Protein ? Disassembly im Verlauf der endosomalen Prozessierung

Literatur Seite 169
147 Hammer, J., E. Bono, F. Gallazi, C. Belunis, Z. Nagy und F. Sinigaglia: Precise Prediction of
major histocompatibility complex class II peptide interaction based on peptide side chain scanning; J.
Exp. Med.180: 2353; 1994
148 Falk, K., O. Rotzschke, S. Stefanovic, G. Jung und H. G. Rammenzee: Pool sequencing of natural
HLA - DR, DQ and DP ligands reveals detailed peptide motifs, constraints of processing and general
rules; Immunogentics 39: 230; 1994
149 Vogt, A.B., H. Kropshofer, H. Kallbacher, M. Kalbus, H.H. Rammensee, J.E. Coloigan, Martin
und R.: Ligand motifs of HLA-DRB5*0101 and DRB1*1501 molecules delineated from self-peptides;
J. Immunol.153: 1665; 1994
150 Reay, P.A., R.M. Cantor und M. M. Davis: Use of global amino acid replacments to define the
requirements for MHC binding and T cell recognition of moth cytochrome c; J. Immunol.153: 1665;
1994
151 Olson, A.J.: AutoDock 3.0 User Guide; User Guide 3: 1-76; 1999
152 Reizis, B., F. Mor, M. Eisenstein, H. Schild, S. Stefanovic, H.G. Rammensee und I. R. Cohen:
The peptide binding specifity of the MHC class II I-A molecule of the Lewis rat, RT1.Bl;
Int.Immunol.8: 1825-1832; 1996
153 Wauben, M.H., M. van der Kraan, M.C. Grosfeld-Stulenmeyer und I. Joosten: Definition of an
extended MHC class II-peptide binding motif for the autoimmune disease-associated Lewis rat RT1.Bl
molecule; Int.Immunol 9: 281-290; 1997
154 Panjwani, N., O. Akbari, S. Garcia, M. Brazi und Brigitta Stockinger: The HSC73 Molecular
Chaperone: Involvment in MHC Class II Antigen Presentation; J. Immunol.163: 1936-1942; 1999
155 Hammerling, G.J., B. Manoury, C. Watts, L. Adorini und A. Lanzavecchia: Peptide binding and
editing: generation of TCR ligands.; Res Immunol.149: 863-5; 1998
156 Westermeier, R.: Electrophoresis in Practise; VCH Weinheim 1. Aufl.; 1993
157 Kropshofer, H., S.O. Arndt, G. Moldenhauer, G.J. Hammerling und A. Vogt: HLA-DM acts as a
molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH.; Immunity.6: 293-302;
1997
158 Righetti, P.G.: Immobilized pH gradients: theory and methodology.; Elsevier, 1. Aufl.; 1989
159 Riese, R.J., P.R. Wolf, D. Bromme, L.R. Natkin, J.A. Villadangos, H.L. Ploegh und H. A.
Chapman: Essential role for cathepsin S in MHC class II-associated invariant chain processing and
peptide loading; Immunity 4: 357-365; 1996
160 vanNoort, J.M. und A. C. M. vanderDrift: The selectivity of Cathepsin D suggests an Involvment of
the Enzyme in the Generation of T-cell-Epitopes; J.Biol.chem 264 : 14159; 1989
161 Gradehandt, G. und E. Rüde: The endo/lysosomal protease cathepsin B is able to process
conalbumin fragments for presentation to T cells; Immunology 74: 393; 1991
162 Kageyama, T., M. Ichinose und S. Yonezawa: Processing of the precursors to neurotensin and
other bioactive peptides by cathepsin E; J. Biol. Chem.270: 19135-19140; 1995
163 Tomkinson, B.: Tripeptidyl peptidases: enzymes that count; TIBS 24: 355-359; 1999
164 Kupper, T.S.: Immune and inflammatory processes in cutaneus tissues: mechanisms and
speculations; J. Clin. Invest.86: 1783-1789; 1990
165 Kulke, M.: Untersuchungen zur Peptidpersistenz bei epidermalen Langerhans Zellen der Lewis-Ratte;
Diplomarbeit am FB Biologie der Johannes Gutenberg Universität Mainz; 1998
166 Bot, A., S. Bot, S. Antohi, K. Karjalainen und C. Bona: Kinetics of generation and persistence on
membrane class II molecules of a viral peptide expressed on foreign and self Proteins;
J.Immunol.157: 3436; 1996
167 Davidson, H.W. und C. Watts: Epitope-directed Processing of Specific Antigen by B Lymphocytes;
J. Cell. Biol.109: 85-92; 1989