I. Brooks

发表

Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations.

K. P. Murphy, M. Doyle, D. Mcnulty, 1994, Biochemistry.

Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods.

I. Brooks, D. O'Shannessy, M. Brigham-Burke, 1993, Analytical biochemistry.

The soluble form of E-selectin is an asymmetric monomer. Expression, purification, and characterization of the recombinant protein.

K. Kopple, J. Trill, D. Mcnulty, 1994, The Journal of biological chemistry.

Determination of rate and equilibrium binding constants for macromolecular interactions by surface plasmon resonance.

I. Brooks, D. O'Shannessy, M. Brigham-Burke, 1994, Methods in enzymology.

Mutational effects on inclusion body formation in the periplasmic expression of the immunoglobulin VL domain REI.

D. Mcnulty, I. Brooks, R. Wetzel, 1996, Folding & design.

Kinetic and mutational analysis of human immunodeficiency virus type 1 reverse transcriptase inhibition by inophyllums, a novel class of non-nucleoside inhibitors.

J. Culp, C. Debouck, R. Hertzberg, 1994, The Journal of biological chemistry.

Biological and biophysical characterization of recombinant soluble human E-selectin purified at large scale by reversed-phase high-performance liquid chromatography.

D. Mcnulty, S. D. Burrows, S. Franklin, 1995, Journal of chromatography. B, Biomedical applications.

Determining confidence intervals for parameters derived from analysis of equilibrium analytical ultracentrifugation data.

D. G. Watts, I. Brooks, K. K. Soneson, 1994, Methods in enzymology.

Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface.

I. Brooks, D. Coen, P. Digard, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Proteolysis of an active site peptide of lactate dehydrogenase by human immunodeficiency virus type 1 protease.

C. Debouck, I. Brooks, J. Strickler, 1992, Biochemistry.

Measurement of protein interaction bioenergetics: application to structural variants of anti-sCD4 antibody.

R W Sweet, M. Doyle, I. Brooks, 2000, Methods in enzymology.

Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases.

M. Minnich, J. Culp, C. Debouck, 1992, Biochemistry.

Association of Rei Immunoglobulin Light Chain VL Domains: The Functional Linearity Of Parameters in Equilibrium Analytical Ultracentrifuge Models for Self-Associating Systems

D. G. Watts, I. Brooks, R. Wetzel, 1994 .

Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins.

S. Carr, M. Doyle, Baoguang Zhao, 1995, The Journal of biological chemistry.