Results 31 to 40 of about 57,806 (244)

Analysis of the interaction of Plexin-B1 and Plexin-B2 with Rnd family proteins. [PDF]

PLoS ONE, 2017
The Rnd family of proteins, Rnd1, Rnd2 and Rnd3, are atypical Rho family GTPases, which bind to but do not hydrolyse GTP. They interact with plexins, which are receptors for semaphorins, and are hypothesised to regulate plexin signalling.
Thomas Wylie, Ritu Garg, Anne J Ridley, Maria R Conte   +3 more
doaj   +1 more source

Novel split-luciferase-based genetically encoded biosensors for noninvasive visualization of Rho GTPases. [PDF]

PLoS ONE, 2013
Rho family GTPases are critical regulators of many important cellular processes and the dysregulation of their activities is implicated in a variety of human diseases including oncogenesis and propagation of malignancy.
Weibing Leng, Xiaohui Pang, Hongwei Xia, Mingxing Li, Liu Chen, Qiulin Tang, Dandan Yuan, Ronghui Li, Libo Li, Fabao Gao, Feng Bi   +10 more
doaj   +1 more source

RHGF-2 is an essential Rho-1 specific RhoGEF that binds to the multi-PDZ domain scaffold protein MPZ-1 in Caenorhabditis elegans. [PDF]

PLoS ONE, 2012
RhoGEF proteins activate the Rho family of small GTPases and thus play a key role in regulating fundamental cellular processes such as cell morphology and polarity, cell cycle progression and gene transcription.
Li Lin, Thuy Tran, Shuang Hu, Todd Cramer, Richard Komuniecki, Robert M Steven   +5 more
doaj   +1 more source

The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms [PDF]

, 2008
© 2008 by The American Society for Cell Biology. Under the License and Publishing Agreement, authors grant to the general public, effective two months after publication of (i.e.,.
Ammerer G., Andoh T., Bose I., Bosl W. J., Bourmeyster N., Christopher Tiedje, Chuang T. H., Cole K. C., Daniel Lew, DerMardirossian C., DerMardirossian C., Dovas A., Dransart E., Eitzen G., Forget M. A., Gladfelter A. S., Gulli M. P., Hoffman G. R., Höfken T., Höfken T., Imme Sakwa, Irazoqui J. E., Irazoqui J. E., Jaffe A. B., Janke C., Jensen S., Kassir Y., Kim L., Knop M., Koch G., Lee D. H., Longtine M. S., Marco E., Masuda T., Mazón M. J., Mehta D., Mösch H. U., Nomanbhoy T. K., Palecek S. P., Park H. O., Ptacek J., Richman T. J., Richman T. J., Roberts R. L., Roth A. F., Rotin D., Scheffzek K., Schwamborn J. C., Seshan A., Takahashi K., Tcheperegine S. E., Thomas Höfken, Ursula Just, Valdez-Taubas J., Wang H. R., Wedlich-Soldner R., Yamashita T., Yamochi W., Ziman M.   +58 more
core   +3 more sources

Posttranslational modification of the RHO of plants protein RACB by phosphorylation and cross-kingdom conserved ubiquitination.

PLoS ONE, 2022
Small RHO-type G-proteins act as signaling hubs and master regulators of polarity in eukaryotic cells. Their activity is tightly controlled, as defective RHO signaling leads to aberrant growth and developmental defects.
Lukas Weiß, Lana Gaelings, Tina Reiner, Julia Mergner, Bernhard Kuster, Attila Fehér, Götz Hensel, Manfred Gahrtz, Jochen Kumlehn, Stefan Engelhardt, Ralph Hückelhoven   +10 more
doaj   +1 more source

Reciprocal regulation of PKA and rac signaling [PDF]

, 2013
Activated G protein-coupled receptors (GPCRs) and receptor tyrosine kinases relay extracellular signals through spatial and temporal controlled kinase and GTPase entities.
A. Riml, Baillie, Bhola, Birukova, Cook, Cuevas, Daaka, Delcourt, Dewire, Dorsam, Dumaz, E. Stefan, Eblen, G. S. Baillie, Gerits, Gloerich, Hafner, Hoffmann, Howe, Jaffe, K. R. Liedl, Kinderman, King, Kraynov, Kumar, Ligr, Malbon, Manser, Molli, Nika, Pierce, R. G. Huber, Sahai, Sch  fer, Scott, Smith, Stefan, Stork, T. Valovka, Taylor, Thaker, V. A. Bachmann, Wang, Wennerberg, Wong, Zenke, Zhang, Zhao   +47 more
core   +1 more source

Structure of a highly conserved domain of Rock1 required for Shroom-mediated regulation of cell morphology. [PDF]

PLoS ONE, 2013
Rho-associated coiled coil containing protein kinase (Rho-kinase or Rock) is a well-defined determinant of actin organization and dynamics in most animal cells characterized to date.
Swarna Mohan, Debamitra Das, Robert J Bauer, Annie Heroux, Jenna K Zalewski, Simone Heber, Atinuke M Dosunmu-Ogunbi, Michael A Trakselis, Jeffrey D Hildebrand, Andrew P Vandemark   +9 more
doaj   +1 more source

Coxiella burnetii Phagocytosis Is Regulated by GTPases of the Rho Family and the RhoA Effectors mDia1 and ROCK [PDF]

, 2015
The GTPases belonging to the Rho family control the actin cytoskeleton rearrangements needed for particle internalization during phagocytosis. ROCK and mDia1 are downstream effectors of RhoA, a GTPase involved in that process.
A Alonso, A Schonichen, A Subtil, A Tierrez, A Yoneda, AB Hall, AB Jaffe, AD Hoppe, AL Bishop, AP Wheeler, AR Frampton Jr., AS Alberts, B Qualmann, BJ Wallar, C Capo, C Cougoule, C Yang, CA Burnham, CM Haglund, CW Gourlay, D Howe, D Michaelson, D Michaelson, D Truong, Daniel E. Voth, DE Voth, DJ Hackam, DM Underhill, DM Waag, DT Brandt, E Alix, E Caron, E Colucci-Guyon, E Lemichez, EJ van Schaik, EM Rosales, EN Firat-Karalar, F Li, F Matsumura, F Niedergang, G Kaplan, GD Fairn, H Bierne, H Bierne, H Genth, HJ Newton, IM Olazabal, J Dellacasagrande, J Faix, J Hanisch, J Pizarro-Cerda, J Pizarro-Cerda, JA McDonough, JA Swanson, JC Patel, JC Patel, JE Heindl, Jesús S. Distel, JG Duman, JG Kim, K Aktories, K Bhadriraju, L Hodgson, LA Allen, M Aguilera, M Amano, M Amano, M Fernandez-Borja, M Kaksonen, M Ladwein, María I. Colombo, MG Gutierrez, Milton O. Aguilera, ML Gardel, N Ramalingam, N Watanabe, N Watanabe, NA Khan, O Billker, O Pertz, O Pertz, OB Matas, OG Baca, OG Baca, P Aspenstrom, P Cossart, P Croise, P Hotulainen, PJ Roberts, PS Romano, R Fox, RA Carabeo, RC May, RC May, Rodolfo M. Ortiz Flores, Romina P. Salinas, RS Flannagan, S Meconi, SJ Heasman, SK Hussain, T Dubois, T Tominaga, V Benard, VC Tam, W Beron, Walter Berón, WI Goh, X Chi, XD Ren, Z Woldehiwet   +109 more
core   +7 more sources

Regulation of polarised growth in fungi [PDF]

, 2008
Polarised growth in fungi occurs through the delivery of secretory vesicles along tracks formed by cytoskeletal elements to specific sites on the cell surface where they dock with a multiprotein structure called the exocyst before fusing with the ...
Adamo, Adamo, Adams, Akashi, Ayad-Durieux, Bachewich, Bartnicki-Garcia, Bartnicki-Garcia, Bassilana, Bassilana, Bassilana, Behrens, Berman, Bidlingmaier, Bose, Boyce, Boyce, Boyce, Boyd, Brown, Caviston, Chant, Chapa y Lazo, Collinge, Colman-Lerner, Court, Crampin, Cvrckova, Dong, Drgonova, Dunkler, Feng, Finger, France, Gao, Girbardt, Gladfelter, Goehring, Gorovits, Gulli, Guo, Harris, Harris, Hartwell, Hergovich, Hou, Hou, Irazoqui, Jin, Karnoub, Knechtle, Kohno, Konzack, Kron, Leberer, Leberer, Leberer, Leonhard, Lew, Li, Liu, Loeb, Loeb, Longtine, Mahlert, Mata, McCollum, McCusker, Medkova, Mehta, Mendenhall, Nelson, Nonaka, Novick, Pan, Park, Pearson, Peter, Peter E. Sudbery, Philippsen, Punt, Qadota, Racki, Read, Santangelo, Schmidt, Seiler, Seiler, Sinha, Smith, Soll, Stevenson, Sudbery, Sudbery, Sudbery, Tamaskovic, Tanaka, Tcheperegine, Trinci, Verde, Versele, Virag, Virag, Walton, Walworth, Wedlich-Soldner, Wedlich-Soldner, Wendland, Wu, Yarden, Zhang, Zheng, Zheng   +112 more
core   +1 more source

Isolation and Imaging of His- and RFP-tagged Amyloid-like Proteins from Caenorhabditis elegans by TEM and SIM

Bio-Protocol, 2019
In our recently published paper, we highlight that during normal aging of C. elegans age-dependent aggregates of proteins form and lead to functional decline of tissues. The protocol described here details the isolation of two proteins from C. elegans in
Amberley Stephens, Meng Lu, Gabriele Kaminski Schierle   +2 more
doaj   +1 more source