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Two Distinct Raf Domains Mediate Interaction with Ras

The Journal of biological chemistry, 1995-04, Vol.270 (17), p.9809-9812

1995

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Solution Structure and Dynamics of Ras p21.cntdot.GDP Determined by Heteronuclear Three- and Four-Dimensional NMR Spectroscopy

Biochemistry (Easton), 1994-03, Vol.33 (12), p.3515-3531

1994

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Solution structure and dynamics of Ras p21-GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy

Biochemistry (Easton), 1994-03, Vol.33 (12), p.3515-3531

1994

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Redox regulation of cell signalling

Nature (London), 1996-05, Vol.381 (6581), p.380-381

1996

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Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors

Molecular and Cellular Biology, 1994-02, Vol.14 (2), p.1113-1121

1994

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Structural and dynamic differences between normal and transforming N-ras gene products: a 31P and isotope-edited 1H NMR study

Biochemistry (Easton), 1989-11, Vol.28 (24), p.9478-9484

CAMPBELL-BURK, S

1989

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[1] Refolding and purification of ras proteins

Methods in Enzymology, 1995, Vol.255, p.3-13

1995

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Biomolecular applications of heteronuclear multidimensional NMR

Current opinion in biotechnology, 1994-08, Vol.5 (4), p.346-354

1994

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Biological and Structural Characterization of a Ras Transforming Mutation at the Phenylalanine-156 Residue, which is Conserved in all Members of the Ras Superfamily

Proceedings of the National Academy of Sciences - PNAS, 1995-02, Vol.92 (5), p.1272-1276

1995

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Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins

Journal of the American Chemical Society, 1992-03, Vol.114 (6), p.2262-2264

1992

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Structural and dynamic differences between normal and transforming N-ras gene products: a phosphorus-31 and isotope-edited proton NMR study

Biochemistry (Easton), 1989-11, Vol.28 (24), p.9478-9484

Campbell-Burk, Sharon

1989

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Identification of Resonances from an Oncogenic Activating Locus of Human N-RAS-Encoded p21 Protein Using Isotope-Edited NMR

Proceedings of the National Academy of Sciences - PNAS, 1989-02, Vol.86 (3), p.817-820

1989

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Secondary structure and signal assignments of human‐immunodeficiency‐virus‐1 protease complexed to a novel, structure‐based inhibitor

European journal of biochemistry, 1994-01, Vol.219 (1‐2), p.707-712

1994

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Improved 4D NMR experiments for the assignment of backbone nuclei in13C/15N labelled proteins

Journal of biomolecular NMR, 1992-11, Vol.2 (6), p.631-637

1992

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15N-correlated three-dimensional relayed NOESY experiments in uniformly 15N-labeled proteins

Journal of magnetic resonance (1969), 1992-02, Vol.96 (2), p.408-415

1992

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Observation of labile amide protons via indirect detection of 15N single-quantum transitions

Journal of magnetic resonance (1969), 1991-06, Vol.93 (1), p.171-177

1991

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Identification of Residues Critical for Ras(17N) Growth-Inhibitory Phenotype and for Ras Interaction with Guanine Nucleotide Exchange Factors

Molecular and cellular biology, 1994-02, Vol.14 (2), p.1113-1121

1994

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Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy

Journal of biomolecular NMR, 1992-11, Vol.2 (6), p.639-646

1992

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Two Distinct Raf Domains Mediate Interaction with Ras

Solution Structure and Dynamics of Ras p21.cntdot.GDP Determined by Heteronuclear Three- and Four-Dimensional NMR Spectroscopy

Solution structure and dynamics of Ras p21-GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy

Redox regulation of cell signalling

Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors

Structural and dynamic differences between normal and transforming N-ras gene products: a 31P and isotope-edited 1H NMR study

[1] Refolding and purification of ras proteins

Biomolecular applications of heteronuclear multidimensional NMR

Biological and Structural Characterization of a Ras Transforming Mutation at the Phenylalanine-156 Residue, which is Conserved in all Members of the Ras Superfamily

Four-dimensional heteronuclear triple resonance NMR methods for the assignment of backbone nuclei in proteins

Structural and dynamic differences between normal and transforming N-ras gene products: a phosphorus-31 and isotope-edited proton NMR study

Identification of Resonances from an Oncogenic Activating Locus of Human N-RAS-Encoded p21 Protein Using Isotope-Edited NMR

Secondary structure and signal assignments of human‐immunodeficiency‐virus‐1 protease complexed to a novel, structure‐based inhibitor

Improved 4D NMR experiments for the assignment of backbone nuclei in13C/15N labelled proteins

15N-correlated three-dimensional relayed NOESY experiments in uniformly 15N-labeled proteins

Observation of labile amide protons via indirect detection of 15N single-quantum transitions

Identification of Residues Critical for Ras(17N) Growth-Inhibitory Phenotype and for Ras Interaction with Guanine Nucleotide Exchange Factors

Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy

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