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  • 1
    Electronic Resource
    Electronic Resource
    Reaction of (bromoacetamido)nucleoside affinity labels with ribonuclease A: evidence for steric control of reaction specificity and alkylation rate (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 135-146 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00375a020
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  • 2
    Electronic Resource
    Electronic Resource
    The High-Risk Occupational Disease Notification and Prevention Act (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 572 (1989), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1989.tb13591.x
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  • 3
    Electronic Resource
    Electronic Resource
    Structural effects of amino acid substitutions on the P21 proteins: Evidence for a malignant conformation (1985)
    Springer
    The protein journal 4 (1985), S. 353-362 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; three-dimensional structure ; amino acid substitution ; P21 proteins ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The conformational effects of different amino acid substitutions for Gly at position 12 in theras-oncogene-encoded P21 proteins have been investigated using conformational energy calculations. Mutations that cause amino acid substitutions for Gly 12 result in a protein that produces malignant transformation of cells. It had previously been shown that substitution of Val, Lys, or Ser for Gly at position 12 results in a major conformational change, and that the preferred lowest energy structure for each of the substituted peptides is identical. It is now found that substitution for Gly 12 of other amino acids that have widely disparate helix-nucleating potentials and completely different side chains (Asp, Asn, Cys, Phe, Tle, Leu, and Ala) all produce this identical lowest energy conformation. This finding is consistent with the recent results of site-specific mutagenesis experiments showing that P21 proteins containing these amino acids at position 12 all promote malignant transformation of cells and suggests the existence of a “malignancy-causing” conformation for the P21 proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025176
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  • 4
    Electronic Resource
    Electronic Resource
    Correlation of structure with transforming activity of the P21 proteins with substitutions at positions 12 and 16 (1987)
    Springer
    The protein journal 6 (1987), S. 375-385 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; three-dimensional structure ; amino acid substitutions ; P21 proteins ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structural effects of amino acid substitutions at positions 12 and 16 in the amino-terminal segment (Tyr 4-Ala 18) of the ras-oncogene-encoded P21 proteins have been investigated using conformational energy analysis. The P21 protein with Val at position 12 and Lys at position 16 is known to have high transforming ability, while the P21 protein with Val at position 12 and Asn at position 16 is known to have poor transforming ability, similar to that of the normal protein (with Gly at 12 and Lys at 16.) The current results demonstrate a significant conformational change at position 15 induced by the substitution of Asn for Lys at position 16, which could explain this alteration in transformation potential. These findings are consistent with previous results suggesting the existence of a normal and a malignancy-causing conformation for the P21 proteins and suggest that the critical transforming region may encompass residues 12–15.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02343336
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  • 5
    Electronic Resource
    Electronic Resource
    Structural effects of amino acid substitutions on the matrix protein of vesicular stomatitis virus (1987)
    Springer
    The protein journal 6 (1987), S. 463-472 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; three-dimensional structure ; amino acid substitutions ; matrix protein ; vesicular stomatitis virus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structural effects of amino acid substitutions for Gly at position 21 in the amino-terminal segment (Lys 15-Pro 26) of the matrix (M) protein of vesicular stomatitis virus (VSV) have been investigated using conformational energy analysis. Monoclonal antibody-binding experiments and protein digestion studies of the M protein indicate that this segment is important to its ribonucleoprotein recognition and its transcription-inhibitory activity. Temperaturesensitive mutants of VSV that do not bind monoclonal antibody and that are devoid of transcription-inhibitory activity are known to have the substitution of Glu for Gly at position 21. The current findings demonstrate a significant conformational change at position 21 induced by the substitution of Glu for Gly, which could explain this alteration in antibody binding and transcription-inhibitory activity. Furthermore, the results indicate that the substitution of any noncyclic L-amino acid for Gly at position 21 may be expected to produce similar changes in M protein function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276732
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  • 6
    Electronic Resource
    Electronic Resource
    Conformational effects of the substitution of ARG for GLY 13 in theras oncogene-encoded P21 protein (1988)
    Springer
    The protein journal 7 (1988), S. 349-354 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; amino acid substitution ; position 13 ; P21 protein ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The effect of the substitution of Arg for Gly 13 on the structure of the transforming region decapeptide (Leu 6-Gly 15) of the ras oncogene encoded P21 protein has been investigated using conformational energy analysis. A human malignancy has been identified that contains a ras gene with a single mutation in the thirteenth codon such that the encoded protein would have Arg substituted for Gly at this position, and transfection of cells in culture with this gene results in malignant transformation. Conformational analysis demonstrates that the Arg 13 decapeptide adopts a conformation identical to that for other peptides with substitutions at position 13 (Asp 13, Val 13) from transforming proteins that is distinctively different from that for peptides (Gly 13, Ser 13) from normal, nontransforming proteins. This is found to be an indirect effect resulting from changes in the conformation of Gly 12 produced by substitutions at position 13. These results are consistent with recent analysis of crystallographic data of proteins on conformational preferences for glycine in tripeptide sequences.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024884
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  • 7
    Electronic Resource
    Electronic Resource
    Conformational energy analysis of the leucine repeat regions of C/EBP, GCN4, and the proteins of themyc, jun, andfos oncogenes (1989)
    Springer
    The protein journal 8 (1989), S. 679-688 
    Details
    ISSN: 1573-4943
    Keywords: amphipathic helix ; leucine zipper ; DNA binding proteins ; conformational energy analysis ; three-dimensional structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract It has been recently proposed that certain DNA binding proteins (including C/EBP, GCN4 and themyc, jun, andfos oncogene proteins) share a common structural motif based on helix-promoting regions containing heptad repeat sequences of leucines. It has been suggested that this structure is critical to the biological activity of these proteins, since it facilitates the formation of functional dimers held together by interdigitating leucine side-chains along the hydrophobic interfaces between long α-helical regions of the polypeptide chains in a configuration termed the “leucine zipper.” In this paper, conformational energy analysis is used to determine the preferred three-dimensional structures of the leucine repeat regions of these proteins. The results indicate that, in all cases, the global minimum energy conformation for these regions is an amphipathic α-helix with the leucine side-chains arrayed on one side in such a way to favor “leucine zipper” dimerization. Furthermore, amino acid substitutions in these regions (such as Pro for Leu), that are known to inhibit dimer formation and prevent DNA binding, are found to produce significant conformational changes that disrupt the amphipathic helical structure. Thus, these results provide support for the proposed “leucine zipper” configuration as a critical structural feature of this class of DNA binding proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025608
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  • 8
    Electronic Resource
    Electronic Resource
    Identification of the Site of Inhibition of Oncogenic ras–p21-Induced Signal Transduction by a Peptide from a ras Effector Domain (1999)
    Springer
    The protein journal 18 (1999), S. 881-884 
    Details
    ISSN: 1573-4943
    Keywords: p21 35–47 peptide ; raf inhibition ; JNK and jun ; selective inhibition of oncogenic ras–p21
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We have previously found that a peptide corresponding to residues 35–47 of the ras-p21 protein, from its switch 1 effector domain region, strongly inhibits oocyte maturation induced by oncogenic p21, but not by insulin-activated cellular wild-type p21. Another ras–p21 peptide corresponding to residues 96–110 that blocks ras–jun and jun kinase (JNK) interactions exhibits a similar pattern of inhibition. We have also found that c-raf strongly induces oocyte maturation and that dominant negative c-raf strongly blocks oncogenic p21-induced oocyte maturation. We now find that the p21 35–47, but not the 96–110, peptide completely blocks c-raf-induced maturation. This finding suggests that the 35–47 peptide blocks oncogenic ras at the level of raf; that activated normal and oncogenic ras–p21 have differing requirements for raf-dependent signaling; and that the two oncogenic-ras-selective inhibitory peptides, 35–47 and 96–110, act at two different critical downstream sites, the former at raf, the latter at JNK/jun, both of which are required for oncogenic ras-p21 signaling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020635414089
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  • 9
    Electronic Resource
    Electronic Resource
    Inhibition of Oncogenic and Activated Wild-Type ras–p21 Protein-Induced Oocyte Maturation by Peptides from the Guanine-Nucleotide Exchange Protein, SOS, Identified from Molecular Dynamics Calculations. Selective Inhibition of Oncogenic ras–p21 (1999)
    Springer
    The protein journal 18 (1999), S. 875-879 
    Details
    ISSN: 1573-4943
    Keywords: ras–p21–SOS complex ; effector domain ; oocyte maturation ; inhibitory peptides ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In the preceding paper we performed molecular dynamics calculations of the average structures of the SOS protein bound to wild-type and oncogenic ras–p21. Based on these calculations, we have identified four major domains of the SOS protein, consisting of residues 631–641, 676–691, 718–729, and 994–1004, which differ in structure between the two complexes. We have now microinjected synthetic peptides corresponding to each of these domains into Xenopus laevis oocytes either together with oncogenic (Val 12)-p21 or into oocytes subsequently incubated with insulin. We find that the first three peptides inhibit both oncogenic and wild-type p21-induced oocyte maturation, while the last peptide much more strongly inhibits oncogenic p21 protein-induced oocyte maturation. These results suggest that each identified SOS region is involved in ras–stimulated signal transduction and that the 994–1004 domain is involved uniquely with oncogenic ras–p21 signaling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020683330019
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  • 10
    Electronic Resource
    Electronic Resource
    The structure of the carboxyl terminus of the p21 protein. Structural relationship to the nucleotide-binding/transforming regions of the protein (1990)
    Springer
    The protein journal 9 (1990), S. 137-142 
    Details
    ISSN: 1573-4943
    Keywords: ras Oncogene-encoded p21 protein ; C-terminus ; membrane binding ; cell transformation ; helical hairpin conformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The carboxyl-terminal region of theras oncogene-encoded p21 protein is critical to the protein's function, since membrane binding through the C-terminus is necessary for its cellular activity. X-ray crystal structures for truncated p21 proteins are available, but none of these include the C-terminal region of the protein (from residues 172–189). Using conformational energy analysis, we determined the preferred three-dimensional structures for this C-terminal octadecapeptide of the H-ras oncogene p21 protein and generated these structures onto the crystal structure of the remainder of the protein. The results indicate that, like other membrane-associated proteins, the membrane-binding C-terminus of p21 assumes a helical hairpin conformation. In several low-energy orientations, the C-terminal structure is in close proximity to other critical locales of p21. These include the central transforming region (around Gln 61) and the amino terminal transforming region (around Gly 12), indicating that extracellular signals can be transduced through the C-terminal helical hairpin to the effector regions of the protein. This finding is consistent with the results of recent genetic experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025304
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