Sequential assignment of the backbone nuclei (1H,15N and13C) of c-H-ras p21 (1–166).GDP using a novel 4D NMR strategy

1992 ◽  
Vol 2 (6) ◽  
pp. 639-646 ◽  
Author(s):  
Sharon L. Campbell-Burka ◽  
Peter J. Domaillea ◽  
Melissa A. Starovasnik ◽  
Wayne Boucher ◽  
Ernest D. Laue
Keyword(s):  
Sequential Assignment ◽  
Ras P21 ◽  
4D Nmr

Sequential assignment of NMR spectra of peptides at natural isotopic abundance with Zero and Ultra-Low Field-TOCSY

2021 ◽  
Author(s):  
Alexey S. Kiryutin ◽  
Ivan V. Zhukov ◽  
Fabien Ferrage ◽  
G Bodenhausen ◽  
Alexandra V. Yurkovskaya ◽  
...  
Keyword(s):  
High Field ◽  
Nmr Spectra ◽  
Correlation Spectroscopy ◽  
Sequential Assignment ◽  
Isotopic Abundance ◽  
Natural Isotopic Abundance ◽  
Low Field ◽  
Total Correlation ◽  
High Resolution Nmr ◽  
Novel Method

A novel method dubbed ZULF-TOCSY results from the combination of Zero and Ultra-Low Field (ZULF) with high-field, high-resolution NMR, leading to a generalization of the concept of total correlation spectroscopy...

RAS p21 and other Gn proteins are detected in mammalian cell lines by [γ-35S]GTPγS binding

1989 ◽  
Vol 159 (3) ◽  
pp. 1269-1274 ◽  
Author(s):  
J.G. Comerford ◽  
J.R. Gibson ◽  
A.P. Dawson ◽  
I. Gibson
Keyword(s):  
Cell Lines ◽  
Mammalian Cell ◽  
Mammalian Cell Lines ◽  
Gtpγs Binding ◽  
Ras P21

scholarly journals ras Oncogene p21 expression is increased in premalignant lesions and high grade bladder carcinoma.

1985 ◽  
Vol 161 (5) ◽  
pp. 1213-1218 ◽  
Author(s):  
M V Viola ◽  
F Fromowitz ◽  
S Oravez ◽  
S Deb ◽  
J Schlom
Keyword(s):  
Bladder Carcinoma ◽  
Premalignant Lesions ◽  
Low Grade ◽  
Staining Reaction ◽  
High Grade ◽  
Ras Oncogene ◽  
Intense Staining ◽  
Bladder Urothelium ◽  
Normal Bladder ◽  
Ras P21

ras Oncogene p21 antigen is present in the most superficial cells of the normal bladder urothelium, as demonstrated by immunohistochemical staining. The pattern and intensity of p21 staining of cells in epithelial hyperplasia and low grade bladder carcinoma were similar to that seen in the normal urothelium. In contrast, epithelial cells in "premalignant" (dysplastic) lesions and high grade carcinomas exhibited an intense staining reaction for p21 antigen. ras p21 may be a useful marker for the malignant potential of both premalignant lesions and carcinomas of the bladder.

Proton NMR studies of transforming and nontransforming H-ras p21 mutants

Biochemistry ◽  
1990 ◽  
Vol 29 (2) ◽  
pp. 504-511 ◽  
Author(s):  
Ilme Schlichting ◽  
Jacob John ◽  
Mathias Frech ◽  
Pierre Chardin ◽  
Alfred Wittinghofer ◽  
...  
Keyword(s):  
Proton Nmr ◽  
Nmr Studies ◽  
Ras P21

An isotope edited classical Raman difference spectroscopic study of the interactions of guanine nucleotides with elongation factor Tu and H-ras p21

Biochemistry ◽  
1991 ◽  
Vol 30 (45) ◽  
pp. 10914-10920 ◽  
Author(s):  
Danny Manor ◽  
Gezhi Weng ◽  
Hua Deng ◽  
Sharon Cosloy ◽  
Cun Xiang Chen ◽  
...  
Keyword(s):  
Spectroscopic Study ◽  
Elongation Factor ◽  
Guanine Nucleotides ◽  
Elongation Factor Tu ◽  
Ras P21

ralGDS family members interact with the effector loop of ras p21

1994 ◽  
Vol 14 (11) ◽  
pp. 7483-7491
Author(s):  
A Kikuchi ◽  
S D Demo ◽  
Z H Ye ◽  
Y W Chen ◽  
L T Williams
Keyword(s):  
Hybrid System ◽  
Family Members ◽  
Dominant Negative Mutant ◽  
Yeast Two Hybrid ◽  
Amino Acid Homology ◽  
Yeast Two Hybrid System ◽  
Ras P21 ◽  
Two Hybrid ◽  
Interacting Domain

Using a yeast two-hybrid system, we identified a novel protein which interacts with ras p21. This protein shares 69% amino acid homology with ral guanine nucleotide dissociation stimulator (ralGDS), a GDP/GTP exchange protein for ral p24. We designated this protein RGL, for ralGDS-like. Using the yeast two-hybrid system, we found that an effector loop mutant of ras p21 was defective in interacting with the ras p21-interacting domain of RGL, suggesting that this domain binds to ras p21 through the effector loop of ras p21. Since ralGDS contained a region highly homologous with the ras p21-interacting domain of RGL, we examined whether ralGDS could interact with ras p21. In the yeast two-hybrid system, ralGDS failed to interact with an effector loop mutant of ras p21. In insect cells, ralGDS made a complex with v-ras p21 but not with a dominant negative mutant of ras p21. ralGDS interacted with the GTP-bound form of ras p21 but not with the GDP-bound form in vitro. ralGDS inhibited both the GTPase-activating activity of the neurofibromatosis gene product (NF1) for ras p21 and the interaction of Raf with ras p21 in vitro. These results demonstrate that ralGDS specifically interacts with the active form of ras p21 and that ralGDS can compete with NF1 and Raf for binding to the effector loop of ras p21. Therefore, ralGDS family members may be effector proteins of ras p21 or may inhibit interactions between ras p21 and its effectors.

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