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Weiterführende Literatur Zum Lehrbuch „Biochemie“ (Kapitel 4 – 50) Weiterführende Literatur zum Lehrbuch „Biochemie“ (Kapitel 4 – 50) Im Buch ist aus Platzgründen auf die Angabe weiterführender Literatur verzichtet worden. Auskünfte zu den thematischen Schwerpunkten der vier Hauptteile II bis V geben die im Folgenden aufgeführten knapp 1000 einschlägigen Artikel aus wissenschaftlichen Fachzeitschriften. Die Zusammenstellung folgt der Gliederung des Buchs. Jeder Link führt direkt zur Literaturliste des entsprechenden Kapitels, aber es ist stets auch die gesamte Literatur hinterlegt (z.B. für einen kompletten Ausdruck). Die Aufstellung enthält überwiegend Review-Artikel der letzten 4 Jahre, in denen der aktuelle Kenntnisstand zu einem ausgewählten Thema von führenden Wissenschaftlern präsentiert wird. Beim Einführungsteil (Kapitel 1 bis 3) haben wir dagegen bewusst auf Spezialliteratur verzichtet; hier sei auf einschlägige Lehrbücher der Biochemie, Molekularbiologie, Genetik und Zellbiologie, die diesen fundamentalen Aspekten breiten Raum widmen, verwiesen. Falls Sie als Leser interessante Artikel finden, die unsere Literatursammlung ergänzen und bereichern könnten, bitten wir um kurze Mitteilung an den Verlag. Werner Müller-Esterl Ulrich Brandt Oliver Anderka Stefan Kerscher 1 Teil II Struktur und Funktion von Proteinen 4 Proteine – Werkzeuge der Zelle 4.1 Liganden binden an Proteine und verändern deren Konformation Wilson MA, Brunger AT (2000) The 1.0 Å crystal structure of Ca2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity, J Mol Biol 301, 1237-1256 O'Day DH & Myre MA (2004) Calmodulin-binding domains in Alzheimer's disease proteins: extending the calcium hypothesis. Biochemical and Biophysical Research Communications, 320, 1051-1054. 4.2 Enzyme binden Substrate und setzen sie zu Produkten um Showalter AK & Tsai MD (2002) A reexamination of the nucleotide incorporation fidelity of DNA polymerases. Biochemistry, 41, 10571-10576.Johnson KA (2008) Role of induced fit in enzyme specificity: A molecular forward/reverse switch. Journal of Biological Chemistry, 283, 26297-26301. 4.3 Liganden kommunizieren über allosterische Effekte Ridge KD et al (2003) Phototransduction: crystal clear, Trends Biochem Sci 28, 479- 487 Villaverde A (2003) Allosteric enzymes as biosensors for molecular diagnosis. Febs Letters, 554, 169-172. Ascenzi P & Fasano M (2010) Allostery in a monomeric protein: The case of human serum albumin. Biophysical Chemistry, 148, 16-22. 4.4 Die Bindung und Hydrolyse von Nucleotiden steuert Motorproteine Tomkiewicz D, Nouwen N, & Driessen AJM (2007) Pushing, pulling and trapping - Modes of motor protein supported protein translocation. Febs Letters, 581, 2820- 2828. 2 Enernark EJ & Joshua-Tor L (2008) On helicases and other motor proteins. Current Opinion in Structural Biology, 18, 243-257. (PDF) 4.5 Regulatorproteine werden oft über Phosphorylierung gesteuert Johnson LN (2009) The regulation of protein phosphorylation. Biochemical Society Transactions, 037, 627-641. Bradshaw JM (2010) The Src, Syk, and Tec family kinases: Distinct types of molecular switches. Cellular Signalling, 22, 1175-1184. 4.6 Enzyme passen sich metabolischen Bedürfnissen an Roach PJ (2002) Glycogen and its metabolism, Curr Mol Med 2, 101-120 4.7 Proteine können auf mechanische Spannung reagieren Tsunozaki M & Bautista DM (2009) Mammalian somatosensory mechanotransduction. Current Opinion in Neurobiology, 19, 362-369. Arnadottir J & Chalfie M (2010) Eukaryotic Mechanosensitive Channels. Annual Review of Biophysics, Vol 39, 39, 111-137. 3 5 Ebenen der Proteinarchitektur 5.1 Die Proteinstruktur ist hierarchisch gegliedert Liu M, Grigoriev A (2004) Protein domains correlate strongly with exons in multiple eukaryotic genomes - evidence of exon shuffling?, Trends Genet 20, 399-403 Thomas A, Joris B, & Brasseur R (2010) Standardized evaluation of protein stability. Biochimica et Biophysica Acta-Proteins and Proteomics, 1804, 1265-1271. 5.2 Aminosäuren werden zu Polypeptidketten verknüpft Tamura K, Alexander RW (2004) Peptide synthesis through evolution, Cell Mol Life Sci 61, 1317-1330 Rohde H & Seitz O (2010) Ligation-Desulfurization: A Powerful Combination in the Synthesis of Peptides and Glycopeptides. Biopolymers, 94, 551-559. Belousoff MJ, Davidovich C, Zimmerman E, Caspi Y, Wekselman I, Rozenszajn L, Shapira T, Sade-Falk O, Taha L, Bashan A, Weiss MS, & Yonath A (2010) Ancient machinery embedded in the contemporary ribosome. Biochemical Society Transactions, 38, 422-427. 5.3 Polypeptide können nach ihrer Synthese modifiziert werden Jensen ON (2004) Modification-specific proteomics: characterization of post- translational modifications by mass spectrometry, Curr Opin Chem Biol 8, 33-41 Freitas MA, Sklenar AR, & Parthun MR (2004) Application of mass spectrometry to the identification and quantification of histone post-translational modifications. Journal of Cellular Biochemistry, 92, 691-700. (PDF) 5.4 Planare Peptidbindungen bilden das Rückgrat der Proteine Takahashi K, Uchida C, Shin RW, Shimazaki K, & Uchida T (2008) Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease. Cellular and Molecular Life Sciences, 65, 359-375. 4 5.5 Die α-Helix ist ein prominentes Sekundärstrukturelement Chiang D, Joshi AK, & Dill KA (2006) A grammatical theory for the conformational changes of simple helix bundles. Journal of Computational Biology, 13, 21-42. 5.6 β-Faltblätter und β-Schleifen bilden ausgedehnte Sekundärstrukturen Khakshoor O & Nowick JS (2008) Artificial beta-sheets: chemical models of beta- sheets. Current Opinion in Chemical Biology, 12, 722-729. (PDF) 5.7 Sekundärstrukturelemente bilden wiederkehrende Motive Watanabe M, Kobashigawa Y, Aizawa T, Demura M, & Nitta K (2004) A non-native alpha-helix is formed in the beta-sheet region of the molten globule state of canine milk lysozyme. Protein Journal, 23, 335-342. 5.8 Nichtkovalente Wechselwirkungen stabilisieren die Tertiärstruktur Boas FE & Harbury PB (2007) Potential energy functions for protein design. Current Opinion in Structural Biology, 17, 199-204. 5.9 Globuläre Proteine falten sich zu kompakten Strukturen Frauenfelder H et al (2003) Myoglobin: the hydrogen atom of biology and a paradigm of complexity, Proc Natl Acad Sci U S A 100, 8615-8617. (PDF) Elber R (2010) Ligand diffusion in globins: simulations versus experiment. Current Opinion in Structural Biology, 20, 162-167. 5.10 Mehrere Untereinheiten bilden die Quartärstruktur der Proteine Brinda KV, Surolia A, & Vishveshwara S (2005) Insights into the quaternary association of proteins through structure graphs: a case study of lectins. Biochemical Journal, 391, 1-15. (PDF) Rosenzweig R & Glickman MH (2008) Chaperone-driven proteasome assembly. Biochemical Society Transactions, 36, 807-812. 5 5.11 Proteine falten schrittweise in ihre native Konformation Dobson CM (2003) Protein folding and misfolding, Nature 426, 884-890 Foguel B & Silva JL (2004) New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies. Biochemistry, 43, 11361-11370. Ito K & Inaba K (2008) The disulfide bond formation (Dsb) system. Current Opinion in Structural Biology, 18, 450-458. Bandopadhyay R & de Belleroche J (2010) Pathogenesis of Parkinson's disease: emerging role of molecular chaperones. Trends in Molecular Medicine, 16, 27-36. 5.12 Proteine können reversibel denaturieren May BC et al (2004) Prions: so many fibers, so little infectivity, Trends Biochem Sci 29, 162-165 Oberhauser AF & Carrion-Vazquez M (2008) Mechanical biochemistry of proteins one molecule at a time. Journal of Biological Chemistry, 283, 6617-6621. (PDF) Perrin RJ, Fagan AM, & Holtzman DM (2009) Multimodal techniques for diagnosis and prognosis of Alzheimer's disease. Nature, 461, 916-922. 5.13 Proteine können maßgeschneidert werden Georlette D et al (2004) Some like it cold: biocatalysis at low temperatures, FEMS Microbiol Rev 28, 25-42 Tian J & Xie ZJ (2008) The Na-K-ATPase and calcium-signaling microdomains. Physiology, 23, 205-211. (PDF) Wang HX, Nakata E, & Hamachi I (2009) Recent Progress in Strategies for the Creation of Protein-Based Fluorescent Biosensors. Chembiochem, 10, 2560-2577. Omenetto FG & Kaplan DL (2010) New Opportunities for an Ancient Material. Science, 329, 528-531. Cartellieri M, Bachmann M, Feldmann A, Bippes C, Stamova S, Wehner R, Temme A, & Schmitz M (2010) Chimeric Antigen Receptor-Engineered T Cells for Immunotherapy of Cancer. Journal of Biomedicine and Biotechnology. (PDF) 6 6 Proteine auf dem Prüfstand 6.1 Proteine müssen für die Aufreinigung in wässriger Lösung vorliegen Bowie JU (2001) Stabilizing membrane proteins, Curr Opin Struct Biol 11, 397-402 Seddon AM, Curnow P, & Booth PJ (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochimica et Biophysica Acta-Biomembranes, 1666, 105-117. 6.2 Die Gelfiltrationschromatographie trennt Proteine nach ihrer Größe Winzor DJ (2003) The development of chromatography for the characterization of protein interactions: a personal perspective, Biochem Soc Trans 31, 1010-1014 Berek D (2010) Size exclusion chromatography - A blessing and a curse of science and technology of synthetic polymers. Journal of Separation Science, 33, 315-335. 6.3 Die Ionenaustauschchromatographie trennt Proteine unterschiedlicher Ladung Stahlberg J (1999) Retention models for ions in chromatography, J Chromatogr A 855, 3-55 Jungbauer A & Hahn R (2009) Ion-Exchange Chromatography. Guide
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