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A Novel DYT-5 Mutation with Phenotypic Variability within a Colombian Family.

Tremor and other hyperkinetic movements (New York, N.Y.)

Bernal-Pacheco O, Oyama G, Briton A, Singleton AB, Fernandez HH, Rodriguez RL, Malaty IA, Okun MS.
PMID: 24255805
Tremor Other Hyperkinet Mov (N Y). 2013 Oct 10;3. doi: 10.7916/D86W98SW. eCollection 2013.

BACKGROUND: DYT-5 dystonia usually presents as a dopa-responsive dystonia (DRD) with early or late parkinsonian manifestations and/or dystonic features. Genetically, these patients have been described as having a wide array of independent mutations in the guanosine triphosphate cyclohydrolase 1...

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Bernal-Pacheco O, Oyama G, Briton A, et al. A Novel DYT-5 Mutation with Phenotypic Variability within a Colombian Family. Tremor Other Hyperkinet Mov (N Y). 2013;3doi: 10.7916/D86W98SW.
Bernal-Pacheco, O., Oyama, G., Briton, A., Singleton, A. B., Fernandez, H. H., Rodriguez, R. L., Malaty, I. A., & Okun, M. S. (2013). A Novel DYT-5 Mutation with Phenotypic Variability within a Colombian Family. Tremor and other hyperkinetic movements (New York, N.Y.), 3. https://doi.org/10.7916/D86W98SW
Bernal-Pacheco, Oscar, et al. "A Novel DYT-5 Mutation with Phenotypic Variability within a Colombian Family." Tremor and other hyperkinetic movements (New York, N.Y.) vol. 3 (2013). doi: https://doi.org/10.7916/D86W98SW
Bernal-Pacheco O, Oyama G, Briton A, Singleton AB, Fernandez HH, Rodriguez RL, Malaty IA, Okun MS. A Novel DYT-5 Mutation with Phenotypic Variability within a Colombian Family. Tremor Other Hyperkinet Mov (N Y). 2013 Oct 10;3. doi: 10.7916/D86W98SW. eCollection 2013. PMID: 24255805; PMCID: PMC3822405.
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Prolonged activation of cAMP signaling leads to endothelial barrier disruption via transcriptional repression of RRAS.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Perrot CY, Sawada J, Komatsu M.
PMID: 29775418
FASEB J. 2018 May 18;fj201700818RRR. doi: 10.1096/fj.201700818RRR. Epub 2018 May 18.

The increase in cAMP levels in endothelial cells triggers cellular signaling to alter vascular permeability. It is generally considered that cAMP signaling stabilizes the endothelial barrier function and reduces permeability. However, previous studies have only examined the permeability shortly...

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Perrot CY, Sawada J, Komatsu M. Prolonged activation of cAMP signaling leads to endothelial barrier disruption via transcriptional repression of RRAS. FASEB J. 2018;fj201700818RRRdoi: 10.1096/fj.201700818RRR.
Perrot, C. Y., Sawada, J., & Komatsu, M. (2018). Prolonged activation of cAMP signaling leads to endothelial barrier disruption via transcriptional repression of RRAS. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, fj201700818RRR. https://doi.org/10.1096/fj.201700818RRR
Perrot, Carole Y, et al. "Prolonged activation of cAMP signaling leads to endothelial barrier disruption via transcriptional repression of RRAS." FASEB journal : official publication of the Federation of American Societies for Experimental Biology vol. (2018): fj201700818RRR. doi: https://doi.org/10.1096/fj.201700818RRR
Perrot CY, Sawada J, Komatsu M. Prolonged activation of cAMP signaling leads to endothelial barrier disruption via transcriptional repression of RRAS. FASEB J. 2018 May 18;fj201700818RRR. doi: 10.1096/fj.201700818RRR. Epub 2018 May 18. PMID: 29775418; PMCID: PMC6181640.
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Re-programming Hydrogel Properties Using a Fuel-Driven Reaction Cycle.

Journal of the American Chemical Society

Singh N, Lainer B, Formon GJM, De Piccoli S, Hermans TM.
PMID: 32065526
J Am Chem Soc. 2020 Mar 04;142(9):4083-4087. doi: 10.1021/jacs.9b11503. Epub 2020 Feb 21.

Nature uses catalysis as an indispensable tool to control assembly and reaction cycles in vital non-equilibrium supramolecular processes. For instance, enzymatic methionine oxidation regulates actin (dis-)assembly, and catalytic guanosine triphosphate hydrolysis is found in tubulin (dis-)assembly. Here we present...

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Singh N, Lainer B, Formon GJM, et al. Re-programming Hydrogel Properties Using a Fuel-Driven Reaction Cycle. J Am Chem Soc. 2020;142(9):4083-4087doi: 10.1021/jacs.9b11503.
Singh, N., Lainer, B., Formon, G. J. M., De Piccoli, S., & Hermans, T. M. (2020). Re-programming Hydrogel Properties Using a Fuel-Driven Reaction Cycle. Journal of the American Chemical Society, 142(9), 4083-4087. https://doi.org/10.1021/jacs.9b11503
Singh, Nishant, et al. "Re-programming Hydrogel Properties Using a Fuel-Driven Reaction Cycle." Journal of the American Chemical Society vol. 142,9 (2020): 4083-4087. doi: https://doi.org/10.1021/jacs.9b11503
Singh N, Lainer B, Formon GJM, De Piccoli S, Hermans TM. Re-programming Hydrogel Properties Using a Fuel-Driven Reaction Cycle. J Am Chem Soc. 2020 Mar 04;142(9):4083-4087. doi: 10.1021/jacs.9b11503. Epub 2020 Feb 21. PMID: 32065526.
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CD13 regulation of membrane recycling: implications for cancer dissemination.

Molecular & cellular oncology

Ghosh M, Shapiro LH.
PMID: 31692781
Mol Cell Oncol. 2019 Aug 09;6(6):e1648024. doi: 10.1080/23723556.2019.1648024. eCollection 2019.

Membrane recycling is critical to numerous cell functions and its dysregulation contributes to cancer and metastasis. We established that activation of the transmembrane molecule aminopeptidase N (ANPEP, also known as CD13) tethers the IQ motif containing, guanosine triphosphate hydrolase...

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Ghosh M, Shapiro LH. CD13 regulation of membrane recycling: implications for cancer dissemination. Mol Cell Oncol. 2019;6(6):e1648024doi: 10.1080/23723556.2019.1648024.
Ghosh, M., & Shapiro, L. H. (2019). CD13 regulation of membrane recycling: implications for cancer dissemination. Molecular & cellular oncology, 6(6), e1648024. https://doi.org/10.1080/23723556.2019.1648024
Ghosh, Mallika, and Shapiro, Linda H. "CD13 regulation of membrane recycling: implications for cancer dissemination." Molecular & cellular oncology vol. 6,6 (2019): e1648024. doi: https://doi.org/10.1080/23723556.2019.1648024
Ghosh M, Shapiro LH. CD13 regulation of membrane recycling: implications for cancer dissemination. Mol Cell Oncol. 2019 Aug 09;6(6):e1648024. doi: 10.1080/23723556.2019.1648024. eCollection 2019. PMID: 31692781; PMCID: PMC6816439.
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In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis.

Computers in biology and medicine

Gerber M, Goel S, Maitra R.
PMID: 34920161
Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09.

KRAS mutation is prevalent in around 30% of all cancers and is an undruggable molecular target. Of seven mutations at codon 12 and 13, only one, the G12C mutant is finally proven to be druggable, as evidenced by the...

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Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021;141:105110doi: 10.1016/j.compbiomed.2021.105110.
Gerber, M., Goel, S., & Maitra, R. (2021). In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Computers in biology and medicine, 141105110. https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber, Michael, et al. "In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis." Computers in biology and medicine vol. 141 (2021): 105110. doi: https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09. PMID: 34920161.
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In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis.

Computers in biology and medicine

Gerber M, Goel S, Maitra R.
PMID: 34920161
Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09.

KRAS mutation is prevalent in around 30% of all cancers and is an undruggable molecular target. Of seven mutations at codon 12 and 13, only one, the G12C mutant is finally proven to be druggable, as evidenced by the...

Cite
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021;141:105110doi: 10.1016/j.compbiomed.2021.105110.
Gerber, M., Goel, S., & Maitra, R. (2021). In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Computers in biology and medicine, 141105110. https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber, Michael, et al. "In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis." Computers in biology and medicine vol. 141 (2021): 105110. doi: https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09. PMID: 34920161.
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In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis.

Computers in biology and medicine

Gerber M, Goel S, Maitra R.
PMID: 34920161
Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09.

KRAS mutation is prevalent in around 30% of all cancers and is an undruggable molecular target. Of seven mutations at codon 12 and 13, only one, the G12C mutant is finally proven to be druggable, as evidenced by the...

Cite
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021;141:105110doi: 10.1016/j.compbiomed.2021.105110.
Gerber, M., Goel, S., & Maitra, R. (2021). In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Computers in biology and medicine, 141105110. https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber, Michael, et al. "In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis." Computers in biology and medicine vol. 141 (2021): 105110. doi: https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09. PMID: 34920161.
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Conformational switch that induces GDP release from Gi.

Journal of structural biology

Ham D, Ahn D, Ashim J, Cho Y, Kim HR, Yu W, Chung KY.
PMID: 33418033
J Struct Biol. 2021 Mar;213(1):107694. doi: 10.1016/j.jsb.2020.107694. Epub 2021 Jan 06.

Heterotrimeric guanine nucleotide-binding proteins (G proteins) are composed of α, β, and γ subunits. Gα switches between guanosine diphosphate (GDP)-bound inactive and guanosine triphosphate (GTP)-bound active states, and Gβγ interacts with the GDP-bound state. The GDP-binding regions are composed...

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Ham D, Ahn D, Ashim J, et al. Conformational switch that induces GDP release from Gi. J Struct Biol. 2021;213(1):107694doi: 10.1016/j.jsb.2020.107694.
Ham, D., Ahn, D., Ashim, J., Cho, Y., Kim, H. R., Yu, W., & Chung, K. Y. (2021). Conformational switch that induces GDP release from Gi. Journal of structural biology, 213(1), 107694. https://doi.org/10.1016/j.jsb.2020.107694
Ham, Donghee, et al. "Conformational switch that induces GDP release from Gi." Journal of structural biology vol. 213,1 (2021): 107694. doi: https://doi.org/10.1016/j.jsb.2020.107694
Ham D, Ahn D, Ashim J, Cho Y, Kim HR, Yu W, Chung KY. Conformational switch that induces GDP release from Gi. J Struct Biol. 2021 Mar;213(1):107694. doi: 10.1016/j.jsb.2020.107694. Epub 2021 Jan 06. PMID: 33418033.
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Lipid Profiles of RAS Nanoclusters Regulate RAS Function.

Biomolecules

Zhou Y, Hancock JF.
PMID: 34680072
Biomolecules. 2021 Sep 30;11(10). doi: 10.3390/biom11101439.

The lipid-anchored RAS (Rat sarcoma) small GTPases (guanosine triphosphate hydrolases) are highly prevalent in human cancer. Traditional strategies of targeting the enzymatic activities of RAS have been shown to be difficult. Alternatively, RAS function and pathology are mostly restricted...

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Zhou Y, Hancock JF. Lipid Profiles of RAS Nanoclusters Regulate RAS Function. Biomolecules. 2021;11(10)doi: 10.3390/biom11101439.
Zhou, Y., & Hancock, J. F. (2021). Lipid Profiles of RAS Nanoclusters Regulate RAS Function. Biomolecules, 11(10), . https://doi.org/10.3390/biom11101439
Zhou, Yong, and Hancock, John F. "Lipid Profiles of RAS Nanoclusters Regulate RAS Function." Biomolecules vol. 11,10 (2021). doi: https://doi.org/10.3390/biom11101439
Zhou Y, Hancock JF. Lipid Profiles of RAS Nanoclusters Regulate RAS Function. Biomolecules. 2021 Sep 30;11(10). doi: 10.3390/biom11101439. PMID: 34680072; PMCID: PMC8533076.
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In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis.

Computers in biology and medicine

Gerber M, Goel S, Maitra R.
PMID: 34920161
Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09.

KRAS mutation is prevalent in around 30% of all cancers and is an undruggable molecular target. Of seven mutations at codon 12 and 13, only one, the G12C mutant is finally proven to be druggable, as evidenced by the...

Cite
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021;141:105110doi: 10.1016/j.compbiomed.2021.105110.
Gerber, M., Goel, S., & Maitra, R. (2021). In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Computers in biology and medicine, 141105110. https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber, Michael, et al. "In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis." Computers in biology and medicine vol. 141 (2021): 105110. doi: https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09. PMID: 34920161.
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HER2 mediates clinical resistance to the KRAS.

European journal of cancer (Oxford, England : 1990)

Ho CSL, Tüns AI, Schildhaus HU, Wiesweg M, Grüner BM, Hegedus B, Schuler M, Schramm A, Oeck S.
PMID: 34715459
Eur J Cancer. 2021 Dec;159:16-23. doi: 10.1016/j.ejca.2021.10.003. Epub 2021 Oct 26.

INTRODUCTION: Mutant RAS guanosine triphosphate hydrolases (GTPases) are key oncogenic drivers in many cancers. The KRASMETHODS: A biopsy from progressing lung cancer of a patient treated with the KRASRESULTS: We demonstrated acquisition of HER2 copy number gain and KRASCONCLUSIONS:...

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Ho CSL, Tüns AI, Schildhaus HU, et al. HER2 mediates clinical resistance to the KRAS. Eur J Cancer. 2021;159:16-23doi: 10.1016/j.ejca.2021.10.003.
Ho, C. S. L., Tüns, A. I., Schildhaus, H. U., Wiesweg, M., Grüner, B. M., Hegedus, B., Schuler, M., Schramm, A., & Oeck, S. (2021). HER2 mediates clinical resistance to the KRAS. European journal of cancer (Oxford, England : 1990), 15916-23. https://doi.org/10.1016/j.ejca.2021.10.003
Ho, Cassandra S L, et al. "HER2 mediates clinical resistance to the KRAS." European journal of cancer (Oxford, England : 1990) vol. 159 (2021): 16-23. doi: https://doi.org/10.1016/j.ejca.2021.10.003
Ho CSL, Tüns AI, Schildhaus HU, Wiesweg M, Grüner BM, Hegedus B, Schuler M, Schramm A, Oeck S. HER2 mediates clinical resistance to the KRAS. Eur J Cancer. 2021 Dec;159:16-23. doi: 10.1016/j.ejca.2021.10.003. Epub 2021 Oct 26. PMID: 34715459.
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In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis.

Computers in biology and medicine

Gerber M, Goel S, Maitra R.
PMID: 34920161
Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09.

KRAS mutation is prevalent in around 30% of all cancers and is an undruggable molecular target. Of seven mutations at codon 12 and 13, only one, the G12C mutant is finally proven to be druggable, as evidenced by the...

Cite
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021;141:105110doi: 10.1016/j.compbiomed.2021.105110.
Gerber, M., Goel, S., & Maitra, R. (2021). In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Computers in biology and medicine, 141105110. https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber, Michael, et al. "In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis." Computers in biology and medicine vol. 141 (2021): 105110. doi: https://doi.org/10.1016/j.compbiomed.2021.105110
Gerber M, Goel S, Maitra R. In silico comparative analysis of KRAS mutations at codons 12 and 13: Structural modifications of P-Loop, switch I&II regions preventing GTP hydrolysis. Comput Biol Med. 2021 Dec 09;141:105110. doi: 10.1016/j.compbiomed.2021.105110. Epub 2021 Dec 09. PMID: 34920161.
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Showing 13 to 24 of 144 entries