J. Walder

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Predicting stability of DNA duplexes in solutions containing magnesium and monovalent cations.

Yong You, Richard Owczarzy, Mark A Behlke, 2008, Biochemistry.

Oligodeoxynucleotide-directed mutagenesis using the yeast transformation system.

J. Walder, R. Walder, J. A. Walder, 1986, Gene.

Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo.

P. K. Smith, M. Rendell, J. Walder, 1986, The Journal of laboratory and clinical medicine.

Substrate specificity of human RNase H1 and its role in excision repair of ribose residues misincorporated in DNA.

J. Walder, P. Eder, R. Walder, 1993, Biochimie.

Chemically modified and recombinant hemoglobin blood substitutes.

J. Walder, S. R. Snyder, J. A. Walder, 1991, Biotechnology.

Pathways of degradation and mechanism of action of antisense oligonucleotides in Xenopus laevis embryos.

D. L. Weeks, J. Walder, J. Dagle, 1991, Antisense research and development.

Cyclin B mRNA depletion only transiently inhibits the Xenopus embryonic cell cycle.

D. L. Weeks, J. Walder, J. Dagle, 1991, Development.

Isolation and characterization of a new hemoglobin derivative cross-linked between the alpha chains (lysine 99 alpha 1----lysine 99 alpha 2).

P. Rogers, A. Arnone, J. Walder, 1986, The Journal of biological chemistry.

Kinetic analysis of Escherichia coli RNase H using DNA-RNA-DNA/DNA substrates.

R. Hogrefe, H. Hogrefe, J. Walder, 1990, The Journal of biological chemistry.

A protein kinase inhibitor gene reduces both basal and multihormone-stimulated prolactin gene transcription.

R. Day, R. Maurer, J. Walder, 1989, Journal of Biological Chemistry.

Physical properties of oligonucleotides containing phosphoramidate-modified internucleoside linkages.

J. Walder, M. Andracki, J. Dagle, 1991, Nucleic acids research.

HbXL99 alpha: a hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute.

J. Walder, R. Walder, S. R. Snyder, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism for the increase in solubility of deoxyhemoglobin S due to cross-linking the beta chains between lysine-82 beta 1 and lysine-82 beta 2.

A. Arnone, J. Walder, R. Chatterjee, 1982, Biochemistry.

Design and operation of an adapter for the measurement of platelet aggregation with a spectrophotometer.

I. M. Klotz, J. Walder, 1978, Analytical biochemistry.

Targeted degradation of mRNA in Xenopus oocytes and embryos directed by modified oligonucleotides: studies of An2 and cyclin in embryogenesis.

D. L. Weeks, J. Walder, J. Dagle, 1990, Nucleic acids research.

Use of high specific activity StarFire oligonucleotide probes to visualize low-abundance pre-mRNA splicing intermediates in S. pombe.

W. McDonald, M. Behlke, E. Devor, 2000, BioTechniques.

Allosteric kinetics and equilibria of triligated, cross-linked hemoglobin.

F. Ferrone, J. Walder, M. Andracki, 1993, Biophysical journal.

Isolation and characterization of the triply oxidized derivative of a cross-linked hemoglobin.

J. Walder, A. Deyoung, R. Noble, 1992, Biochemistry.

The interaction of hemoglobin with the cytoplasmic domain of band 3 of the human erythrocyte membrane.

P. Low, E. Kaiser, T. Steck, 1984, The Journal of biological chemistry.

Development of antisickling compounds that chemically modify hemoglobin S specifically within the 2,3-diphosphoglycerate binding site.

A. Arnone, J. Walder, R. Walder, 1980, Journal of molecular biology.

Diaspirins that cross-link beta chains of hemoglobin: bis(3,5-dibromosalicyl) succinate and bis(3,5-dibromosalicyl) fumarate.

I. M. Klotz, J. Walder, R. Walder, 1979, Biochemistry.

Prolongation of the intravascular retention of hemoglobin modified with a long-chain fatty acid derivative.

J. Walder, M. Andracki, S. Fowler, 1994, Artificial cells, blood substitutes, and immobilization biotechnology.

Alternative aspirins as antisickling agents: acetyl-3,5-dibromosalicylic acid.

I. M. Klotz, J. Walder, W. Watkin, 1977, Proceedings of the National Academy of Sciences of the United States of America.

The 35-nucleotide spliced leader sequence is common to all trypanosome messenger RNA's.

J. Donelson, D. Dorfman, D. Engman, 1986, Science.

Substrate specificity and kinetics of degradation of antisense oligonucleotides by a 3' exonuclease in plasma.

J. Walder, P. Eder, J A Walder, 1991, Antisense research and development.

Role of RNase H in hybrid-arrested translation by antisense oligonucleotides.

J. Walder, R. Walder, J. A. Walder, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Chemical Modifications of Hemoglobin S at the 2,3-Diphosphoglycerate Binding Site: An Approach to Therapy of Sickle Cell Disease

J. Walder, R. Walder, 1981 .

Complementary carrier peptide synthesis: general strategy and implications for prebiotic origin of peptide synthesis.

S. Freier, R. Letsinger, I. M. Klotz, 1979, Proceedings of the National Academy of Sciences of the United States of America.

Effects of sodium ions on DNA duplex oligomers: improved predictions of melting temperatures.

Lingyan Huang, Yong You, Richard Owczarzy, 2004, Biochemistry.

Schiff base adducts of hemoglobin. Modifications that inhibit erythrocyte sickling.

I. M. Klotz, J. Walder, R. Zaugg, 1977, The Journal of biological chemistry.

Dielectric studies of amino acid conformation

J. Walder, 1976 .

RNase H-dependent PCR (rhPCR): improved specificity and single nucleotide polymorphism detection using blocked cleavable primers

M. Behlke, S. Rose, J. Walder, 2011, BMC biotechnology.

Improved Performance of Anti-miRNA Oligonucleotides Using a Novel Non-Nucleotide Modifier

M. Behlke, K. A. Lennox, R. Owczarzy, 2013, Molecular therapy. Nucleic acids.

Antisense DNA and RNA: progress and prospects.

J. Walder, 1988, Genes & development.

Partial characterization of the copolymerization reaction of erythrocyte membrane band 3 with hemichromes.

P. Low, J. Walder, P S Low, 1987, Biochemistry.

The effect of 2,3-diphosphoglycerate on the solubility of deoxyhemoglobin S.

B. Kim, J. Walder, W. N. Poillon, 1986, Archives of biochemistry and biophysics.

Human hemoglobin expression in Escherichia coli: importance of optimal codon usage.

S. Sligar, J. Walder, R. Walder, 1992, Biochemistry.

Thermodynamic treatment of oligonucleotide duplex–simplex equilibria

M. Behlke, I. M. Klotz, R. Owczarzy, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Epithelial-mesenchymal transformation of embryonic cardiac endothelial cells is inhibited by a modified antisense oligodeoxynucleotide to transforming growth factor beta 3.

D. L. Weeks, Raymond B. Runyan, J. Walder, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Cloning of the MspI modification enzyme. The site of modification and its effects on cleavage by MspI and HpaII.

J. Walder, R. Chatterjee, R. Walder, 1983, The Journal of biological chemistry.

Modification of hemoglobin with analogs of aspirin.

I. M. Klotz, J. Walder, R. Walder, 1980, The Journal of biological chemistry.

Ribonuclease H from K562 human erythroleukemia cells. Purification, characterization, and substrate specificity.

J. Walder, P. Eder, P S Eder, 1991, The Journal of biological chemistry.

Cloning and expression of the Pst I restriction-modification system in Escherichia coli.

J. Hartley, J. Donelson, J. Walder, 1981, Proceedings of the National Academy of Sciences of the United States of America.

The organization and complete nucleotide sequence of the PstI restriction-modification system.

J. Donelson, J. Walder, R. Walder, 1984, The Journal of biological chemistry.

Characterization of modified antisense oligonucleotides in Xenopus laevis embryos.

M. Behlke, S. Rose, K. A. Lennox, 2006, Oligonucleotides.

Preparation of intramolecularly cross-linked hemoglobins.

J. Walder, R. Walder, M. Andracki, 1994, Methods in enzymology.

Structural features required for the reactivity and intracellular transport of bis(3,5-dibromosalicyl)fumarate and related anti-sickling compounds that modify hemoglobin S at the 2,3-diphosphoglycerate binding site.

J. Walder, Y. Iwai, R. Chatterjee, 1984, The Journal of biological chemistry.