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Institut für Molekular- und Zellphysiologie



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Bibliothek der Medizinischen Hochschule Hannover


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2014

  • Transport and Diffusion of Tau protein in neurons., Scholz, T. und Mandelkow, E. Cell Mol Life Sci. 2014 Aug; 71(16):3139-50. doi: 10.1007/s00018-014-1610-7. Epub 2014 Apr 1. [Pubmed Link]
  • ATP turnover by individual myosin molecules hints at two conformers of the myosin active site., Amrute-Nayak M1, Lambeck KA, Radocaj A, Huhnt HE, Scholz T, Hahn N, Tsiavaliaris G, Walter WJ, Brenner B., Proc Natl Acad Sci U S A. 2014 Feb 18;111(7):2536-41. doi: 10.1073/pnas.1316390111. Epub 2014 Feb 3., [PubMed - as supplied by publisher]
  • Molecular mechanism regulating myosin and cardiac functions by ELC., Lossie J, Köhncke C, Mahmoodzadeh S, Steffen W, Canepari M, Maffei M, Taube M, Larchevêque O, Baumert P, Haase H, Bottinelli R, Regitz-Zagrosek V, Morano I., Biochem Biophys Res Commun. 2014 Jul 18;450(1):464-9. doi: 10.1016/j.bbrc.2014.05.142. Epub 2014 Jun 6., PMID: 24911555 [Pubmed Link]
  • Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules: TEKTINS, Ca2+-BINDING PROTEINS, AND STABLE PROTOFILAMENTS., Linck R, Fu X, Lin J, Ouch C, Schefter A, Steffen W, Warren P, Nicastro D., J Biol Chem. 2014 Jun 20;289(25):17427-44. doi: 10.1074/jbc.M114.568949. Epub 2014 May 2., PMID: 24794867, [Pubmed Link]
  • Faster cross-bridge detachment and increased tension cost in human hypertrophic cardiomyopathy with the R403Q MYH7 mutation., Witjas-Paalberends ER, Ferrara C, Scellini B, Piroddi N, Montag J, Tesi C, Stienen GJ, Michels M, Ho CY, Kraft T, Poggesi C, van der Velden J., J Physiol. 2014 Aug 1;592(Pt 15):3257-72. doi: 10.1113/jphysiol.2014.274571. Epub 2014 Jun 13., PMID: 24928957, [Pubmed Link]

2013

  • Familial hypertrophic cardiomyopathy: Functional effects of myosin mutation R723G in cardiomyocytes., Kraft T, Paalberends ER, Boontje NM, Tripathi S, Brandis A, Montag J, Hodgkinson JL, Francino A, Navarro-Lopez F, Brenner B, Stienen GJ, van der Velden J., J Mol Cell Cardiol. 2013 Jan 11. doi:pii: S0022-2828(13)00004-7. 10.1016/j.yjmcc.2013.01.001. [Epub ahead of print]
  • PMID: 23318932, [PubMed - as supplied by publisher]

  • MAPKAPK2/3 Regulate SERCA2a Expression and Fiber Type Composition to Modulate Skeletal Muscle and Cardiomyocyte Function., Scharf M, Neef S, Freund R, Geers-Knörr C, Franz-Wachtel M, Brandis A, Krone D, Schneider H, Groos S, Menon MB, Chang KC, Kraft T, Meissner JD, Boheler KR, Maier LS, Gaestel M, Scheibe RJ. Mol Cell Biol. 2013 Apr 22. [Epub ahead of print], PMID: 23608535 [PubMed - as supplied by publisher]


  • Lipoteichoic acid from Staphylococcus aureus directly affects cardiomyocyte contractility and calcium transients. Mutig, N., Geers-Knoerr, C., Piep, B., Pahuja, A., Vogt, P.M., Brenner, B., Niederbichler, A.D., Kraft, T., Mol Immunol 56 (4): 720–728 (2013). doi: 10.1016/j.molimm.2013.07.007.

2012

  • Kinetic Mechanism of Ca(2+)-controlled Changes of Skeletal Troponin I in Psoas Myofibrils. Lopez-Davila AJ, Elhamine F, Ruess DF, Papadopoulos S, Iorga B, Kulozik FP, Zittrich S, Solzin J, Pfitzer G, Stehle R. Biophys J. 2012 Sep 19;103(6):1254-64. doi: 10.1016/j.bpj.2012.08.022. PMID: 22995498 [PubMed]


  • ATP binding and cross-bridge detachment steps during full Ca² activation: comparison of myofibril and muscle fibre mechanics by sinusoidal analysis. Iorga B, Wang L, Stehle R, Pfitzer G, Kawai M. J Physiol. 2012 Jul 15;590(Pt 14):3361-73. Epub 2012 May 14. PMID: 22586213 [PubMed]


  • Tau protein diffuses along the microtubule lattice., Hinrichs, M.H., Jalal, A., Brenner, B., Mandelkow, E., Kumar, S. und Scholz, T. (2012) J Biol Chem. 287, 38559-68. Epub 2012 Sep 27, 2012 as doi:10.1074/jbc.M112.369785


  • Polarisationserhaltene Faseroptik für die Fluoreszenzmikroskopie. Laser+Photonik. Krischke, A., Oechsner, U., Knothe, C., Brenner, B., und Scholz, T. 2012. 5/2012, 38-41


  • Mechanical and kinetic properties of β-cardiac/slow skeletal muscle myosin, Brenner, B., Hahn, N., Hanke, E., Martinmehr, F., Scholz, T., Steffen, W. und Kraft, T. J Muscle Res Cell Motility. published July 31, 2012 as doi:10.1007/s10974-012-9315-8


  • Two independent switches regulate cytoplasmic dynein’s processivity and directionality, Wilhelm J. Walter, Michael P. Koonce, Bernhard Brenner, and Walter Steffen Link PNAS 12. March 2012, PMID: 22411823


  • RGBV-Faseroptik für TIRF-Mikroskopie und Biophotonik. BioPhotonik. Krischke, A., Oechsner, U., Knothe, C., Federau, G., Brenner, B., und Scholz, T. 2012. 1/2012, 22-26, Link (778 KB)


  • SERCA2a gene therapy restores microRNA-1 expression in heart failure via an Akt/FoxO3A-dependent pathway Regalla Kumarswamy, Alexander R. Lyon, Ingo Volkmann, Adam M. Mills, Julia Bretthauer, Aanchal Pahuja, Cornelia Geers-Knörr, Theresia Kraft, Roger J. Hajjar, Kenneth T. Macleod, Sian E. Harding and Thomas Thum, European Heart Journal Advance Access published February 23, 2012 Link

    Presseinformation MHH 05.03.2012


  • Effects of Basic Calponin on the Flexural Mechanics and Stability of F-Actin. Cytoskeleton Jensen,M.H. Watt, J., Hodgkinson, J.L., Gallant, G. Appel,S., El-Mezgueldi, M., Angelini, T.E., Morgan, K.G.,Lehman, W. and Moore, J.R. (2012).

2011

  • Processive behaviour of kinesin observed using micro-fabricated cantilevers. Nanotechnology. Scholz, T., Vicary, J.A., Jeppesen, G.M., Ulcinas, A., Hörber, J.K.H. und Antognozzi, M., 2011 22,095707. Epub 2011 Jan 27. Nanotechnology. 2011 Mar 4;22(9):095707. Epub 2011 Jan 27. PMID: 21270491 PubMed

  • Myosin-1C associates with microtubules and stabilizes the mitotic spindle during cell division. J Cell Sci. 2011 Jun 28. [Epub ahead of print]. PubMed (*equal contribution), Rump, A.*, Scholz, T.*, Thiel, C., Hartmann, F.K., Uta, P., Hinrichs, M.H., Taft, M.H., Tsiavaliaris, G. (2011)


  • Unequal allelic expression of wild-type and mutated β-myosin in familial hypertrophic cardiomyopathy. Tripathi S, Schultz I, Becker E, Montag J, Borchert B, Francino A, Navarro-Lopez F, Perrot A, Özcelik C, Osterziel KJ, McKenna WJ, Brenner B, Kraft T. Basic Res Cardiol. 2011 Nov;106(6):1041-55. Epub 2011 Jul 19. PMID: 21769673, [PubMed - in process] , Free PMC Article

2010

  • A common MLP (muscle LIM protein) variant is associated with cardiomyopathy. Knöll R, Kostin S, Klede S, Savvatis K, Klinge L, Stehle I, Gunkel S, Kötter S, Babicz K, Sohns M, Miocic S, Didié M, Knöll G, Zimmermann WH, Thelen P, Bickeböller H, Maier LS, Schaper W, Schaper J, Kraft T, Tschöpe C, Linke WA, Chien KR. Circ Res. 2010 Mar 5;106(4):695-704. Epub 2009 Dec 31. PubMed Link


  • Targeted optimization of a protein nanomachine for operation in biohybrid devices. Amrute-Nayak M, Diensthuber RP, Steffen W, Kathmann D, Hartmann FK, Fedorov R, Urbanke C, Manstein DJ, Brenner B, Tsiavaliaris G. Angew Chem Int Ed Engl. 2010;49(2):312-6. PubMed Link


  • The left and right ventricle of a patient with a R723G mutation of the beta-myosin heavy chain and severe hypertrophic cardiomyopathy show no differences in the expression of myosin mRNA., Borchert B, Tripathi S, Francino A, Navarro-Lopez F, Kraft T. Cardiol J. 2010;17(5):518-22. PubMed Link


  • Burn-induced organ dysfunction: vagus nerve stimulation improves cardiac function. Niederbichler AD, Papst S, Claassen L, Jokuszies A, Ipaktchi K, Reimers K, Hirsch T, Steinstraesser L, Kraft T, Vogt PM. Eplasty. 2010 Jun 21;10:e45., PubMed Link


  • Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. Radtke K, Kieneke D, Wolfstein A, Michael K, Steffen W, Scholz T, Karger A, Sodeik B. PLoS Pathog. 2010 Jul 8;6(7):e1000991.PubMed Link


  • Structure of the hDmc1-ssDNA Filament Reveals the Principles of Its Architecture. Okorokov, A.L, Chaban, Y.L., Bugreev, D.V., Hodgkinson, J., Mazin, A.V., Orlova, E.V. (2010). PloS one, 5 , Issue 1, e8586, 1-14. Link

2009

  • W. Bintig, J. Baumgart, W. J. Walter, A. Heisterkamp, H. Lubatschowski, and A. Ngezahayo, Purinergic signalling in rat GFSHR-17 granulosa cells: an in vitro model of granulosa cells in maturing follicles,  Journal of Bioenergetics and Biomembranes (2009 Feb 4) (in press) PubMed Link


  • Radocaj A, Weiss T, Helsby WI, Brenner B, Kraft T., Force-Generating Cross-Bridges during Ramp-Shaped Releases: Evidence for a New Structural State, Biophys J. 2009 Feb 18;96(4):1430-1446, PubMed Link

  • Hodgkinson JL, Horsley A, Stabat D, Simon M, Johnson S, da Fonseca PC, Morris EP, Wall JS, Lea SM, Blocker AJ., Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. Nat Struct Mol Biol. 2009 May;16(5):477-85. Epub 2009 Apr 26. PMID: 19396171

  • White HE, Hodgkinson JL, Jahn TR, Cohen-Krausz S, Gosal WS, Müller S, Orlova EV, Radford SE, Saibil HR., Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils. J Mol Biol. 2009 May 29;389(1):48-57. Epub 2009 Apr 5. PMID: 19345691

  • Seebohm,B., Matinmehr,F., Köhler,J., Francino, A., Navarro-Lopez, F., Perrot, A., Özcelik, C., McKenna, W.J., Brenner, B., Kraft, T., Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance. Biophys J. 2009 Aug 5;97(3):806-24, PMID: 19651039

  • Niederbichler AD, Papst S, Claassen L, Jokuszies A, Steinstraesser L, Hirsch T, Altintas MA, Ipaktchi KR, Reimers K, Kraft T, Vogt PM., Burn-induced organ dysfunction: Vagus nerve stimulation attenuates organ and serum cytokine levels. Burns. 2009 May 29.Sep;35(6):783-9. Epub 2009 May 30.

  • Fedorov, R., Böhl, M., Tsiavaliaris, G., Hartmann, F.K., Taft, M.H., Baruch, P., Brenner, B., Martin, R., Knölker, H.-J., Gutzeit, H.O., Manstein, D.J., The mechanism of pentabromopseudilin inhibition of myosin motor activity. Nat. Struc. Mol. Biol. 2009 16:80-88

  • Walter WJ, Brenner B, Steffen W., Cytoplasmic dynein is not a conventional processive motor. J Struct Biol. 2010 May;170(2):266-9. Epub 2009 Dec 2.

2008

  • Phosphorylation in C-Terminus of the Rat Connexin46 (rCx46) and Regulaton of the Conducting Activity of the Formed Connexons W. J. Walter, C. Zeilinger, W. Bintig, H.-A. Kolb, and A. Ngezahayo Journal of Bioenergetics and Biomembranes

  • What's the point of the T3SS needle? Blocker, A.J., Deane, J.E., Veenendaal, A.K.J., Roversi, P., Hodgkinson, J.L., Johnson, S. and Lea, S.M. (2008). Proc. Natl. Acad. Sci. USA. 105, 6507-13

2007

  • Quantification of Mutant versus Wild-Type Myosin in Human Muscle Biopsies Using Nano-LC/ESI-MS, Edgar Becker, Francisco Navarro-López, Antonio Francino, Bernhard Brenner and Theresia Kraft, Anal. Chem. 2007, 79,9531-9538 pdf-download

  • Inorganic phosphate binds to the empty nucleotide binding pocket of conventional myosin II, Mamta Amrute-Nayak, Massimo Antognozzi1, Tim Scholz, Hiroaki Kojima, and Bernhard Brenner, J Biol Chem. 2008 Feb 15;283(7):3773-81. Epub 2007 Dec 12.pdf-download

  • A microtubule-based, dynein-dependent force induces local cell protrusions: Implications for neurite initiation. Dehmelt L, Nalbant P, Steffen W, Halpain S., Brain Cell Biol. 2007 Feb;35(1):39-56. Epub 2007 Mar 13. PMID: 17940912 [Abstract PubMed]

  • Single Molecule Measurement of the Stiffness of the Rigor Myosin Head. Lewalle A, Steffen W, Stephenson O, Ouyang Z, Sleep J., Biophys J. 2007 Dec 7; [Epub ahead of print], PMID: 18065470 [Pubmed Abstruct]

2006

  • Brenner B. The stroke size of myosins: a reevaluation. J Muscle Res Cell Motil. 2006; 27:173-87. Abstract

  • Kopp P, Lammers R, Aepfelbacher M, Woehlke G, Rudel T, Machuy N, Steffen W, Linder S. The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages. Mol Biol Cell 2006; 17:2811-23. 2006. Abstract

  • Setter PW, Malvey-Dorn E, Steffen W, Stephens RE, Linck RW. Tektin interactions and a model for molecular functions. Exp Cell Res 2006; 312:2880-96 Abstract

  • Schramm B, de Haan CA, Young J, Doglio L, Schleich S, Reese C, Popov A, Steffen W, Schroer T, Krijnse-Locker J. Vaccinia-Virus-Induced Cellular Contractility Facilitates the Subcellular Localization of the Viral Replication Sites. Traffic 2006; 7:1352-67 Abstract

    Buchbeiträge

  • Hodgkinson JL, Steffen W. Direct labeling of components in protein complexes by immuno-electron microscopy. In: Celis JE, editor. Cell Biology & Laboratory Handbook, 3rd edition. Academic Press; 2006. Vol. 3, p. 307-12 Abstract

  • Steffen W, Lewalle A, Sleep J. Optical Tweezers: Application to the study of motor proteins. In: Celis JE, editor. Cell Biology & Laboratory Handbook, 3rd edition. Academic Press; 2006. Vol. 3, p. 37-45


2005

  • Becker, N.B., Altmann, S.M., Scholz, T ., Hörber, J.K.H., Stelzer, E.H.K. und Rohrbach, A. Three-dimensional bead position histograms reveal single-molecule nanomechanics. Physical Review E. 71 (2PT 1):021907.(2005) Abstract
  • Brenner B, Mählmann E, Mattei T, Kraft T. Driving filament sliding: weak binding cross-bridge states, strong binding cross-bridge states, and the power stroke. Adv Exp Med Biol 2005; 565:75-91 Abstract
  • Heineke J, Ruetten H, Willenbockel C, Gross SC, Naguib M, Schaefer A, Kempf T, Hilfiker-Kleiner D, Caroni P, Kraft T, Kaiser RA, Molkentin JD, Drexler H, and Wollert KC. Attenuation of cardiac remodeling after myocardial infarction by muscle LIM protein-calcineurin signaling at the sarcomeric Z-disc. Proc Natl Acad Sci U S A. 2005;102:1655-60. Epub 2005 Jan 21. Abstract
  • Kirschner S.E., Becker E., Antognozzi M., Kubis H.-P., Francino A., Navarro-López F., Bit-Avagim N., Perrot A., Mirrakhimov M. M., Osterziel K.-J. , McKenna W.J., Brenner B., Kraft T. , Hypertrophic cardiomyopathy-related ß-myosin mutations cause highly variable calcium sensitivity with functional imbalances among individual muscle cells. Am J. Physiol. Heart Circ. Physiol. 288: 2005 (in press) toll-free link
  • Kraft T, Mählmann E, Mattei T, Brenner B. Initiation of the power stroke in muscle: insights from the phosphate analog AlF4. Proc Natl Acad Sci U S A. 2005, 102:13861-6. Epub 2005 Sep 20. Abstract
  • Scholz, T., Altmann, S.M., Antognozzi, M., Tischer, C., Hörber, J.K.H. und Brenner, B. Mechanical properties of single myosin molecules probed with the Photonic Force Microscope. Biophys J. 2005; 88(1):360-371. Abstract

    Buchbeiträge
  • Brenner B. Muskulatur. In: Klinke R, Pape HC, Silbernagl S. Physiologie. 5. Auflage. Stuttgart: Thieme Verlag; 2005.
  • Korbmacher C, Greger R, Brenner B, Silbernagl S. Zelluläre Motilität. In: Klinke R, Pape HC, Silbernagl S. Physiologie. 5. Auflage. Stuttgart: Thieme Verlag; 2005.


2004
  • Gafurov B, Fredricksen S, Cai A, Brenner B, Chase PB, Chalovich JM. The Delta14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin. Biochemistry 2004; 43:15276-85. Medline
  • Tongers J, Fiedler B, Konig D, Kempf T, Klein G, Heineke J, Kraft T, Gambaryan S, Lohmann SM, Drexler H, Wollert KC. Heme oxygenase-1 inhibition of MAP kinases, calcineurin/NFAT signaling, and hypertrophy in cardiac myocytes. Cardiovasc Res. 2004; 63:545-52. Medline


2003
  • Claus P, Doring F, Gringel S, Muller-Ostermeyer F, Fuhlrott J, Kraft T , Grothe C. Differential intranuclear localization of fibroblast growth factor-2 isoforms and specific interaction with the survival of motoneuron protein. J Biol Chem 2003; 278:479-85. Abstract
  • Heineke J, Kempf T, Kraft T , Hilfiker A, Morawietz H, Scheubel RJ, Caroni P, Lohmann SM, Drexler H, Wollert KC. Downregulation of cytoskeletal muscle LIM protein by nitric oxide: impact on cardiac myocyte hypertrophy. Circulation 2003;107:1424-32. Abstract
  • Köhler D, Ruff C, Meyhöfer E, Bähler M. Different degrees of lever arm rotation control myosin step size. J Cell Biol. 2003;161:237-241. Abstract
  • Köhler J, Chen Y, Brenner B, Gordon AM, Kraft T , Martyn DA, Regnier M, Rivera AJ, Wang C-K, Chase PB. Familial hypertrophic cardiomyopathy mutations in troponin I (K183., G203S, K206Q) enhance filament sliding. Physiol. Genomics 2003;14:117-28. Abstract
  • Lakämper S, Kallipolitou A, Woehlke G, Schliwa M, Meyhöfer E. Single Fungal Kinesin Motor Molecules Move Processively along Microtubules. Biophys J. 2003; 84:1833-43. Abstract
  • Scholz T, Brenner B. Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform. J Muscle Res Cell Motil 2003; 24:77-86. Abstract


2002
  • Herm-Gotz A, Weiss S, Stratmann R, Fujita-Becker S, Ruff C, Meyhöfer E, Soldati T, Manstein DJ, Geeves MA, Soldati D. Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. EMBO J. 2002; 21:2149-58. Abstract
  • Kofidis T., Akhyari P., Boublik J., Theodorou P., Martin U., Ruhparwar A., Fischer S., Eschenhagen T., Kubis HP., Kraft T ., Leyh R., Haverich A.: In vitro engineering of heart muscle: artificial myocardial tissue. J. Thorac. Cardiovasc. Surg. 124(1):63-9 (2002). Abstract
  • Köhler J, Winkler G, Schulte I, Scholz T, McKenna W, Brenner B, Kraft T . Mutation of the myosin converter domain alters cross-bridge elasticity. Proc Natl Acad Sci USA 2002; 99:3557-62. Abstruct
  • Kraft, T., Mattei, T., Radocaj, A., Piep, B., Nocula, Ch., Furch, M., and Brenner, B.: Structural features of cross-bridges in isometrically contracting skeletal muscle. Biophys. J. 82(5):2536-47 (2002). Abstract


2001
  • Chen, Y., Yan, B., Chalovich, J.M., and Brenner, B .: Theoretical Kinetic Studies of Models for Binding Myosin Subfragment-1 to Regulated Actin: Hill Model versus Geeves Model. Biophys. J. 80, 2338-2349 (2001). Abstract
  • Kallipolitou A, Deluca D, Majdic U, Lakämper S, Cross R, Meyhöfer E, Moroder L, Schliwa M, Woehlke G. Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa. EMBO J. 2001; 20:6226-35. Abstract
  • Ruff, C., Furch, M., Brenner, B ., Manstein, D., and Meyhöfer, E.: Single-molecule tracking of myosins with genetically engineered amplifier domains. Nature Struc. Biol. 8, 226-229 (2001). Abstract

    Lehrbuchkapitel:
  • Rüdel R, Brenner B. Muskeln und Motilität. In: Dudel, Menzel, Schmidt editors. Neurowissenschaft; vom Molekül zur Kognition. 2nd ed. Berlin, Heidelberg: Springer; 2001. p. 145-166


2000
  • Becker, M. H., Wermter, T. B., Brenner, B ., Walter, G.F., and Berger, A.: Comparison of clinical performance, histology and single-fiber contractility in free neurovascular muscle flaps. J Reconstr. Microsurg. Oct;16(7):525-34.(2000) Abstract
  • Kraft, T., Hornemann, T., Stolz, M., Nier, V., and Wallimann, T.: Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ . J. Muscle Res. Cell Motil. 21, 691-703 (2000). Abstract
  • Stehle, R., and Brenner, B .: Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle. Implications for cross-bridge action during maximum velocity of filament sliding. Biophys. J. 78, 1458-1473 (2000). Abstract


1999
  • Brenner, B. and Chalovich, J.M.: Kinetics of Thin Filament Activation Probed by Fluorescence of N-((2-Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz- 2-oxa-1,3-diazole-labelled Troponin I Incorporated in Skinned Fibers of Rabbit Psoas Muscle. Implications for Regulation of Muscle Contraction. Biophys. J. 77, 2692-2708 (1999). Abstract
  • Brenner, B., Kraft, T., Yu, L.C., and Chalovich, J.M.: Thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole -labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Biophys. J. 77, 2677-2691 (1999). Abstract
  • Frisbie, S.M., Reedy, M.C., Yu, L.C., Brenner, B ., Chalovich, J.M., and Kraft, T .: Sarcomeric binding pattern of exogenously added intact caldesmon its C-terminal 20kDa fragment in skinned fibers of skeletal muscle. J. Muscle Res. Cell Motil. 20, 291-303 (1999).
  • Kraft, T., Xu, S., Brenner, B., and Yu, L.C.: The effect of thin filament activation on the attachment of weak binding cross-bridges: A 2D-Xray-diffraction study on single muscle fibers. Biophys. J. 76, 1494-1513 (1999). Abstract
  • Nier, V., Schultz, I., Brenner, B ., Forssmann, W.-G., and Raida, M.: Variability in the ratio of mutant to wildtype myosin heavy chain present in the soleus muscle of patients with familial hypertrophic cardiomyopathy. A new approach for the quantification of mutant to wildtype protein. FEBS Letters, 461, 246-252 (1999). Abstract
  • Tasche, C., Meyhöfer, E., and Brenner, B .: A force transducer to measure the mechanical properties of single cardiac myocytes. Am J. Physiol.-Heart and Circ. Physiol. 277, H2400-H2408 (1999). Abstract
  • Thedinga, E., Karim, N., Kraft. T., and Brenner, B .: A single-fiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers. J. Muscle Res. Cell Motil. 20, 785-796 (1999). Abstract


1998
  • Brenner, B.: Muscle Mechanics II: skinned muscle fibres. In: Current Methods in Muscle Physiology (H. Sugi, ed.) Oxford Univ. Press, pp. 33-69 (1998).
  • Brenner, B., Kraft, T., and Chalovich, J.M.: Fluorescence of NBD-labeled troponin-I as a probe for the kinetics of thin filament activation in skeletal muscle fibers. Adv. Exp. Med. Mol. Biol. 453, 177-185 (1998).
  • Kraft, T., Mattei, T., Brenner, B.: Structural features of force-generating cross-bridges: A 2D-X-ray diffraction study. Adv. Exp. Med. Biol. 289-296 (1998). Abstract
  • Stolz, M., Kraft, T ., Wallimann, T.: The isoenzyme-diagnostic regions of muscle-type creatine kinase, the M-260 and M-300 box. are not responsible for its binding to the myofibrillar M-band. Eur. J. Cell Biol. 77, 1-9 (1998). Abstract
  • Wallimann, T., Dolder, M., Schlattner, U., Eder, M., Hornemann, T., Kraft, T ., Stolz, M.: Creatine kinase: An enzyme with a central role in cellular energy metabolism. Magentic Resonance Materials in Physics, Biology and Medicine 6, 116-119 (1998). Medline-Link
  • Xu, S., Malinchik, S., Frisbie, S., Gu, J., Kraft, T ., Rapp, G., Chalovich, J.M., Brenner, B ., and Yu, L.C.: X-ray diffraction studies of the cross-bridge intermediate states. Adv. Exp. Med. Mol. Biol. 453, 271-277 (1998). Abstract


1997
  • Frisbie, S.M., Chalovich, J.M., Brenner, B ., Yu, L.C.: Modulation of cross-bridge affinity for MgGTP by Ca 2+ in skinned fibers of rabbit psoas muscle. Biophys. J. 72, 2255-2261 (1997). Abstract
  • Heubach, J.F., Hartwell, R., Ledwon, M., Kraft, T., Brenner, B ., Chalovich, J.M.: Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers. Biophys. J. 72, 1287-1294 (1997). Abstract
  • Kraft, T., Brenner, B.: Force enhancement without changes in cross-bridge turnover kinetics: the effect of EMD 57033. Biophys. J. 72, 272-282 (1997). Abstract
  • Xu, S., Malinchik, S., Gilroy, D., Kraft, Th., Brenner, B ., and Yu, L.C.: X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle. Biophys. J. 72, 2292-2303 (1997). Abstract


1996
  • Brenner, B., Kraft, T., DasGupta, G., Reisler, E.: Effect of antibody fragments against the N-terminus of actin on cross-bridge binding to actin and force generation in skinned fibers of the rabbit psoas muscle. Biophys. J. 70, 48-56 (1996).
  • Brenner, B., Xu, S., Chalovich, J.M., Yu, L.C.: Radial equilibrium lengths of acto-myosin cross-bridges in muscle. Biophys. J. 71, 2751-2758 (1996).


1995
  • Brenner, B., Chalovich, J.M., Yu, L.C.: Distinct molecular processes associated with isometric force generation and with rapid tension recovery after quick release. Biophys. J. 68, 106s-111s (1995). Abstract
  • Kraft, T., Chalovich, J.M., Yu, L.C., Brenner, B.: Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological temperature and ionic strength conditions. Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophys. J. 68, 2404-2418 (1995). Abstract
  • Kraft, T., Messerli, B. Rothen-Rutishauser, B., Perriard, J.-C., Wallimann, T., Brenner, B.: Equilibration and exchange of fluorescently labelled molecules in skinned skeletal muscle fibers visualized by confocal microscopy. Biophys. J., 69, 1246-1258 (1995).
  • Kraft, T., Messerli, M., Rutishauser, B., Wallimann, T., Perriard, J.C., Chalovich, J.M., and Brenner, B.: Equilibration of fluorescently labelled molecules in skeletal muscle fibers studied using confocal microscopy. Biophys. J. 68, 371s (1995).


1993
  • Brenner, B.: Dynamic actin interaction of cross-bridges during force generation. Implications for cross-bridge action in muscle. Adv. Exp. Med. Biol. 332, 531-542 (1993). Abstract
  • Brenner, B.: Mechanisms of changes in calcium sensitivity at the cross-bridge level. In: Modulation of Cardiac Calcium Sensitivity: A New Approach to Increasing the Strength of the Heart. J.A. Lee & D.G. Allen (eds.), Oxford University Press (1993).
  • Brenner, B., Yu, L.C.: Evidence for structural changes in cross-bridges during force generation. Adv. Exp. Med. Biol. 332, 461-467 (1993).
  • Brenner, B., Yu, L.C.: Structural changes in the actomyosin cross-bridges associated with force generation. Proc. Natl. Acad. Sci. USA 90, 5252-5256 (1993). Abstract
  • Chen, Y., Brenner, B .: On the regeneration of the actin-myosin power stroke in contracting muscle. Proc. Natl. Acad. Sci. USA 90, 5148-5152 (1993). Abstract
  • Xu, S., Brenner, B ., Yu, L.C.: State-dependent radial elasticity of attached cross-bridges in single skinned fibres of rabbit psoas muscle. J. Physiol. (Lond.) 461, 283-299 (1993). Abstract


1992
  • Kraft, Th., Yu, L.C., Kuhn, H.J., Brenner, B.: Effect of Ca 2+ on weak cross-bridge interaction with actin in the presence of the nucleotide analog ATP, S. Proc. Natl. Acad. Sci. USA 89, 11362-11366 (1992). Abstract


1991
  • Brenner, B.: Dynamic dissociation and reassociation of actomyosin cross-bridges during force-generation. A newly observed facet of cross-bridge action in muscle. Proc. Natl. Acad. Sci. USA 88, 10490-10494 (1991).
  • Brenner, B.: Dynamic actin interaction of cross-bridges. A general principle and its implications for cross-bridge action in muscle. Adv. Biophys. 27, 259-269 (1991).
  • Brenner, B.: A new concept for the mechanism of Ca 2+ -regulation of muscle contraction. Implications for physiological and pharmacological approaches to modulate contractile function of myocardium. Basic Res. Cardiol. 86,3, 83-92 (1991). Abstract
  • Brenner, B., Yu. L.C.: Characterization of radial force and radial stiffness in Ca 2+ -activated skinned fibres of the rabbit psoas muscle. J. Physiol. (Lond.) 441, 703-718 (1991).
  • Brenner, B., Yu, L.C., Chalovich, J.M.: Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon. Implications for the pathway to force generation. Proc. Natl. Acad. Sci. USA 88, 5739-5743 (1991). Abstract
  • Chalovich, J.M., Yu, L.C., Brenner, B .: Involvement of weak-binding cross-bridges in force production in muscle. J. Muscle Res. Cell Motil. 12, 503-506 (1991).
  • Chalovich, J.M., Yu, L.C., Velaz, L., Kraft, T., Brenner, B .: Caldesmon derived polypeptides as probes of force production in skeletal muscle. In: Peptides as Probes in Muscle Research, J.C. Rüegg (ed.) Springer, pp. 81-94 (1991).
  • Kraft, T., Rommel, U., Trayer, I.P., Brenner, B.: Interference of myosin peptides with weak and strong actin interaction of cross-bridges in skeletal muscle fibers. I: Peptides as Probes in Muscle Research, J.C. Rüegg (ed.) Springer, pp. 69-80 (1991).
  • Squire, J.M., Podolsky, R.J., Barry, J.S., Yu, L.C., Brenner, B .: X-ray diffraction testing for weak-binding cross-bridges in relaxed bony fish muscle fibres at low ionic strength. J. Struct. Biol. 107, 221-226 (1991).


1990
  • Brenner, B.: Muscle mechanics and biochemical kinetics. In: Molecular Mechanism of Muscular Contraction. John Squire (ed.), Macmillan Press Ltd. pp. 77-149 (1990).


1989-1979
  • Yu, L.C., and Brenner, B .: Structures of actomyosin crossbridges in relaxed and rigor muscle fibers. Biophys. J. 55, 441-453 (1989). Abstract
  • Brenner, B.: Effect of Ca 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA 85, 3265-3269 (1988). Medline Link
  • Tutschke, U.: A new photoelectric device for contact-free recording of diameters of short blood vessel segments in vitro . Biomed. Tech. 33, 7-8, 166-172 (1988). Medline-Link
  • Brenner, B.: Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution. Ann. Rev. Physiol. 49, 655-675 (1987). Medline Link
  • Brenner, B. and Eisenberg, E.: The mechanism of muscle contraction. Biochemical, mechanical, and structural approaches to elucidate cross-bridge action in muscle. Basic Res. Cardiol. 82,2, 3-16 (1987). Abstract
  • Fingerle, J., Kraft, T .: The induction of smooth muscle cell proliferation in vitro using an organ culture system. Int. Angiol. 6, 65-72 (1987). Abstract
  • Goldman, Y.E., and Brenner, B .: Molecular mechanism of muscle contraction. General Introduction. Ann Rev. Physiol. 49, 629-636 (1987). Medline Link
  • Brenner, B.: Zum molekularen Mechanismus der Muskelkontraktion. Mechanische, biochemische und röntgenstrukturanalytische Untersuchungen am isolierten kontraktilen Apparat von Skelettmuskelfasern. Habilitationsschrift, Univ. Tübingen (1986).
  • Brenner, B.: The necessity of using two parameters to describe isotonic shortening velocity of muscle tissues: the effect of various interventions upon initial shortening speed (vi) and curvature (b). Basic Res. Cardiol. 81, 54-69 (1986). Abstract
  • Brenner, B.: The cross-bridge cycle in muscle; mechanical, biochemical and structural studies to characterize cross-bridge kinetics in muscle for correlation with the actomyosin ATPase in solution. Basic Res. Cardiol. 81,1, 1-15 (1986). Abstract
  • Brenner, B., Chalovich, J.M., Greene, L.C., Eisenberg, E., and Schoenberg, M.: Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solutions. Biophys. J. 50, 685-691 (1986).
  • Brenner, B. and Eisenberg, E.: Rate of force generation in muscle: correlation with the actomyosin ATPase in solution. Proc. Natl. Acad. Sci. USA 83, 3542-3546 (1986). Abstract
  • Brenner, B., Yu. L.C., Greene, L.C., Eisenberg, E., and Schoenberg, M.: Ca 2+ -sensitive cross-bridge dissociation in the presence of MgPPi in skinned rabbit psoas fibers. Biophys. J. 50, 1101-1108 (1986). Abstract
  • Yu, L.C., and Brenner, B .: High resolution equatorial X-ray diffraction in single skinned rabbit psoas fibers. Biophys. J. 49, 133-135 (1986).
  • Brenner, B.: Sarcomeric domain organization within single skinned rabbit psoas fibers and its effects on laser light diffraction patterns. Biophys. J. 48, 967-982 (1985). Abstract
  • Brenner, B.: Correlation between the cross-bridge cycle in muscle and the actomyosin ATPase cycle in solution. J. Muscle Res. Cell Motil. 6, 659-664 (1985).
  • Brenner, B. and Yu, L.C.: Equatorial X-ray diffraction from skinned rabbit psoas fibers at various degrees of activation: changes in intensities and lattice spacing. Biophys. J. 48, 829-834 (1985). Abstract
  • Fleeter, T.B., Adams, J.P., Brenner, B ., and Podolsky, R.J.: A laser diffraction method for measuring muscle sarcomere length in vivo for application to tendon transfers. J. Hand Surg. 10A, 542-546 (1985).
  • Brenner, B., Yu, L.C., and Podolsky, R.J.: X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys. J. 46, 299-306 (1984). Abstract
  • Schoenberg, M., Brenner, B ., Chalovich, J.M., Greene, L.C., and Eisenberg, E.: Cross-bridge attachment in relaxed muscle. In: Contractile Mechanism in Muscle (H. Sugi and G.H. Pollack eds.) Plenum Publ. Corp. (1984).
  • Brenner, B.: A technique for stabilizing the striation pattern in fully activated skinned rabbit psoas fibers. Biophys. J. 41, 99-102 (1983). Abstract
  • Brenner, B., Schoenberg, M., Chalovich, J.M., Greene, L.C., and Eisenberg, E.: Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc. Natl. Acad. Sci. USA 79, 7288-7291 (1982). Abstract
  • Brenner, B., and Jacob, R.: Ca++ activation and maximum unloaded shortening velocity. Investigations on glycerinated skeletal and heart muscle preparations. Basic Res. Cardiol. 75, 40-46 (1980).
  • Brenner, B.: Effect of free sarcoplasmic Ca 2+ -concentration on maximum unloaded shortening velocity. Measurements on single glycerinated rabbit psoas muscle fibers. J. Muscle Res. Cell Motil. 1, 409-428 (1980).
  • Jacob, R., Brenner, B ., Ebrecht, G., Holubarsch, Ch., and Medugorac I.: Elastic and contractile properties of the myocardium in experimental cardiac hypertrophy of the rat. Methodological and pathophysiological considerations. Basic Res. Cardiol. 75, 253-261 (1980). Medline Link
  • Jacob, R., Holubarsch, Ch., Moser, H., and Brenner, B .: Quantification and interpretation of changes in myocardial elasticity under hypoxia: experimental models employing whole heart preparations and isolated muscle strips. Adv. Clinical Cardiol. 1, 211-228 (1980).
  • Brenner, B.: Indirekter Nachweis einer dehnungsinduzierten Ca 2+ -Freisetzung aus dem sarkoplasmatischen Retikulum glyzerinisierter Skelett- und Herzmuskelpräparate. Basic Res. Cardiol. 74, 177-202 (1979).
  • Tutschke, U., Eisert, W., Niemann, E.G.: Messung der Sauerstoffsättigung an nicht hämolysiertem Blut mit Hilfe von Lasern. Biomed. Tech. 21:279-292 (1979). Medline-Link

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ViSdP: Prof. Dr. med. B. Brenner, Letzte Änderung 28.03.2014 (bp)