A. Lautwein

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Lysosomes from Human B Lymphocytes the Processing of Myelin Basic Protein in Asparagine-Specific Endoprotease , Controls Cathepsin G , and Not the

S. Stevanović, H. Wiendl, R. Lehmann, 2004 .

Cathepsin G, and Not the Asparagine-Specific Endoprotease, Controls the Processing of Myelin Basic Protein in Lysosomes from Human B Lymphocytes1

S. Stevanović, H. Wiendl, R. Lehmann, 2004, The Journal of Immunology.

Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis.

S. Stevanović, R. Kurek, E. Weber, 2003, The Journal of clinical investigation.

Antigen processing and presentation in human muscle: cathepsin S is critical for MHC class II expression and upregulated in inflammatory myopathies

H. Wiendl, Hanns Lochmüller, S. Krause, 2003, Journal of Neuroimmunology.

Crystallization and preliminary X‐ray crystallographic study of the Ras‐GTPase‐activating domain of human p120GAP

A. Wittinghofer, A. Scherer, K. Scheffzek, 1997, Proteins.

A New CYP2E1 Inhibitor, 12-Imidazolyl-1-dodecanol, Represents a Potential Treatment for Hepatocellular Carcinoma

F. Kuchenbauer, T. Barth, T. Wirth, 2021, Canadian journal of gastroenterology & hepatology.

ω‐Imidazolyl‐alkyl derivatives as new preclinical drug candidates for treating non‐alcoholic steatohepatitis

T. Wirth, R. Dvorský, D. Buckert, 2021, Physiological reports.

Crystallization and preliminary X-ray structure analysis of thermally unstable p21(H-ras) guanosine complexes.

W. Kabsch, I. Schlichting, E. Pai, 1994, Acta crystallographica. Section D, Biological crystallography.

The Ras-RasGAP complex: How to complement an inefficient active site

W. Kabsch, L. Wiesmüller, A. Wittinghofer, 1999 .

The inhibition of the GTPase activating protein‐Ha‐ras interaction by acidic lipids is due to physical association of the C‐terminal domain of the GTPase activating protein with micellar structures.

J. Serth, A. Wittinghofer, M. Frech, 1991, The EMBO journal.

Mutational andKinetic Analyses oftheGTPase-Activating Protein (GAP)-p2l Interaction: TheC-Terminal DomainofGAP IsNot Sufficient forFullActivity

J. John, H. Roché, R. Clark, 1992 .

Activity and subcellular distribution of cathepsins in primary human monocytes

E. Weber, C. Driessen, H. Overkleeft, 2003, Journal of leukocyte biology.

ω-imidazolyl-alkyl derivatives as new preclinical drug candidates for NASH therapy

T. Wirth, R. Dvorský, D. Buckert, 2019, bioRxiv.

Drug targeting CYP2E1 for the treatment of early-stage alcoholic steatohepatitis

F. Kuchenbauer, T. Wirth, T. Simmet, 2020, PloS one.

Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity

A. Wittinghofer, M. Frech, J. Scheffler, 1992, Molecular and cellular biology.

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.

W. Kabsch, L. Wiesmüller, A. Wittinghofer, 1997, Science.

Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras

W. Kabsch, A. Wittinghofer, M. Ahmadian, 1996, Nature.

Structural Differences in the Minimal Catalytic Domains of the GTPase-activating Proteins p120GAP and Neurofibromin*

F. Bischoff, L. Wiesmüller, A. Wittinghofer, 1996, The Journal of Biological Chemistry.

Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras.

M Geyer, H. Kalbitzer, E. Pai, 1994, Biochemistry.

Three-dimensional structure and properties of wild-type and mutant H-ras-encoded p21.

E. Pai, R. Goody, A. Wittinghofer, 1993, Ciba Foundation symposium.

Is there a rate-limiting step before GTP cleavage by H-ras p21?

R. Goody, A. Wittinghofer, H. Rensland, 1991, Biochemistry.

The Three-Dimensional Structure of P21 in the Catalytically Active Conformation and Analysis of Oncogenic Mutants

W. Kabsch, I. Schlichting, E. Pai, 1991 .

Inflammatory stimuli recruit cathepsin activity to late endosomal compartments in human dendritic cells

H. Kalbacher, T. Burster, E. Weber, 2002, European journal of immunology.

Human B lymphoblastoid cells contain distinct patterns of cathepsin activity in endocytic compartments and regulate MHC class II transport in a cathepsin S‐independent manner

Alfred Nordheim, Michael Reich, A. Nordheim, 2004, Journal of leukocyte biology.