K. Shelton

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Selective Synthesis of a Nuclear Acidic Protein in Liver Cells stimulated by Cortisol

V. Allfrey, K. Shelton, VINCENT G. ALLFREY, 1970, Nature.

A procedure for purifying low-abundance protein components from the brain cytoskeleton-nuclear matrix fraction

E. Klann, K. Shelton, Gerry Nixon, 1991, Journal of Neuroscience Methods.

In vitro oxidation of intrinsic sulfhydryl groups yields polymers of the two predominant polypeptides in the nuclear envelope fraction.

D. Cochran, K. Shelton, 1978, Biochemistry.

Major oligomeric structural proteins of the HeLa nucleus.

C. Cobbs, K. Shelton, 1978, Archives of biochemistry and biophysics.

Nuclear envelope fraction proteins: isolation and comparison with the nuclear protein of the avian erythrocyte.

C. Cobbs, J. Povlishock, K. Shelton, 1976, Archives of biochemistry and biophysics.

Selective effects of nonionic detergent and salt solutions in dissolving nuclear envelope protein.?20U.

K. Shelton, 1976, Biochimica et biophysica acta.

Protein—protein interaction in the nuclear envelope

D. Cochran, K. Shelton, 1976, FEBS letters.

Self-administration of phenylpropanolamine (PPA) by rats previously trained to self-administer amphetamine

P. Wellman, S. Schenk, K. Shelton, 1989, Pharmacology Biochemistry and Behavior.

The induction of stress-related proteins by lead.

K. Shelton, P. M. Egle, J. M. Todd, 1986, The Journal of biological chemistry.

The proteins of lead-induced intranuclear inclusion bodies.

K. Shelton, P. M. Egle, 1982, The Journal of biological chemistry.

Evidence that glutathione participates in the induction of a stress protein.

K. Shelton, P. M. Egle, J. M. Todd, 1986, Biochemical and biophysical research communications.

Characteristics of nuclear proteins during granulocyte development

R. Scott, W. Grogan, K. Shelton, 1980, Blut.

The role of the nuclear protein matrix during development of rabbit granulocytes.

R. Scott, K. Shelton, J. Haar, 1981, Blood.

Nuclear lamins of erythrocyte and liver.

D. Cochran, J. Ruffolo, K. Shelton, 1980, The Journal of biological chemistry.

Nuclear residual proteins from goose erythroid cells and liver.

K. Shelton, J. M. Neelin, 1971, Biochemistry.

Chronic lead intoxication causes a brain-specific nuclear protein to accumulate in the nuclei of cells lining kidney tubules.

K. Shelton, P. M. Egle, 1986, The Journal of biological chemistry.

Tryptophanyl fluorescence of sodium dodecyl sulfate treated and 2-mercaptoethanol reduced proteins: a simple assay for tryptophan.

K. S. Rogers, K. Shelton, 1971, Analytical biochemistry.

Phosphoproteins of the avian erythrocyte.

C. Cobbs, K. Shelton, 1975, Archives of biochemistry and biophysics.

Nuclear envelope proteins: identification of lamin B subtypes.

D. Cochran, K. Shelton, P. M. Egle, 1981, Biochemical and biophysical research communications.

Phosphate incorporation into "nuclear" residual proteins of goose erythrocytes.

V. Seligy, K. Shelton, J. M. Neelin, 1972, Archives of biochemistry and biophysics.

Oligomeric structure of the major nuclear envelope protein lamin B.

D. Cochran, K. Shelton, V. Guthrie, 1982, The Journal of biological chemistry.

Dodecyl sulfate-polyacrylamide gel electrophoresis of N'-dimethylaminonaphthalene-5-sulfonyl-proteins: a covalently attached fluorescent label.

K. Shelton, 1971, Biochemical and biophysical research communications.

A nuclear matrix protein stabilized by lead exposure: current knowledge and future prospects.

E. Klann, J. Bigbee, K. Shelton, 1993, Neurotoxicology.

Preexposure sensitizes rats to the rewarding effects of cocaine

S. Schenk, B. Horger, K. Shelton, 1990, Pharmacology Biochemistry and Behavior.

A lead-associated nuclear protein which increases in maturing brain and in differentiating neuroblastoma 2A cells exposed to cyclic AMP-elevating agents.

E. Klann, K. Shelton, 1990, Brain research. Developmental brain research.

Low‐abundance 32‐kilodalton nuclear protein specifically enriched in the central nervous system

E. Klann, J. G. Cunningham, K. Shelton, 1990, Journal of neuroscience research.

The effect of lead on the metabolism of a nuclear matrix protein which becomes prominent in lead-induced intranuclear inclusion bodies.

E. Klann, K. Shelton, 1989, The Journal of biological chemistry.

Stress proteins are not induced in mammalian cells exposed to radiofrequency or microwave radiation.

S F Cleary, S. Cleary, L. M. Liu, 1997, Bioelectromagnetics.

On the variation of the major nuclear envelope (lamina) polypeptides.

D. Cochran, K. Shelton, V. Guthrie, 1980, Biochemical and biophysical research communications.

Analysis of the nuclear envelope polypeptides by isoelectric focusing and electrophoresis.

K. Shelton, P. M. Egle, 1979, Biochemical and biophysical research communications.

Supersensitivity to the reinforcing effects of cocaine following 6-hydroxydopamine lesions to the medial prefrontal cortex in rats

R. Peltier, S. Schenk, B. Horger, 1991, Brain Research.

The disposition of membrane polypeptides in stored blood.

K. Shelton, Keith A. Frey, 1975, Biochemical and biophysical research communications.

The acid-dependent conversion of major nuclear oligomeric polypeptides into a smaller species.

K. Shelton, 1978, Biochemical and biophysical research communications.

Comparison of the major polypeptides of the erythrocyte nuclear envelope.

D. Cochran, L. Yeoman, K. Shelton, 1979, Journal of supramolecular structure.