Although the gene sequences of the opioid receptors were determined in the 1990s it has taken much longer to translate this into visualizing their three-dimensional structure. The μ‎-opioid receptor consists of seven transmembrane α‎-helices that are connected by three extracellular loops and three intracellular loops, with a wide open binding pocket which offers many potential ligand interaction sites, and evidence of dimerization. Understanding the crystal structure of the μ‎-opioid receptor in much more detail aids explanation of the molecular determinants of ligand recognition and selectivity and will be of use in designing novel opioids with improved efficacy and fewer side effects.
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49

(Editor), Stephen E. Harding, and Babur Z. Chowdhry (Editor), eds. Protein-Ligand Interactions: A Practical Approach Volume 2: Structure and Spectroscopy (Practical Approach Series). Oxford University Press, USA, 2001.

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50

1938-, Kallenbach Neville R., ed. Chemistry & physics of DNA-ligand interactions. Schenectady, NY: Adenine Press, 1990.

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