K. Lin

发表

Crystal structure of a transcriptionally active Smad4 fragment.

B. Qin, S. Lam, Kai Lin, 1999, Structure.

Sedimentation studies reveal a direct role of phosphorylation in Smad3:Smad4 homo- and hetero-trimerization.

Benoy M. Chacko, J. Correia, S. Lam, 2001, Biochemistry.

Structural basis of Smad1 activation by receptor kinase phosphorylation.

J J Correia, Benoy M. Chacko, B. Qin, 2001, Molecular cell.

Low concentration of inducer favors production of active form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli.

K. Lin, L. Li, Q. Yang, 1997, Protein expression and purification.

In Vitro Transcription of the Rat Insulin-like Growth Factor-I Gene (*)

L. Phillips, K. Lin, P. Farmer, 1996, The Journal of Biological Chemistry.

Identification of Core Sequences Involved in Metabolism-Dependent Nuclear Protein Binding to the Rat Insulin-Like Growth Factor I Gene1.

L. Phillips, K. Lin, C. Pao, 1999, Endocrinology.

Transcriptional Regulation of the Rat Insulin-like Growth Factor-I Gene Involves Metabolism-dependent Binding of Nuclear Proteins to a Downstream Region (*)

L. Phillips, K. Lin, P. Farmer, 1995, The Journal of Biological Chemistry.

Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Use of site-directed mutagenesis to evaluate the roles of His-258 and His-392 in catalysis.

K. Lin, A. Tauler, S. Pilkis, 1990, The Journal of biological chemistry.

Mechanism of modulation of rat liver fructose-2,6-bisphosphatase by nucleoside triphosphates.

K. Lin, S. Pilkis, D. Okar, 1994, The Journal of biological chemistry.

Expression of mammalian liver glycolytic/gluconeogenic enzymes in Escherichia coli: recovery of active enzyme is strain and temperature dependent.

K. Lin, I. Kurland, A. Lange, 1990, Protein expression and purification.

Arg-257 and Arg-307 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase bind the C-2 phospho group of fructose-2,6-bisphosphate in the fructose-2,6-bisphosphatase domain.

J. Correia, K. Lin, L. Li, 1992, The Journal of biological chemistry.

Site-directed mutagenesis in rat liver 6-phosphofructo-2-kinase. Mutation at the fructose 6-phosphate binding site affects phosphate activation.

J. Correia, K. Lin, I. Kurland, 1992, The Journal of biological chemistry.

Evidence for NH2- and COOH-terminal interactions in rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

K. Lin, I. Kurland, L. Li, 1994, Journal of Biological Chemistry.

Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The role of surface loop basic residues in substrate binding to the fructose-2,6-bisphosphatase domain.

J. Correia, K. Lin, L. Li, 1992, The Journal of biological chemistry.

Lysine 356 is a critical residue for binding the C-6 phospho group of fructose 2,6-bisphosphate to the fructose-2,6-bisphosphatase domain of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

J. Correia, K. Lin, L. Li, 1992, The Journal of biological chemistry.

Glu327 is part of a catalytic triad in rat liver fructose-2,6-bisphosphatase.

J. Correia, K. Lin, L. Li, 1992, The Journal of biological chemistry.

Preliminary X-ray analysis of a truncated form of recombinant fructose-2,6-bisphosphatase.

J. Pflugrath, K. Lin, S. Pilkis, 1994, Journal of molecular biology.

Cloning and characterization of a plasma membrane Na+/H+ antiporter gene from Cucumis sativus

K. Lin, Z. Li, Shu Wang, 2013, Russian Journal of Plant Physiology.