The interaction of Ras with GTPase‐activating proteins

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392

The GTPase superfamily: a conserved switch for diverse cell functions

Bourne, H. R., Sanders, D. A. R., & McCormick, F. P. (1990) · Nature · doi:10.1038/348125a0 · Cited by 2,336

A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants

Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211

The neurofibromatosis type 1 gene encodes a protein related to GAP

Xu, G., O'Connell, P., Viskochil, D., Cawthon, R., Robertson, M., Culver, M., Dunn, D., Stevens, J., Gesteland, R., White, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90024-9 · Cited by 1,095

A major segment of the neurofibromatosis type 1 gene: cDNA sequence, genomic structure, and point mutations

Cawthon, R., Weiss, R. B., Xu, G., Viskochil, D. H., Culver, M., Stevens, J., Robertson, M. A., Dunn, D. M., Gesteland, R. F., O'Connell, P., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90253-b · Cited by 1,093

Deletions and a translocation interrupt a cloned gene at the neurofibromatosis type 1 locus

Viskochil, D. H., Buchberg, A. M., Xu, G., Cawthon, R., Stevens, J., Wolff, R. K., Culver, M., Carey, J. C., Copeland, N. G., Jenkins, N. A., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90252-a · Cited by 1,082

Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras Proteins

Milburn, M. V., Tong, L., deVos, A. M., Brünger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S. (1990) · Science · doi:10.1126/science.2406906 · Cited by 1,062

The GAP-related domain of the neurofibromatosis type 1 gene product interacts with ras p21

Martin, G. A., Viskoohil, D., Bollag, G. E., McCabe, P. C., Crosier, W. J., Haubruck, H., Conroy, L., Clark, R., O'Connell, P., Cawthon, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90150-d · Cited by 983

Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

PAI, E. F., Kabsch, W., Krengel, U., Holmes, K. C., John, J., & Wittinghofer, A. (1989) · Nature · doi:10.1038/341209a0 · Cited by 876

Probing the Electrostatic Effects of H-Ras Tyrosine 32 Mutations on Intrinsic GTP Hydrolysis Using Vibrational Stark Effect Spectroscopy of a Thiocyanate Probe

Fink, J. C., Landry, D., & Webb, L. J. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00075 · Cited by 3

Cell polarity control by an unconventional G-protein complex in bacteria

Dinet, C., Sebban‐Kreuzer, C., Byrne, D., Lhospice, S., Herrou, J., Durbesson, F., Vincentelli, R., Calvez, V., Sturgis, J. N., Michelot, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74081-1 · Cited by 3

Structural Principles of Ras Interaction with Regulators and Effectors

Fiegen, D., Dvorský, R., & Ahmadian, M. R. (2006) · Springer eBooks · doi:10.1007/1-4020-4708-8_3 · Cited by 3

Oncogenes and Signal Transduction

Bafico, A., Grumolato, L., & Aaronson, S. A. (2008) · Elsevier eBooks · doi:10.1016/b978-141603703-3.10002-0 · Cited by 4

Mechanistic insights on spatiotemporal control of Ras-signaling

Charrier, C., Mrachacz, S., Schulze, S., & Lammers, M. (2026) · Biological Chemistry · doi:10.1515/hsz-2025-0243 · Cited by 2

The Role of Mutation and Epimutation in the Development of Human Disease

Rivenbark, A. G., & Coleman, W. B. (2009) · Molecular pathology library · doi:10.1007/978-0-387-89626-7_5 · Cited by 2

Molecular biology, models, and histopathology of chronic pancreatitis and pancreatic cancer

Mihaljević, A. L., Esposito, I., Frieß, H., & Kleeff, J. H. (2009) · European surgery. Supplement/European surgery · doi:10.1007/s10353-009-0496-3 · Cited by 2

Structural basis of neurofibromin tetramerization and dimer-tetramer equilibriumPreprint

Si, S., Tueting, C., Lohse, S., Landfester, K., Lieberwirth, I., Kastritis, P. L., & Harder, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.13.638105 · Cited by 2

Control of Small GTPase Ras Using a Calmodulin-based Ionochromic Nanodevice

Zhang, Z., Sabek, Y., & Maruta, S. (2024) · Biosciences Biotechnology Research Asia · doi:10.13005/bbra/3247 · Cited by 1

The intersection of EGFR and the Ras signaling pathway

Wislez, M., & Kurie, J. M. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-356-1_7 · Cited by 1

Localization of the Novel GAP Family Protein SPAL in Epithelial Cells.

Kohu, K., Roy, B. C., Kuroda, T., Kakinuma, N., Akiyama, T., & Senda, T. (2000) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.33.451 · Cited by 1

ATP Hydrolysis in the b TP and b DP Catalytic Sites of F 1 -ATPase

Dittrich, M., Hayashi, S., & Schulten, K. J. (2004) · Cited by 1

Inhibition of mutant RAS-RAF interaction by mimicking structural and dynamic properties of phosphorylated RASPreprint

Ilter, M., Kaşmer, R., Jalalypour, F., Atılgan, C., Topcu, O., Karakaş, N., & Şensoy, Ö. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.24.489309 · Cited by 1

Estudo da expressão do Gene ABR em leucemia mieloide cronica (LMC) utilizando real-time RT-PCR (qPCR),

Namasu, C. Y. (2006) · doi:10.47749/t/unicamp.2006.373559

Myelodysplasia-Related AML

Parker, J. E. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-322-6_3

Effect of the altered codon position and encoded amino acid on transformation by point mutation in ras genes

Caballero, S. G., & Mangues, R. (2002) · Revista de Oncología · doi:10.1007/bf02712390

The Role of p120 RasGAP in T Cells and Lymphatics.

Lapinski, P. E. (2009) · Deep Blue (University of Michigan)

Identificación y análisis funcional de nuevos oncogenes amplificados en cáncer de pulmón

Castillo, S. D. (2011) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

ISOPRENOID ANALOGS AS CHEMICAL GENETIC TOOLS TO PROVIDE INSIGHTS INTO FARNESYL TRANSFERASE TARGET SELECTION AND CELLULAR ACTIVITY

Troutman, J. M. (2006) · UKnowledge (University of Kentucky)

Regulation of endocytosis and secretion by Rab GTPase activating proteins

Haas, A. K. (2008) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.8660

Neurofibromin and IL-4 as Regulators of T Cell Development, Function, and Homeostasis

Oliver, J. A. (2012) · Deep Blue (University of Michigan)

The Ras-RasGAP Complex: How to Complement an Inefficient Active Site

Scheffzek, K., Ahmadian, M. R., Wiesmüller, L., Lautwein, A., Kabsch, W., Schmitz, F., & Wittinghofer, A. (1999) · Phosphorus, sulfur, and silicon and the related elements · doi:10.1080/10426509908039666

CHARACTERIZATION OF DROSOPHILA HOMOLOGUES OF ACTIVATED Cdc42 ASSOCIATED KINASE (ACK)

Xu, X. (2005) · Summit (Simon Fraser University)

Specific Signaling Through Heteromeric PDGF Receptor Complexes

Ekman, S. (2000) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Roles of Mutation and Epimutation in the Development of Lung Disease

Coleman, W. B. (2008) · Molecular pathology library · doi:10.1007/978-0-387-72430-0_5

The role of a putative arginine finger and guanine nucleotides in homo- and heterodimerization of two GTPases involved in protein import into chloroplasts

Weibel, P. (2005) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-004938892 · Cited by 1

Structural and functional analysis of Eukaryal-like proteins from the hyperthermophilic archaeon Sulfolobus solfataricus

Wu, H. (2007) · doi:10.18174/2498

Peculiarities in Activation of Hydrolytic Activity of Elongation Factors

Paleskava, A., Kaiumov, M., KIRILLOV, S. V., & Konevega, A. L. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920110103

Chapter 6 Molecular Crowding, Transfer of Information and Channelling of Molecules within Supramolecular Edifices

(1999) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60549-9

Phylogenetic studies of the vesicular fusion machinery

Kienle, N. (2010) · doi:10.53846/goediss-3157

Structural and functional analysis of yeast proteins involved in ER-to-Golgi transport: Sec24p family proteins and the GTPase activating protein Gyp5p

Antoni, A. D. (2001) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-665

TP53-status dependent oncogenic EZH2 Activity in Pancreatic Cancer

Versemann, L. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9359

Caractérisation d’un transporteur ABC d’antibiotiques de Streptococcus pneumoniae, PatA-PatB

Mathieu, K. (2019) · theses.fr (ABES) · doi:10.70675/baa8a399z3cefz452bza32eza8a0f2d45eef

Sub-lethal dose exposure of cyflufenamid, flutianil, quinoxyfen, trifloxystrobin and metrafenone effects on conidial germination and gene expression in the grape powdery mildew pathogen

Sharma, N., Mahey, M., Naegele, R. P., & Miles, T. D. (2026) · Frontiers in Microbiology · doi:10.3389/fmicb.2026.1944688

BindingDB Entry 50021622: Design, Synthesis, and Biological Evaluation of Potent and Selective PROTAC Degraders of Oncogenic KRASG12D.

BindingDB (2025) · UC San Diego · doi:10.7270/q2ww7pb2

Minireview The interaction of Ras with GTPase-activating proteins

Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R. (1997)

Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras

Scheffzek, K., Lautwein, A., Kabsch, W., Ahmadian, M. R., & Wittinghofer, A. (1996) · Nature · doi:10.1038/384591a0 · Cited by 173

The Ras-RasGAP Complex: How to Complement an Inefficient Active Site

Scheffzek, K., Ahmadian, M. R., Wiesmüller, L., Lautwein, A., Kabsch, W., Schmitz, F., & Wittinghofer, A. (1999) · Phosphorus, sulfur, and silicon and the related elements · doi:10.1080/10426509908039666

Turning off the Ras switch with the flick of a finger

Noel, J. P. (1997) · Nature Structural Biology · doi:10.1038/nsb0997-677 · Cited by 18

Common mechanisms of catalysis in small and heterotrimeric GTPases and their respective GAPs

Gerwert, K. B., Mann, D., & Kötting, C. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0314 · Cited by 25