J. Qin

发表

The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.

A. Gronenborn, G. Clore, J. Kuszewski, 1996, Structure.

Correlation between the steric bulk of the distal E7 and E11 residues and the tilt of the FeCN unit in cyanometmyoglobin as determined by NMR from the orientation of the magnetic axes in single and double point mutants.

S. Sligar, M. Chiu, K. Rajarathnam, 1994, Biochemistry.

Solution structure determination of the heme cavity in the E7 His-->Val cyano-met myoglobin point mutant based on the 1H NMR detected dipolar field of the iron: evidence for contraction of the heme pocket.

S. Sligar, M. Chiu, K. Rajarathnam, 1993, Biochemistry.

HIGH RESOLUTION SOLUTION NMR STRUCTURE OF MIXED DISULFIDE INTERMEDIATE BETWEEN MUTANT HUMAN THIOREDOXIN AND A 13 RESIDUE PEPTIDE COMPRISING ITS TARGET SITE IN HUMAN NFKB

A. Gronenborn, G. Clore, J. Qin, 1995 .

Ionization equilibria for side-chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NF kappa B.

A M Gronenborn, G M Clore, A. Gronenborn, 1996, Biochemistry.

Recruitment of the protein tyrosine phosphatase CSW by DOS is an essential step during signaling by the Sevenless receptor tyrosine kinase

Xiaolong Zhang, J. Qin, M. Simon, 1999, The EMBO journal.

Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκB

Jeffrey R. Huth, G. Marius Clore, Angela M. Gronenborn, 1995 .

Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.

A M Gronenborn, G M Clore, A. Gronenborn, 1995, Structure.

Oligomerization of a MutS Mismatch Repair Protein from Thermus aquaticus *

C. Ban, P. Hsieh, Wei Yang, 1999, The Journal of Biological Chemistry.

Solution 1H nuclear magnetic resonance determination of the distal pocket structure of cyanomet complexes of genetically engineered sperm whale myoglobin His64 (E7)-->Val, Thr67 (E10)-->Arg. The role of distal hydrogen bonding by Arg67 (E10) in modulating ligand tilt.

M. Brunori, F. Cutruzzolà, G. L. La Mar, 1993, Biophysical journal.

Solution 1H nuclear magnetic resonance determination of hydrogen bonding of the E10 (66) Arg side-chain to the bound ligand in Aplysia cyano-met myoglobin.

M. Brunori, M. Bolognesi, F. Ascoli, 1992, Journal of molecular biology.

The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin.

A M Gronenborn, G M Clore, A. Gronenborn, 1994, Structure.

Characterization and crystallization of a minimal catalytic core domain from mammalian type II adenylyl cyclase

J. Hurley, Wei-Jen Tang, Gongyi Zhang, 1997, Protein science : a publication of the Protein Society.

Structural and functional characterization of sperm whale myoglobin mutants: role of arginine (E10) in ligand stabilization.

M. Brunori, F. Cutruzzolà, G. L. La Mar, 1993, Biochemistry.

Complete sequence-specific1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: Application toAplysia cyano-metmyoglobin

J. Qin, G. N. Mar, 1992 .

Solution nuclear magnetic resonance determination of active site structure for a paramagnetic protein: cyanomet Aplysia myoglobin.

M. Brunori, F. Ascoli, G. L. La Mar, 1993, Journal of molecular biology.

Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.

J. Qin, W. Gu, R. Roeder, 1999, Molecular cell.