C. Li

Occupancy of a C2‐C2 type ‘Zinc‐finger’ protein domain by copper Direct observation by electrospray ionization mass spectrometry

T. Yip, T. Hutchens, M. Allen, 1992, FEBS letters.

Proteins associated with untransformed estrogen receptor in vitro. Perturbation of hydrophobic interactions induces alterations in quaternary structure and exposure of the DNA-binding site.

T. Hutchens, P. Besch, C. Li, 1987, Biochemistry.

Ligand‐binding properties of estrogen receptor proteins after interaction with surface‐immobilized Zn(II) ions: Evidence for localized surface interactions and minimal conformational changes

T. Hutchens, C. Li, C. Li, 1990, Journal of molecular recognition : JMR.

Estrogen receptor interaction with immobilized metals: Differential molecular recognition of Zn2+, Cu2+ and Ni2+ and separation of receptor isoforms

T. Hutchens, C. Li, C. Li, 1988, Journal of molecular recognition : JMR.

Two high-affinity ligand binding states of uterine estrogen receptor distinguished by modulation of hydrophobic environment.

T. Hutchens, P. Besch, C. Li, 1987, Biochemistry.

Urea-induced transformation of native estrogen receptor and evidence for separate DNA-and ATP-binding sites.

T. Hutchens, P. Besch, C. Li, 1986, Biochemical and biophysical research communications.

Multiple DNA-binding estrogen receptor forms resolved by interaction with immobilized metal ions. Identification of a metal-binding domain.

T. Yip, T. Hutchens, C. Li, 1989, The Journal of biological chemistry.

Synthetic metal-binding protein surface domains for metal ion-dependent interaction chromatography. I. Analysis of bound metal ions by matrix-assisted UV laser desorption time-of-flight mass spectrometry.

T. Yip, T. Hutchens, R. Nelson, 1992, Journal of chromatography.