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Showing 1 to 12 of 154 entries
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RasGRP Ras guanine nucleotide exchange factors in cancer.

Frontiers in biology

Ksionda O, Limnander A, Roose JP.
PMID: 24744772
Front Biol (Beijing). 2013 Oct 01;8(5):508-532. doi: 10.1007/s11515-013-1276-9.

RasGRP proteins are activators of Ras and other related small GTPases by the virtue of functioning as guanine nucleotide exchange factors (GEFs). In vertebrates, four RasGRP family members have been described. RasGRP-1 through -4 share many structural domains but...

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Ksionda O, Limnander A, Roose JP. RasGRP Ras guanine nucleotide exchange factors in cancer. Front Biol (Beijing). 2013;8(5):508-532doi: 10.1007/s11515-013-1276-9.
Ksionda, O., Limnander, A., & Roose, J. P. (2013). RasGRP Ras guanine nucleotide exchange factors in cancer. Frontiers in biology, 8(5), 508-532. https://doi.org/10.1007/s11515-013-1276-9
Ksionda, Olga, et al. "RasGRP Ras guanine nucleotide exchange factors in cancer." Frontiers in biology vol. 8,5 (2013): 508-532. doi: https://doi.org/10.1007/s11515-013-1276-9
Ksionda O, Limnander A, Roose JP. RasGRP Ras guanine nucleotide exchange factors in cancer. Front Biol (Beijing). 2013 Oct 01;8(5):508-532. doi: 10.1007/s11515-013-1276-9. PMID: 24744772; PMCID: PMC3987922.
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Roles of Rap1 signaling in tumor cell migration and invasion.

Cancer biology & medicine

Zhang YL, Wang RC, Cheng K, Ring BZ, Su L.
PMID: 28443208
Cancer Biol Med. 2017 Feb;14(1):90-99. doi: 10.20892/j.issn.2095-3941.2016.0086.

Ras-associated protein-1 (Rap1), a small GTPase in the Ras-related protein family, is an important regulator of basic cellular functions (e.g., formation and control of cell adhesions and junctions), cellular migration, and polarization. Through its interaction with other proteins, Rap1...

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Zhang YL, Wang RC, Cheng K, et al. Roles of Rap1 signaling in tumor cell migration and invasion. Cancer Biol Med. 2017;14(1):90-99doi: 10.20892/j.issn.2095-3941.2016.0086.
Zhang, Y. L., Wang, R. C., Cheng, K., Ring, B. Z., & Su, L. (2017). Roles of Rap1 signaling in tumor cell migration and invasion. Cancer biology & medicine, 14(1), 90-99. https://doi.org/10.20892/j.issn.2095-3941.2016.0086
Zhang, Yi-Lei, et al. "Roles of Rap1 signaling in tumor cell migration and invasion." Cancer biology & medicine vol. 14,1 (2017): 90-99. doi: https://doi.org/10.20892/j.issn.2095-3941.2016.0086
Zhang YL, Wang RC, Cheng K, Ring BZ, Su L. Roles of Rap1 signaling in tumor cell migration and invasion. Cancer Biol Med. 2017 Feb;14(1):90-99. doi: 10.20892/j.issn.2095-3941.2016.0086. PMID: 28443208; PMCID: PMC5365179.
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Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways.

Cellular logistics

Lipatova Z, Segev N.
PMID: 25610722
Cell Logist. 2014 Jul 03;4(3):e954870. doi: 10.4161/21592780.2014.954870. eCollection 2014.

A prevailing question in the Ypt/Rab field is whether these conserved GTPases are specific to cellular compartments. The established role for Ypt1 and its human homolog Rab1 is in endoplasmic reticulum (ER)-to-Golgi transport. More recently these regulators were implicated...

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Lipatova Z, Segev N. Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways. Cell Logist. 2014;4(3):e954870doi: 10.4161/21592780.2014.954870.
Lipatova, Z., & Segev, N. (2014). Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways. Cellular logistics, 4(3), e954870. https://doi.org/10.4161/21592780.2014.954870
Lipatova, Zhanna, and Segev, Nava. "Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways." Cellular logistics vol. 4,3 (2014): e954870. doi: https://doi.org/10.4161/21592780.2014.954870
Lipatova Z, Segev N. Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways. Cell Logist. 2014 Jul 03;4(3):e954870. doi: 10.4161/21592780.2014.954870. eCollection 2014. PMID: 25610722; PMCID: PMC4279804.
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Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame.

Biochimica et biophysica acta

Gentry LR, Martin TD, Reiner DJ, Der CJ.
PMID: 25219551
Biochim Biophys Acta. 2014 Dec;1843(12):2976-2988. doi: 10.1016/j.bbamcr.2014.09.004. Epub 2014 Sep 16.

Since their discovery in 1986, Ral (Ras-like) GTPases have emerged as critical regulators of diverse cellular functions. Ral-selective guanine nucleotide exchange factors (RalGEFs) function as downstream effectors of the Ras oncoprotein, and the RalGEF-Ral signaling network comprises the third...

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Gentry LR, Martin TD, Reiner DJ, et al. Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame. Biochim Biophys Acta. 2014;1843(12):2976-2988doi: 10.1016/j.bbamcr.2014.09.004.
Gentry, L. R., Martin, T. D., Reiner, D. J., & Der, C. J. (2014). Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame. Biochimica et biophysica acta, 1843(12), 2976-2988. https://doi.org/10.1016/j.bbamcr.2014.09.004
Gentry, Leanna R, et al. "Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame." Biochimica et biophysica acta vol. 1843,12 (2014): 2976-2988. doi: https://doi.org/10.1016/j.bbamcr.2014.09.004
Gentry LR, Martin TD, Reiner DJ, Der CJ. Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame. Biochim Biophys Acta. 2014 Dec;1843(12):2976-2988. doi: 10.1016/j.bbamcr.2014.09.004. Epub 2014 Sep 16. PMID: 25219551; PMCID: PMC4201770.
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Dock10, a Cdc42 and Rac1 GEF, induces loss of elongation, filopodia, and ruffles in cervical cancer epithelial HeLa cells.

Biology open

Ruiz-Lafuente N, Alcaraz-García MJ, García-Serna AM, Sebastián-Ruiz S, Moya-Quiles MR, García-Alonso AM, Parrado A.
PMID: 25862245
Biol Open. 2015 Apr 10;4(5):627-35. doi: 10.1242/bio.20149050.

Dock10 is one of the three members of the Dock-D family of Dock proteins, a class of guanine nucleotide exchange factors (GEFs) for Rho GTPases. Its homologs Dock9 and Dock11 are Cdc42 GEFs. Dock10 is required for maintenance of...

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Ruiz-Lafuente N, Alcaraz-García MJ, García-Serna AM, et al. Dock10, a Cdc42 and Rac1 GEF, induces loss of elongation, filopodia, and ruffles in cervical cancer epithelial HeLa cells. Biol Open. 2015;4(5):627-35doi: 10.1242/bio.20149050.
Ruiz-Lafuente, N., Alcaraz-García, M. J., García-Serna, A. M., Sebastián-Ruiz, S., Moya-Quiles, M. R., García-Alonso, A. M., & Parrado, A. (2015). Dock10, a Cdc42 and Rac1 GEF, induces loss of elongation, filopodia, and ruffles in cervical cancer epithelial HeLa cells. Biology open, 4(5), 627-35. https://doi.org/10.1242/bio.20149050
Ruiz-Lafuente, Natalia, et al. "Dock10, a Cdc42 and Rac1 GEF, induces loss of elongation, filopodia, and ruffles in cervical cancer epithelial HeLa cells." Biology open vol. 4,5 (2015): 627-35. doi: https://doi.org/10.1242/bio.20149050
Ruiz-Lafuente N, Alcaraz-García MJ, García-Serna AM, Sebastián-Ruiz S, Moya-Quiles MR, García-Alonso AM, Parrado A. Dock10, a Cdc42 and Rac1 GEF, induces loss of elongation, filopodia, and ruffles in cervical cancer epithelial HeLa cells. Biol Open. 2015 Apr 10;4(5):627-35. doi: 10.1242/bio.20149050. PMID: 25862245; PMCID: PMC4434814.
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The cytohesin guanosine exchange factors (GEFs) are required to promote HGF-mediated renal recovery after acute kidney injury (AKI) in mice.

Physiological reports

Reviriego-Mendoza MM, Santy LC.
PMID: 26116550
Physiol Rep. 2015 Jun;3(6). doi: 10.14814/phy2.12442.

The lack of current treatment and preventable measures for acute kidney injury (AKI) in hospitalized patients results in an increased mortality rate of up to 80% and elevated health costs. Additionally, if not properly repaired, those who survive AKI...

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Reviriego-Mendoza MM, Santy LC. The cytohesin guanosine exchange factors (GEFs) are required to promote HGF-mediated renal recovery after acute kidney injury (AKI) in mice. Physiol Rep. 2015;3(6)doi: 10.14814/phy2.12442.
Reviriego-Mendoza, M. M., & Santy, L. C. (2015). The cytohesin guanosine exchange factors (GEFs) are required to promote HGF-mediated renal recovery after acute kidney injury (AKI) in mice. Physiological reports, 3(6), . https://doi.org/10.14814/phy2.12442
Reviriego-Mendoza, Marta M, and Santy, Lorraine C. "The cytohesin guanosine exchange factors (GEFs) are required to promote HGF-mediated renal recovery after acute kidney injury (AKI) in mice." Physiological reports vol. 3,6 (2015). doi: https://doi.org/10.14814/phy2.12442
Reviriego-Mendoza MM, Santy LC. The cytohesin guanosine exchange factors (GEFs) are required to promote HGF-mediated renal recovery after acute kidney injury (AKI) in mice. Physiol Rep. 2015 Jun;3(6). doi: 10.14814/phy2.12442. PMID: 26116550; PMCID: PMC4522160.
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Rac inhibits thrombin-induced Rho activation: evidence of a Pak-dependent GTPase crosstalk.

Journal of molecular signaling

Rosenfeldt H, Castellone MD, Randazzo PA, Gutkind JS.
PMID: 17224083
J Mol Signal. 2006 Dec 06;1:8. doi: 10.1186/1750-2187-1-8.

The strict spatio-temporal control of Rho GTPases is critical for many cellular functions, including cell motility, contractility, and growth. In this regard, the prototypical Rho family GTPases, Rho, Rac, and Cdc42 regulate the activity of each other by a...

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Rosenfeldt H, Castellone MD, Randazzo PA, et al. Rac inhibits thrombin-induced Rho activation: evidence of a Pak-dependent GTPase crosstalk. J Mol Signal. 2006;1:8doi: 10.1186/1750-2187-1-8.
Rosenfeldt, H., Castellone, M. D., Randazzo, P. A., & Gutkind, J. S. (2006). Rac inhibits thrombin-induced Rho activation: evidence of a Pak-dependent GTPase crosstalk. Journal of molecular signaling, 18. https://doi.org/10.1186/1750-2187-1-8
Rosenfeldt, Hans, et al. "Rac inhibits thrombin-induced Rho activation: evidence of a Pak-dependent GTPase crosstalk." Journal of molecular signaling vol. 1 (2006): 8. doi: https://doi.org/10.1186/1750-2187-1-8
Rosenfeldt H, Castellone MD, Randazzo PA, Gutkind JS. Rac inhibits thrombin-induced Rho activation: evidence of a Pak-dependent GTPase crosstalk. J Mol Signal. 2006 Dec 06;1:8. doi: 10.1186/1750-2187-1-8. PMID: 17224083; PMCID: PMC1769496.
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An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand.

Cell communication and signaling : CCS

Wilsbacher JL, Moores SL, Brugge JS.
PMID: 16709244
Cell Commun Signal. 2006 May 18;4:5. doi: 10.1186/1478-811X-4-5.

BACKGROUND: Vav proteins are guanine nucleotide exchange factors (GEF) for Rho family GTPases and are activated following engagement of membrane receptors. Overexpression of Vav proteins enhances lamellipodium and ruffle formation, migration, and cell spreading, and augments activation of many...

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Wilsbacher JL, Moores SL, Brugge JS. An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand. Cell Commun Signal. 2006;4:5doi: 10.1186/1478-811X-4-5.
Wilsbacher, J. L., Moores, S. L., & Brugge, J. S. (2006). An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand. Cell communication and signaling : CCS, 45. https://doi.org/10.1186/1478-811X-4-5
Wilsbacher, Julie L, et al. "An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand." Cell communication and signaling : CCS vol. 4 (2006): 5. doi: https://doi.org/10.1186/1478-811X-4-5
Wilsbacher JL, Moores SL, Brugge JS. An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand. Cell Commun Signal. 2006 May 18;4:5. doi: 10.1186/1478-811X-4-5. PMID: 16709244; PMCID: PMC1524963.
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Grhl3 and GEF19 in the front rho.

Small GTPases

Darido C, Jane SM.
PMID: 21686262
Small GTPases. 2010 Sep;1(2):104-107. doi: 10.4161/sgtp.1.2.13620.

Directional migration is a critical component of cell motility is observed in many diverse processes including embryogenesis, immune surveillance and wound repair. A central aspect of directional migration is cellular polarity, which is established through several signaling pathways that...

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Darido C, Jane SM. Grhl3 and GEF19 in the front rho. Small GTPases. 2010;1(2):104-107doi: 10.4161/sgtp.1.2.13620.
Darido, C., & Jane, S. M. (2010). Grhl3 and GEF19 in the front rho. Small GTPases, 1(2), 104-107. https://doi.org/10.4161/sgtp.1.2.13620
Darido, Charbel, and Jane, Stephen M. "Grhl3 and GEF19 in the front rho." Small GTPases vol. 1,2 (2010): 104-107. doi: https://doi.org/10.4161/sgtp.1.2.13620
Darido C, Jane SM. Grhl3 and GEF19 in the front rho. Small GTPases. 2010 Sep;1(2):104-107. doi: 10.4161/sgtp.1.2.13620. PMID: 21686262; PMCID: PMC3116594.
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Identification and comparative analysis of novel alternatively spliced transcripts of RhoGEF domain encoding gene in C. elegans and C. briggsae.

Bioinformation

Kashyap L, Tabish M, Ganesh S, Dubey D.
PMID: 18188419
Bioinformation. 2007 Sep 11;2(2):43-9. doi: 10.6026/97320630002043.

Y95B8A.12 gene of C. elegans encodes RhoGEF domain, which is a novel module in the Guanine nucleotide exchange factors (GEFs). Alternative splicing increases transcriptome and proteome diversification. Y95B8A.12 gene has two reported alternatively spliced transcripts by the C. elegans...

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Kashyap L, Tabish M, Ganesh S, et al. Identification and comparative analysis of novel alternatively spliced transcripts of RhoGEF domain encoding gene in C. elegans and C. briggsae. Bioinformation. 2007;2(2):43-9doi: 10.6026/97320630002043.
Kashyap, L., Tabish, M., Ganesh, S., & Dubey, D. (2007). Identification and comparative analysis of novel alternatively spliced transcripts of RhoGEF domain encoding gene in C. elegans and C. briggsae. Bioinformation, 2(2), 43-9. https://doi.org/10.6026/97320630002043
Kashyap, Luv, et al. "Identification and comparative analysis of novel alternatively spliced transcripts of RhoGEF domain encoding gene in C. elegans and C. briggsae." Bioinformation vol. 2,2 (2007): 43-9. doi: https://doi.org/10.6026/97320630002043
Kashyap L, Tabish M, Ganesh S, Dubey D. Identification and comparative analysis of novel alternatively spliced transcripts of RhoGEF domain encoding gene in C. elegans and C. briggsae. Bioinformation. 2007 Sep 11;2(2):43-9. doi: 10.6026/97320630002043. PMID: 18188419; PMCID: PMC2174416.
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Dock protein family in brain development and neurological disease.

Communicative & integrative biology

Shi L.
PMID: 24563715
Commun Integr Biol. 2013 Nov 01;6(6):e26839. doi: 10.4161/cib.26839. Epub 2013 Nov 13.

The family of dedicator of cytokinesis (Dock), a protein family that belongs to the atypical Rho guanine nucleotide exchange factors (GEFs) for Rac and/or Cdc42 GTPases, plays pivotal roles in various processes of brain development. To date, 11 members...

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Shi L. Dock protein family in brain development and neurological disease. Commun Integr Biol. 2013;6(6):e26839doi: 10.4161/cib.26839.
Shi, L. (2013). Dock protein family in brain development and neurological disease. Communicative & integrative biology, 6(6), e26839. https://doi.org/10.4161/cib.26839
Shi, Lei. "Dock protein family in brain development and neurological disease." Communicative & integrative biology vol. 6,6 (2013): e26839. doi: https://doi.org/10.4161/cib.26839
Shi L. Dock protein family in brain development and neurological disease. Commun Integr Biol. 2013 Nov 01;6(6):e26839. doi: 10.4161/cib.26839. Epub 2013 Nov 13. PMID: 24563715; PMCID: PMC3922786.
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Vav1 in hematologic neoplasms, a mini review.

American journal of blood research

Oberley MJ, Wang DS, Yang DT.
PMID: 22432082
Am J Blood Res. 2012;2(1):1-8. Epub 2012 Jan 01.

The Vav family of proteins are guanine nucleotide exchange factors which have been shown to be deregulated in several types of human cancer. There are three members of the Vav family that have been identified which are members of...

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Oberley MJ, Wang DS, Yang DT. Vav1 in hematologic neoplasms, a mini review. Am J Blood Res. 2012;2(1):1-8
Oberley, M. J., Wang, D. S., & Yang, D. T. (2012). Vav1 in hematologic neoplasms, a mini review. American journal of blood research, 2(1), 1-8.
Oberley, Matthew J, et al. "Vav1 in hematologic neoplasms, a mini review." American journal of blood research vol. 2,1 (2012): 1-8.
Oberley MJ, Wang DS, Yang DT. Vav1 in hematologic neoplasms, a mini review. Am J Blood Res. 2012;2(1):1-8. Epub 2012 Jan 01. PMID: 22432082; PMCID: PMC3301436.
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