A. Seelig

发表

The major-histocompatibility-complex-encoded beta-type proteasome subunits LMP2 and LMP7. Evidence that LMP2 and LMP7 are synthesized as proproteins and that cellular levels of both mRNA and LMP-containing 20S proteasomes are differentially regulated.

S. Frentzel, P. Kloetzel, I. Kuhn‐Hartmann, 1993, European journal of biochemistry.

Peptides and the proteasome

J. Howard, A. Seelig, 1993, Nature.

Characterization of mouse proteasome subunit MC3 and identification of proteasome subtypes with different cleavage characteristics. Proteasome subunits, proteasome subpopulations.

P. Kloetzel, A. Seelig, B. Boes, 1993, Enzyme & protein.

ProcessingTransporter Associated with Antigen Endoplasmic Reticulum for Access to MHC Class I Molecules Compete in the

M. Knittler, K. Gülow, J. Howard, 1998 .

Sequence and genomic organization of the Drosophila proteasome PROS-Dm25 gene.

M. Troxell, P. Kloetzel, A. Seelig, 1993, Biochimica et biophysica acta.

Subunit of the '20S' proteasome (multicatalytic proteinase) encoded by the major histocompatibility complex

Günter J. Hämmerling, G. Hämmerling, V. Ortiz-Navarrete, 1991, Nature.

Functional analysis by site-directed mutagenesis of the complex polymorphism in rat transporter associated with antigen processing.

J. Howard, G. Butcher, E. Deverson, 1998, Journal of immunology.

MHC class I molecules compete in the endoplasmic reticulum for access to transporter associated with antigen processing.

M. Knittler, K. Gülow, J. Howard, 1998, Journal of immunology.

Functional analysis of eukaryotic 20S proteasome nuclear localization signal.

P. Henklein, C. Knuehl, P. Kloetzel, 1996, Experimental cell research.

Differential effect of transporter Tap 2 gene introduction into RMA‐S cells on viral antigen processing

W. Kast, M. Ossevoort, F. Momburg, 1993, European journal of immunology.

Antigen processing. Peptides and the proteasome.

J. Howard, A. Seelig, 1993, Nature.

20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes.

P. Kloetzel, S. Frentzel, P. Kloetzel, 1994, Journal of molecular biology.

Drosophila proteasome Dm25 subunit substitutes the mouse MC3 subunit in hybrid proteasomes. The N-terminal domain is essential for subunit incorporation.

G. Multhaup, K. Beyreuther, P. Kloetzel, 1993, The Journal of biological chemistry.

Molecular interaction of the proteasome (multicatalytic proteinase). Evidence that the proteasome is not a constituent of the '26 S' multienzyme complex.

B. Dahlmann, L. Kuehn, P. Kloetzel, 1991, The Biochemical journal.

The proteasome of Drosophila and features of the evolutionarily conserved PROS-gene family.

U. Klein, C. Haass, S. Frentzel, 1991, Biomedica biochimica acta.

The major‐histocompatibility‐complex‐encoded β‐type proteasome subunits LMP2 and LMP7

S. Frentzel, P. Kloetzel, I. Kuhn‐Hartmann, 1993 .