S. Schnierer

发表

MPSA short communications

W. E. Moddeman, J. A. Lindquist, D. N. Perkins, 1988 .

Preparation of active recombinant TIMP-1 from Escherichia coli inclusion bodies and complex formation with the recombinant catalytic domain of PMNL-collagenase.

H. Tschesche, T. Kleine, S. Schnierer, 1993, Biochemistry.

Sporulation of mitochondrial respiratory deficient mit- mutants of Saccharomyces cerevisiae

G. Michaelis, S. Schnierer, E. Pratje, 1979, Molecular and General Genetics MGG.

Recombinant aprotinin homologue with new inhibitory specificity for cathepsin G.

H. Tschesche, S. Schnierer, T. Brinkmann, 1991, European journal of biochemistry.

Mitochondrial DNA of Chlamydomonas reinhardtii: the DNA sequence of a region showing homology with mammalian URF2

B. Dujon, S. Schnierer, E. Pratje, 1984, Current Genetics.

The X‐ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.

R. Huber, P. Reinemer, W. Bode, 1994, The EMBO journal.

The recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificity.

H. Tschesche, V. Knäuper, A. Hillemann, 1993, Biochemical and Biophysical Research Communications - BBRC.

Inhibition of Matrix Metalloproteinases in Rheumatoid Arthritis and the Crystallographic Binding Mode of a Peptide Inhibitor

P. Reinemer, W. Bode, H. Tschesche, 1994, Annals of the New York Academy of Sciences.

Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases

R. Huber, P. Reinemer, W. Bode, 1994, FEBS letters.

Function and Structure of Human Leucocyte Collagenase

P. Reinemer, W. Bode, H. Tschesche, 1995 .