Lehrstuhl für Biotechnologie

Publikationen

Publikationen pro Jahr 1998 2001 2002 2003 2004 2006 2008 2009 2010 2013 2015 2016 2017 2018 2019 2020 2021 2024

• 192 Artikel
• 25 Übersichtsartikel
• 8 Leitartikel
• 7 Kapitel
• 17 Mehr
  • 6 Kommentar/Debatte
  • 6 Kurzer Abriss
  • 2 Brief
  • 1 Buch
  • 1 Konferenzbeitrag
  • 1 Vorwort/Nachwort

Publikationen pro Jahr

Publikationen pro Jahr

Suchergebnisse

• 2004

  IspH protein of Escherichia coli: Studies on iron-sulfur cluster implementation and catalysis

  Gräwert, T., Kaiser, J., Zepeck, F., Laupitz, R., Hecht, S., Amslinger, S., Schramek, N., Schleicher, E., Weber, S., Haslbeck, M., Buchner, J., Rieder, C., Arigoni, D., Bacher, A., Eisenreich, W. & Rohdich, F., 13 Okt. 2004, in: Journal of the American Chemical Society. 126, 40, S. 12847-12855 9 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Escherichia Coli 100%
  • IspH 100%
  • Iron-sulfur Cluster 100%
  • Cysteine 100%
  • Escherichia coli 100%
  106 Zitate (Scopus)

• Oncogenic mutations reduce the stability of Src kinase

  Fabio Falsone, S., Leptihn, S., Osterauer, A., Haslbeck, M. & Buchner, J., 12 Nov. 2004, in: Journal of Molecular Biology. 344, 1, S. 281-291 11 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Src Kinase 100%
  • V-Src 100%
  • Oncogenic mutations 100%
  • Oncogene Src 100%
  • Phosphotransferase 100%
  44 Zitate (Scopus)

• Refolding of inclusion body proteins.

  Mayer, M. & Buchner, J., 2004, in: Methods in molecular medicine. 94, S. 239-254 16 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Protein Expression 100%
  • Upstream Open Reading Frame (uORF) 100%
  • Genome Sequencing 100%
  • Low Molecular Weight 100%
  • Unknown Protein 100%
  66 Zitate (Scopus)

• The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

  Richter, K., Walter, S. & Buchner, J., 1 Okt. 2004, in: Journal of Molecular Biology. 342, 5, S. 1403-1413 11 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Heat Shock Protein 90 (Hsp90) 100%
  • Co-chaperone 100%
  • Chaperone Cycle 100%
  • ATP Synthase 100%
  • SBA-1 100%
  128 Zitate (Scopus)

• The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104

  Grimminger, V., Richter, K., Imhof, A., Buchner, J. & Walter, S., 27 Feb. 2004, in: Journal of Biological Chemistry. 279, 9, S. 7378-7383 6 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Curing Agent 100%
  • ATP Hydrolysis 100%
  • Prion 100%
  • Guanidinium Chloride 100%
  • Hsp104 100%
  114 Zitate (Scopus)
• 2003

  Analysis of the interaction of small heat shock proteins with unfolding proteins

  Stromer, T., Ehrnsperger, M., Gaestel, M. & Buchner, J., 16 Mai 2003, in: Journal of Biological Chemistry. 278, 20, S. 18015-18021 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Small Heat Shock Protein (sHSP) 100%
  • Protein Unfolding 100%
  • Heat Shock Protein 100%
  • Non-native 57%
  • Hsp26 42%
  144 Zitate (Scopus)

• Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90

  Wegele, H., Muschler, P., Bunck, M., Reinstein, J. & Buchner, J., 10 Okt. 2003, in: Journal of Biological Chemistry. 278, 41, S. 39303-39310 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Individual Domain 100%
  • Heat Shock Protein 90 (Hsp90) 100%
  • ATPase Mechanism 100%
  • Hsp90 100%
  • ATPase 100%
  59 Zitate (Scopus)

• Modulation of the ATPase cycle of BiP by peptides and proteins

  Mayer, M., Reinstein, J. & Buchner, J., 27 Juni 2003, in: Journal of Molecular Biology. 330, 1, S. 137-144 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • ATPase Cycle 100%
  • ATPase 100%
  • Substrate Proteins 40%
  • Antibody Domain 40%
  • Hydrolysis 20%
  35 Zitate (Scopus)

• Nicht nur die abiturnote - Auswahl von studienbewerbern an der TU München

  Buchner, J. & Skerra, A., 1 Sept. 2003, in: Nachrichten aus der Chemie. 51, 9, S. 932-935 4 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

• NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol

  Dehner, A., Furrer, J., Richter, K., Schuster, I., Buchner, J. & Kessler, H., 5 Sept. 2003, in: ChemBioChem. 4, 9, S. 870-877 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Heat Shock Protein 90 (Hsp90) 100%
  • N-terminal Domain 100%
  • Geldanamycin 100%
  • Radicicol 100%
  • Perturbation Studies 100%
  73 Zitate (Scopus)

• Recombinant expression and purification of Ssa1p (Hsp70) from Saccharomyces cerevisiae using Pichia pastoris

  Wegele, H., Haslbeck, M. & Buchner, J., 25 März 2003, in: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences. 786, 1-2, S. 109-115 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Saccharomyces Cerevisiae 100%
  • Recombinant Expression 100%
  • Heat Shock Protein 70 (HSP70) 100%
  • Pichia Pastoris 100%
  • Copurification 100%
  19 Zitate (Scopus)

• Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle

  Richter, K., Muschler, P., Hainzl, O., Reinstein, J. & Buchner, J., 21 März 2003, in: Journal of Biological Chemistry. 278, 12, S. 10328-10333 6 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Heat Shock Protein 90 (Hsp90) 100%
  • ATP Synthase 100%
  • ATPase Cycle 100%
  • STI1 100%
  • Dimerization Reaction 100%
  167 Zitate (Scopus)

• Sti1 is a novel activator of the Ssa proteins

  Wegele, H., Haslbeck, M., Reinstein, J. & Buchner, J., 11 Juli 2003, in: Journal of Biological Chemistry. 278, 28, S. 25970-25976 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • STI1 100%
  • Hsp70 100%
  • Hsp90 83%
  • ATPase 50%
  • Ssa1 45%
  105 Zitate (Scopus)

• The N-terminal domain of p53 is natively unfolded

  Dawson, R., Müller, L., Dehner, A., Klein, C., Kessler, H. & Buchner, J., 3 Okt. 2003, in: Journal of Molecular Biology. 332, 5, S. 1131-1141 11 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Natively Unfolded 100%
  • Murine Double Minute 2 (MDM2) 100%
  • N-terminal Domain 100%
  • N-Terminus 100%
  • P53 100%
  204 Zitate (Scopus)
• 2002

  Folding and oxidation of the antibody domain C_H3

  Thies, M. J. W., Talamo, F., Mayer, M., Bell, S., Ruoppolo, M., Marino, G. & Buchner, J., 2002, in: Journal of Molecular Biology. 319, 5, S. 1267-1277 11 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Antibody Domain 100%
  • Disulfide Bridge 100%
  • Disulfide 100%
  • Oxidized State 66%
  • Disulfide Bond 50%
  52 Zitate (Scopus)

• Interaction of the chaperone BiP with an antibody domain: Implications for the chaperone cycle

  Knarr, G., Kies, U., Bell, S., Mayer, M. & Buchner, J., 2002, in: Journal of Molecular Biology. 318, 3, S. 611-620 10 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Chaperone 100%
  • Chaperone Cycle 100%
  • Antibody Domain 100%
  • Substrate Proteins 50%
  • Non-native 50%
  13 Zitate (Scopus)

• Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains

  Buchner, J., Rudolph, R. & Lilie, H., 2002, in: Journal of Molecular Biology. 318, 3, S. 829-836 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Disulfide Bond 100%
  • Antibody Chain 100%
  • Folded State 100%
  • Intra-domain 100%
  • Light Chain 100%
  14 Zitate (Scopus)

• N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

  Richter, K., Reinstein, J. & Buchner, J., 22 Nov. 2002, in: Journal of Biological Chemistry. 277, 47, S. 44905-44910 6 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Heat Shock Protein 90 (Hsp90) 100%
  • ATPase Cycle 100%
  • Catalytic Efficiency 100%
  • Terminal Residue 100%
  • N-Terminus 100%
  59 Zitate (Scopus)

• p53 contains large unstructured regions in its native state

  Bell, S., Klein, C., Müller, L., Hansen, S. & Buchner, J., 2002, in: Journal of Molecular Biology. 322, 5, S. 917-927 11 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Native State 100%
  • Unstructured Regions 100%
  • P53 100%
  • Structure Function 33%
  • Rigid Structure 33%
  224 Zitate (Scopus)

• Refolding and structural characterization of the human p53 tumor suppressor protein

  Bell, S., Hansen, S. & Buchner, J., 2 Mai 2002, in: Biophysical Chemistry. 96, 2-3, S. 243-257 15 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Structural Characterization 100%
  • Tumor Protein p53 (TP53) 100%
  • DNA Binding 100%
  • P53 100%
  • Quaternary Structure 66%
  36 Zitate (Scopus)

• Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity

  Kurek, I., Pirkl, F., Fischer, E., Buchner, J. & Breiman, A., 2002, in: Planta. 215, 1, S. 119-126 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Wheat 100%
  • Molecular Chaperone 100%
  • Citrate Synthase 100%
  • Peptidyl-prolyl Cis-trans Isomerase 100%
  • Cis-Trans Isomerase 100%
  30 Zitate (Scopus)
• 2001

  Coordinated ATP Hydrolysis by the Hsp90 Dimer

  Richter, K., Muschler, P., Hainzl, O. & Buchner, J., 7 Sept. 2001, in: Journal of Biological Chemistry. 276, 36, S. 33689-33696 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Enzymatic Hydrolysis 100%
  • Hsp90 100%
  • Adenosine Triphosphate 100%
  • Heat Shock Protein 90 (Hsp90) 100%
  • ATP Hydrolysis 100%
  176 Zitate (Scopus)

• Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40

  Pirkl, F. & Buchner, J., 2001, in: Journal of Molecular Biology. 308, 4, S. 795-806 12 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Functional Analysis 100%
  • Heat Shock Protein 90 (Hsp90) 100%
  • FKBP51 100%
  • FKBP52 100%
  • Cyp40 100%
  158 Zitate (Scopus)

• Localization of the Chaperone Domain of FKBP52

  Pirkl, F., Fischer, E., Modrow, S. & Buchner, J., 5 Okt. 2001, in: Journal of Biological Chemistry. 276, 40, S. 37034-37041 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Chaperone 100%
  • FKBP52 100%
  • Hsp90 100%
  • Heat Shock Protein 90 (Hsp90) 75%
  • Amino Acids 75%
  49 Zitate (Scopus)

• Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p

  Thual, C., Bousset, L., Komar, A. A., Walter, S., Buchner, J., Cullin, C. & Melki, R., 13 Feb. 2001, in: Biochemistry. 40, 6, S. 1764-1773 10 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Dimerization 100%
  • Yeast Prion 100%
  • Ure2p 100%
  • Prion 100%
  • N-Terminus 50%
  76 Zitate (Scopus)

• The alternatively folded state of the antibody C_H3 domain

  Thies, M. J. W., Kammermeier, R., Richter, K. & Buchner, J., 22 Juni 2001, in: Journal of Molecular Biology. 309, 5, S. 1077-1085 9 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • CH3 Domain 100%
  • Folded State 100%
  • Ionic Strength 100%
  • Disulfide 100%
  • Protein Secondary Structure 100%
  47 Zitate (Scopus)

• The crystal structure of the Fab fragment of the monoclonal antibody MAK33: Implications for folding and interaction with the chaperone BiP

  Augustine, J. G., De La Calle, A., Knarr, G., Buchner, J. & Frederick, C. A., 2 Feb. 2001, in: Journal of Biological Chemistry. 276, 5, S. 3287-3294 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Monoclonal Antibody 100%
  • Chaperone 100%
  • Fab Fragment 100%
  • Crystal Structure 100%
  • Surface Property 50%
  26 Zitate (Scopus)
• 2000

  BiP and PDI cooperate in the oxidative folding of antibodies in vitro

  Mayer, M., Kies, U., Kammermeier, R. & Buchner, J., 22 Sept. 2000, in: Journal of Biological Chemistry. 275, 38, S. 29421-29425 5 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Binding Protein 100%
  • Protein Disulfide Isomerase 100%
  • Oxidative Folding 100%
  • Monospecific Antibody 100%
  • Protein Disulfide-Isomerase 100%
  103 Zitate (Scopus)

• Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties

  Mayr, C., Richter, K., Lilie, H. & Buchner, J., 3 Nov. 2000, in: Journal of Biological Chemistry. 275, 44, S. 34140-34146 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Functional Properties 100%
  • Heat Shock Protein 90 (Hsp90) 100%
  • Saccharomyces Cerevisiae 100%
  • Immunophilin 100%
  • Hsp90 100%
  97 Zitate (Scopus)

• C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle

  Weikl, T., Muschler, P., Richter, K., Veit, T., Reinstein, J. & Buchner, J., 3 Nov. 2000, in: Journal of Molecular Biology. 303, 4, S. 583-592 10 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Hsp90 100%
  • C-Terminus 100%
  • Adenosine Triphosphate 100%
  • ATPase 100%
  • C-terminal Region 100%
  107 Zitate (Scopus)

• Limits of protein folding inside GroE complexes

  Grallert, H., Rutkat, K. & Buchner, J., 7 Juli 2000, in: Journal of Biological Chemistry. 275, 27, S. 20424-20430 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Protein Folding 100%
  • GroES 100%
  • Chaperone Complex 100%
  • Escherichia coli 100%
  • Escherichia Coli 50%
  16 Zitate (Scopus)
• 1999

  Analysis of GroE-assisted folding under nonpermissive conditions

  Grallert, H. & Buchner, J., 16 Juli 1999, in: Journal of Biological Chemistry. 274, 29, S. 20171-20177 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • GroEL 100%
  • GroES 100%
  • Protein Folding 50%
  • Adenosine Triphosphate 50%
  • Heat Shock 50%
  15 Zitate (Scopus)

• An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function

  Weikl, T., Abelmann, K. & Buchner, J., 29 Okt. 1999, in: Journal of Molecular Biology. 293, 3, S. 685-691 7 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • C-terminal Region 100%
  • Heat Shock Protein 90 (Hsp90) 100%
  • Chaperone Function 100%
  • Co-chaperone p23 100%
  • Chaperone Hsp90 100%
  89 Zitate (Scopus)

• BiP-binding sequences in HIV gp160. Implications for the binding specificity of BiP

  Knarr, G., Modrow, S., Todd, A., Gething, M. J. & Buchner, J., 15 Okt. 1999, in: Journal of Biological Chemistry. 274, 42, S. 29850-29857 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Binding Specificity 100%
  • Gp160 100%
  • Binding Site 100%
  • Human Immunodeficiency Virus 100%
  • Endoplasmic reticulum 66%
  50 Zitate (Scopus)

• Contribution of N- and C-terminal domains to the function of hsp90 in Saccharomyces cerevisiae

  Scheibel, T., Weikl, T., Rimerman, R., Smith, D., Lindquist, S. & Buchner, J., 1999, in: Molecular Microbiology. 34, 4, S. 701-713 13 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Amino Terminal Sequence 100%
  • Carboxy Terminal Sequence 100%
  • Saccharomyces cerevisiae 100%
  • N-Terminus 100%
  • Hsp90 100%
  14 Zitate (Scopus)

• Folding and association of the antibody domain C(H)3: Prolyl isomerization preceeds dimerization

  Thies, M. J. W., Mayer, J., Augustine, J. G., Frederick, C. A., Lilie, H. & Buchner, J., 15 Okt. 1999, in: Journal of Molecular Biology. 293, 1, S. 67-79 13 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  • Dimerization 100%
  • Proline Isomerization 100%
  • Antibody Domain 100%
  • Isomerization 100%
  • Cis Configuration 50%
  79 Zitate (Scopus)

• Hsp26: A temperature-regulated chaperone

  Haslbeck, M., Walke, S., Stromer, T., Ehrnsperger, M., White, H. E., Chen, S., Saibil, H. R. & Buchner, J., 1 Dez. 1999, in: EMBO Journal. 18, 23, S. 6744-6751 8 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

  Open Access

  • Chaperone 100%
  • Hsp26 100%
  • Heat Shock Protein 100%
  • Heat Shock 66%
  • Small Heat Shock Protein (sHSP) 50%
  388 Zitate (Scopus)
• 1998

  Analysis of chaperone function using citrate synthase as nonnative substrate protein

  Buchner, J., Grallert, H. & Jakob, U., 1998, in: Methods in Enzymology. 290, S. 323-338 16 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung
  198 Zitate (Scopus)

• Biochemie und molekulargenetik 1997

  Buchner, J. & Seckler, R., 1998, in: Nachrichten aus der Chemie. 46, 2, S. 182-185 4 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

• Purification and characterization of prokaryotic and eukaryotic Hsp90

  Buchner, J., Bose, S., Mayr, C. & Jakob, U., 1998, in: Methods in Enzymology. 290, S. 409-418 10 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung
  21 Zitate (Scopus)

• Purification and characterization of small heat shock proteins

  Buchner, J., Ehrnsperger, M., Gaestel, M. & Walke, S., 1998, in: Methods in Enzymology. 290, S. 339-349 11 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung
  32 Zitate (Scopus)

• Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52

  Buchner, J., Weikl, T., Bügl, H., Pirkl, F. & Bose, S., 1998, in: Methods in Enzymology. 290, S. 418-429 12 S.

  Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung
  22 Zitate (Scopus)