J. Alves

发表

The c-myc promoter: still MysterY and challenge.

I. Wierstra, J. Alves, Inken Wierstra, 2008, Advances in cancer research.

FOXM1, a typical proliferation-associated transcription factor

I. Wierstra, J. Alves, Inken Wierstra, 2007, Biological chemistry.

Protein Engineering of Restriction Enzymes

J. Alves, P. Vennekohl, 2004 .

Probing the function of individual amino acid residues in the DNA binding site of the EcoRI restriction endonuclease by analysing the toxicity of genetically engineered mutants.

T. Oelgeschläger, R. Geiger, A. Pingoud, 1990, Gene.

Genetic engineering of EcoRI mutants with altered amino acid residues in the DNA binding site: physicochemical investigations give evidence for an altered monomer/dimer equilibrium for the Gln144Lys145 and Gln144Lys145Lys200 mutants.

A. Düsterhöft, R. Geiger, C. Urbanke, 1989, Biochemistry.

Asn141 is essential for DNA recognition by EcoRI restriction endonuclease

J. Alves, A. Fritz, W. Küster, 1998, FEBS letters.

A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV.

T. Oelgeschläger, A. Pingoud, J. Alves, 1992, Biochemistry.

Molecular and Functional Characterization of Clathrin- and AP-2-binding Determinants within a Disordered Domain of Auxilin*

J. Alves, R. Frank, E. Ungewickell, 2003, Journal of Biological Chemistry.

Arg(362) and Tyr(365) of the botulinum neurotoxin type a light chain are involved in transition state stabilization.

J. Alves, T. Binz, A. Kollewe, 2002, Biochemistry.

Changing the hydrogen-bonding potential in the DNA binding site of EcoRI by site-directed mutagenesis drastically reduces the enzymatic activity, not, however, the preference of this restriction endonuclease for cleavage within the site-GAATTC-.

R. Geiger, A. Pingoud, J. Alves, 1989, Biochemistry.

A fast and accurate enzyme-linked immunosorbent assay for the determination of the DNA cleavage activity of restriction endonucleases.

A. Jeltsch, A. Pingoud, J. Alves, 1993, Analytical biochemistry.

Unusual Structural Organization of the Endocytic Proteins AP180 and Epsin 1*

R. Knorr, C. Urbanke, J. Alves, 2002, The Journal of Biological Chemistry.

FOXM1c is activated by cyclin E/Cdk2, cyclin A/Cdk2, and cyclin A/Cdk1, but repressed by GSK-3alpha.

I. Wierstra, J. Alves, Inken Wierstra, 2006, Biochemical and biophysical research communications.

Two carbohydrate binding sites in the H(CC)-domain of tetanus neurotoxin are required for toxicity.

J. Alves, H. Bigalke, T. Binz, 2003, Journal of molecular biology.

Site-directed mutagenesis in the catalytic center of the restriction endonuclease EcoRI.

A. Jeltsch, J. Alves, G. Maass, 1995, Gene.

Site directed mutagenesis experiments suggest that Glu 111, Glu 144 and Arg 145 are essential for endonucleolytic activity of EcoRI.

R. Geiger, A. Pingoud, J. Alves, 1986, Nucleic acids research.

Mutational analysis of the function of Gln115 in the EcoRI restriction endonuclease, a critical amino acid for recognition of the inner thymidine residue in the sequence -GAATTC- and for coupling specific DNA binding to catalysis.

T. Oelgeschläger, A. Jeltsch, A. Pingoud, 1993, Journal of molecular biology.

Effect of polyamines and basic proteins on cleavage of DNA by restriction endonucleases.

C. Gualerzi, A. Pingoud, C. Urbanke, 1984, Biochemistry.

Asp‐59 is not important for the catalytic activity of the restriction endonuclease EcoRI

J. Alves, G. Maass, G. Grabowski, 1996, FEBS letters.

Importance of phosphate contacts for sequence recognition by EcoRI restriction enzyme.

J. Alves, S. B. Katti, O. Rosati, 2002, Biochemical and biophysical research communications.

The influence of sequences adjacent to the recognition site on the cleavage of oligodeoxynucleotides by the EcoRI endonuclease.

J. Langowski, A. Pingoud, J. Alves, 1984, European journal of biochemistry.

Two identical subunits of the EcoRI restriction endonuclease Co-operate in the binding and cleavage of the palindromic substrate.

J. Langowski, A. Pingoud, C. Urbanke, 1982, European journal of biochemistry.

Does the specific recognition of DNA by the restriction endonuclease EcoRI involve a linear diffusion step? Investigation of the processivity of the EcoRI endonuclease.

J. Langowski, A. Pingoud, J. Alves, 1983, Nucleic acids research.

Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA.

A. Jeltsch, A. Pingoud, J. Alves, 1994, Biochemistry.

On the divalent metal ion dependence of DNA cleavage by restriction endonucleases of the EcoRI family.

A. Jeltsch, A. Pingoud, M. Fuxreiter, 2009, Journal of molecular biology.

Accuracy of the EcoRV restriction endonuclease: binding and cleavage studies with oligodeoxynucleotide substrates containing degenerate recognition sequences.

J. Alves, H. Wolfes, U. Selent, 1990, Biochemistry.

FOXM1c transactivates the human c‐myc promoter directly via the two TATA boxes P1 and P2

I. Wierstra, J. Alves, Inken Wierstra, 2006, The FEBS journal.

Spectroscopic and hydrodynamic studies reveal structural differences in normal and transforming H-ras gene products.

A. Wittinghofer, A. Pingoud, C. Urbanke, 1988, Biochemistry.

Fluorescence stopped-flow kinetics of the cleavage of synthetic oligodeoxynucleotides by the EcoRI restriction endonuclease.

A. Pingoud, C. Urbanke, J. Alves, 1989, Biochemistry.

Transcription factor FOXM1c is repressed by RB and activated by cyclin D1/Cdk4

I. Wierstra, J. Alves, Inken Wierstra, 2006, Biological chemistry.

Mg2+ confers DNA binding specificity to the EcoRV restriction endonuclease.

A. Pingoud, J. Alves, H. Wolfes, 1992, Biochemistry.

Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity

D. Krüger, J. Alves, M. Schutkowski, 2011, Nucleic acids research.

Molecular analysis of restriction endonuclease EcoRII from Escherichia coli reveals precise regulation of its enzymatic activity by autoinhibition

D. Krüger, M. Szczepek, J. Alves, 2009, Molecular microbiology.

Despite its strong transactivation domain, transcription factor FOXM1c is kept almost inactive by two different inhibitory domains

I. Wierstra, J. Alves, Inken Wierstra, 2006, Biological chemistry.

Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain.

D. Krüger, J. Alves, E. Möncke-Buchner, 2013, Biochimie.

Engineering the product profile of a polysialyltransferase.

J. Alves, R. Gerardy-Schahn, Timothy G Keys, 2014, Nature chemical biology.

Cyclin E/Cdk2, P/CAF, and E1A regulate the transactivation of the c-myc promoter by FOXM1.

I. Wierstra, J. Alves, Inken Wierstra, 2008, Biochemical and biophysical research communications.

On the catalytic mechanism of EcoRI and EcoRV A detailed proposal based on biochemical results, structural data and molecular modelling

A. Jeltsch, A. Pingoud, J. Alves, 1992, FEBS letters.

Accuracy of the EcoRI restriction endonuclease: binding and cleavage studies with oligodeoxynucleotide substrates containing degenerate recognition sequences.

A. Pingoud, J. Alves, G. Maass, 1990, Biochemistry.

Substrate-assisted catalysis in the cleavage of DNA by the EcoRI and EcoRV restriction enzymes.

A. Jeltsch, A. Pingoud, J. Alves, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Influence of divalent cations on inner-arm mutants of restriction endonuclease EcoRI.

J. Alves, S. Windolph, 1997, European journal of biochemistry.

The central domain of transcription factor FOXM1c directly interacts with itself in vivo and switches from an essential to an inhibitory domain depending on the FOXM1c binding site

I. Wierstra, J. Alves, Inken Wierstra, 2007, Biological chemistry.

A monomeric mutant of restriction endonuclease EcoRI nicks DNA without sequence specificity

J. Alves, Petra Fritsche, 2004, Biological chemistry.

FOXM1c and Sp1 transactivate the P1 and P2 promoters of human c-myc synergistically.

J. Alves, Inken Wierstra, 2007, Biochemical and biophysical research communications.