A novel family of Ras-binding domains (Q48058077)

8 February 2018

http://europepmc.org/abstract/MED/8987396

title

A novel family of Ras-binding domains (English)

1 reference

8 February 2018

http://europepmc.org/abstract/MED/8987396

author

Chris Ponting

series ordinal

1

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8 February 2018

http://europepmc.org/abstract/MED/8987396

author name string

D R Benjamin

series ordinal

2

1 reference

8 February 2018

http://europepmc.org/abstract/MED/8987396

publication date

1 November 1996

1 reference

8 February 2018

http://europepmc.org/abstract/MED/8987396

number of pages

4

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Trends in Biochemical Sciences

inferred from page(s)

published in

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8 February 2018

http://europepmc.org/abstract/MED/8987396

volume

21

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8 February 2018

http://europepmc.org/abstract/MED/8987396

issue

11

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8 February 2018

http://europepmc.org/abstract/MED/8987396

page(s)

422-425

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8 February 2018

http://europepmc.org/abstract/MED/8987396

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Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap

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A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1

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Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation

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Theste4+ gene, essential for sexual differentiation ofSchizosaccharomyces pombe, encodes a protein with a leucine zipper motif

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The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue

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SAM: a novel motif in yeast sterile and Drosophila polyhomeotic proteins

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Protein kinase C. Seeing two domains

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7 January 2021

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Identifiers

DOI

1 reference

8 February 2018

http://europepmc.org/abstract/MED/8987396

1 reference

8 February 2018