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1. Full Text Small molecule targeting Cdc42–intersectin interaction disrupts Golgi organization and suppresses cell motility
by Amy Friesland and Yaxue Zhao and Yan-Hua Chen and Lie Wang and Huchen Zhou and Qun Lu
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2013, Volume 110, Issue 4, pp. 1261 - 1266
Signaling through the Rho family of small GTPases has been intensely investigated for its crucial roles in a wide variety of human diseases. Although RhoA and... 
Molecules | Growth cones | Cell motility | Phosphorylation | Neurons | Fluorescence | Fibroblasts | Swiss 3T3 cells | Pseudopodia | Research universities | ACTIVATION | protein trafficking | cytoskeleton | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | VESICLE TRAFFICKING | Cdc42 inhibitor | NEURONAL DEVELOPMENT | RAC | computer-assisted virtual screening | FILOPODIA | CDC42 GTPASES | protein-protein interaction | REGULATORS | ACTIN CYTOSKELETON | RHO-GTPASES | User-Computer Interface | Golgi Apparatus - drug effects | Humans | Swiss 3T3 Cells | Molecular Sequence Data | Golgi Apparatus - physiology | Cell Movement - physiology | Neurons - ultrastructure | cdc42 GTP-Binding Protein - antagonists & inhibitors | Adaptor Proteins, Vesicular Transport - chemistry | Drug Evaluation, Preclinical | Neurons - drug effects | Binding Sites | Wound Healing - drug effects | Amino Acid Sequence | Cell Survival - drug effects | Adaptor Proteins, Vesicular Transport - physiology | Protein Interaction Domains and Motifs - drug effects | Adaptor Proteins, Vesicular Transport - antagonists & inhibitors | Cells, Cultured | Models, Molecular | cdc42 GTP-Binding Protein - physiology | Sequence Homology, Amino Acid | Cell Movement - drug effects | Animals | Signal Transduction - drug effects | cdc42 GTP-Binding Protein - genetics | cdc42 GTP-Binding Protein - chemistry | Mice | Cell interaction | Motility | Physiological aspects | Research | Health aspects | Cells | Golgi apparatus | protein–protein interaction | Biological Sciences
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2. CDC42 shapes up the epicardium
Development, ISSN 0950-1991, 05/2017, Volume 144, Issue 9, pp. e0902 - e0902
Cdc42 protein
Journal Article
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3. Full Text Regulation of microtubule-associated motors drives intermediate filament network polarization
by Leduc, CĂ©cile and Etienne-Manneville, Sandrine
Journal of Cell Biology, ISSN 0021-9525, 06/2017, Volume 216, Issue 6, pp. 1689 - 1703
Intermediate filaments (IFs) are key players in the control of cell morphology and structure as well as in active processes such as cell polarization,... 
IV ALPHA-INTERNEXIN | CYTOPLASMIC DYNEIN | IN-VITRO | CYTOSKELETAL CROSSTALK | VIMENTIN | ACTIN | ASTROCYTE MIGRATION | DEPENDENT TRANSPORT | CELL POLARITY | CDC42 LOCALIZATION | CELL BIOLOGY | Cell Polarity | Optical Imaging | Protein Kinase C - genetics | Neuroglia - pathology | Vimentin - metabolism | Humans | Actins - metabolism | Astrocytes - pathology | cdc42 GTP-Binding Protein - metabolism | Microscopy, Video | Wound Healing | Glial Fibrillary Acidic Protein - metabolism | Intermediate Filaments - metabolism | Microtubules - metabolism | Transfection | RNA Interference | Time Factors | Protein Kinase C - metabolism | Dyneins - metabolism | Signal Transduction | Rats | Nestin - metabolism | Animals | cdc42 GTP-Binding Protein - genetics | Cell Line, Tumor | Neuroglia - metabolism | Dyneins - genetics | Astrocytes - metabolism | Cell Movement | Vimentin | Nestin | Neuroglia | Cellular Biology | Glial Fibrillary Acidic Protein | Life Sciences | Intermediate Filaments | Dyneins | Astrocytes | Actins | Microtubules | cdc42 GTP-Binding Protein | Santé publique et épidémiologie | Protein Kinase C
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4. Full Text Androgen receptor (AR) promotes clear cell renal cell carcinoma (ccRCC) migration and invasion via altering the circHIAT1/miR-195-5p/29a-3p/29c-3p/CDC42 signals
by Wang, Kefeng and Sun, Yin and Tao, Wei and Fei, Xiang and Chang, Chawnshang
Cancer Letters, ISSN 0304-3835, 2017, Volume 394, pp. 1 - 12
Abstract Increasing evidence has demonstrated that androgen receptor (AR) plays important roles to promote the metastasis of clear cell renal cell carcinoma... 
Hematology, Oncology and Palliative Medicine | CDC42 | circRNA | Renal cell carcinoma | Migration | Invasion | Androgen receptor | ACTIVATION | METASTASIS | FILOPODIA FORMATION | CIRCULAR RNAS | HEPATOCELLULAR-CARCINOMA | ONCOLOGY | PATHWAY | RESISTANT PROSTATE-CANCER | EXPRESSION | PROGRESSION | Kidney Neoplasms - genetics | Humans | Receptors, Androgen - metabolism | Gene Expression Regulation, Neoplastic | Carcinoma, Renal Cell - genetics | MicroRNAs - metabolism | cdc42 GTP-Binding Protein - metabolism | Kidney Neoplasms - metabolism | RNA - genetics | Transfection | Time Factors | Monosaccharide Transport Proteins - metabolism | Monosaccharide Transport Proteins - genetics | RNA - metabolism | Signal Transduction | Neoplasm Invasiveness | Carcinoma, Renal Cell - metabolism | Animals | Receptors, Androgen - genetics | Mice, Nude | cdc42 GTP-Binding Protein - genetics | Carcinoma, Renal Cell - secondary | Cell Line, Tumor | Kidney Neoplasms - pathology | MicroRNAs - genetics | Cell Movement | Carcinoma, Renal cell | Metastasis | Hormones | Reservoirs | RNA | Cdc42 protein | Deregulation | Wound healing | Leukocyte migration | Transcription | Gene expression | Tissues | Urology | Cell adhesion & migration | Metastases | Studies | Androgens | Gene amplification | Mutagenesis | Plasmids | Prostate cancer | Clear cell-type renal cell carcinoma | Binding sites | Cell migration | Tumors
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5. Cdc42 and Par Proteins Regulate the Trafficking of Apical Membrane Proteins to Stabilize Dynamic Adherens Junctions in the Drosophila Neuroectoderm
by Harris, Kathryn P
06/2010
Epithelial sheets line the surfaces of the body, forming a barrier between the external environment and internal tissues. During development, regulation of... 
0379 | Epithelial polarity | Cdc42
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6. Full Text Small GTPases and BAR domain proteins regulate branched actin polymerisation for clathrin and dynamin-independent endocytosis
by Sathe, Mugdha and Muthukrishnan, Gayatri and Rae, James and Disanza, Andrea and Thattai, Mukund and Scita, Giorgio and Parton, Robert G and Mayor, Satyajit
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1835 - 16
Using real-time TIRF microscopy imaging, we identify sites of clathrin and dynamin-independent CLIC/GEEC (CG) endocytic vesicle formation. This allows... 
CDC42 | MEMBRANE SCISSION | RECRUITMENT | COMPLEX | MULTIDISCIPLINARY SCIENCES | FILOPODIA | IRSP53 | PICK1 | N-WASP | IDENTIFICATION | SMALL-MOLECULE INHIBITOR | Dynamins - metabolism | Fibroblasts - enzymology | Humans | Actins - metabolism | cdc42 GTP-Binding Protein - metabolism | Endocytosis | Guanine Nucleotide Exchange Factors - metabolism | Actins - chemistry | Protein Domains | ADP-Ribosylation Factor 1 - metabolism | ADP-Ribosylation Factor 1 - genetics | Nuclear Proteins - genetics | Fibroblasts - metabolism | Guanine Nucleotide Exchange Factors - genetics | Polymerization | Nuclear Proteins - metabolism | Nerve Tissue Proteins - genetics | Clathrin - chemistry | Clathrin - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Dynamins - chemistry | cdc42 GTP-Binding Protein - genetics | Protein Binding | Mice | Proteins | Cdc42 protein | Clathrin | Microscopy | Actin | RNA-mediated interference | Dynamin | Cleavage | Curvature | Molecular chains
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7. Full Text Meningococcal Type IV Pili Recruit the Polarity Complex to Cross the Brain Endothelium
by Mathieu Coureuil and Guillain Mikaty and Florence Miller and Hervé Lécuyer and Christine Bernard and Sandrine Bourdoulous and Guillaume Duménil and René-Marc MÚge and Babette B. Weksler and Ignacio A. Romero and Pierre-Olivier Couraud and Xavier Nassif
Science, ISSN 0036-8075, 7/2009, Volume 325, Issue 5936, pp. 83 - 87
Type IV pili mediate the initial interaction of many bacterial pathogens with their host cells. In Neisseria meningitidis, the causative agent of cerebrospinal... 
Intercellular junctions | Cell lines | Actins | Small interfering RNA | Bacteria | Cadherins | Reports | Bacterial adhesion | Infections | Blood brain barrier | Endothelial cells | CDC42 | ADHESION | HUMAN EPITHELIAL-CELLS | PATHOGENIC NEISSERIA | TWITCHING MOTILITY | MULTIDISCIPLINARY SCIENCES | NEISSERIA-MENINGITIDIS | BARRIER | PAR3 | RECEPTOR | ADHERENS | Cell Polarity | Brain - microbiology | Cadherins - metabolism | Humans | cdc42 GTP-Binding Protein - metabolism | Intercellular Junctions - microbiology | Phosphoproteins - metabolism | Blood-Brain Barrier - microbiology | Antigens, CD - metabolism | Catenins | Endothelial Cells - microbiology | Endothelium, Vascular - ultrastructure | Brain - blood supply | Protein Kinase C - metabolism | Membrane Proteins - metabolism | Neisseria meningitidis - physiology | Neisseria meningitidis - pathogenicity | Cell Line | Brain - cytology | Endothelial Cells - metabolism | Cell Cycle Proteins - metabolism | Intercellular Junctions - metabolism | Cell Adhesion Molecules - metabolism | Blood-Brain Barrier - metabolism | Endothelium, Vascular - microbiology | Bacterial Adhesion | Endothelium, Vascular - metabolism | Fimbriae, Bacterial - physiology | Adaptor Proteins, Signal Transducing - metabolism | Intercellular Junctions - ultrastructure | Measurement | Polarity (Biology) | Neisseria meningitidis | Properties | Health aspects | Endothelium | Brain | Meningitis | Eukaryotes | Cell adhesion & migration | Fimbriae, Bacterial | Endothelial Cells | Cell Adhesion Molecules | Intercellular Junctions | Membrane Proteins | Life Sciences | Microbiology and Parasitology | Adaptor Proteins, Signal Transducing | Phosphoproteins | cdc42 GTP-Binding Protein | Endothelium, Vascular | Cell Cycle Proteins | Antigens, CD | Protein Kinase C | Blood-Brain Barrier | cytology | meningitis | microbiology | physiology | ultrastructure | blood brain barrier | pathogenicity | blood supply | metabolism
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8. ADAR1 regulates ARHGAP26 gene expression through RNA editing by disrupting miR-30b-3p and miR-573 binding
by Wang, Q and Hui, H and Guo, Z and Zhang, W and Hu, Y and He, T and Tai, Y and Peng, P and Wang, LI
RNA, ISSN 1355-8382, 11/2013, Volume 19, Issue 11, pp. 1525 - 1536
Rho GTPase activating protein 26 (ARHGAP26) is a negative regulator of the Rho family that converts the small G proteins RhoA and Cdc42 to their inactive... 
Cdc42 protein
Journal Article
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9. Full Text miR-137 inhibits the proliferation of lung cancer cells by targeting Cdc42 and Cdk6
by Zhu, Xiaolan and Li, Hao and Li, Yuefeng and Shen, Huiling and Long, Lulu and Hui, Lulu and Xu, Wenlin
FEBS Letters, ISSN 0014-5793, 01/2013, Volume 587, Issue 1, pp. 73 - 81
â–ș Ectopic expression of miR-137 in lung cancer cells downregulates Cdc42, Cdk6 and induced G1 cell cycle arrest. â–ș Cdc42 and Cdk6 are targets of miR-137. â–ș... 
miR-137 | Cdk6 | Lung cancer | Cdc42 | Cyclin-Dependent Kinase 6 - antagonists & inhibitors | Lung Neoplasms - drug therapy | Cell Proliferation | DNA Modification Methylases - antagonists & inhibitors | Humans | Lung Neoplasms - metabolism | Gene Expression Regulation, Neoplastic | MicroRNAs - metabolism | cdc42 GTP-Binding Protein - metabolism | G1 Phase - drug effects | cdc42 GTP-Binding Protein - antagonists & inhibitors | Antineoplastic Agents - pharmacology | Lung - metabolism | Gene Transfer Techniques | Down-Regulation | Carcinoma, Non-Small-Cell Lung - metabolism | Cyclin-Dependent Kinase 6 - genetics | Gene Silencing | Cyclin-Dependent Kinase 6 - metabolism | Lung Neoplasms - therapy | Xenograft Model Antitumor Assays | Carcinoma, Non-Small-Cell Lung - therapy | Animals | cdc42 GTP-Binding Protein - genetics | Lung - drug effects | Cell Line, Tumor | Histone Deacetylase Inhibitors - pharmacology | Mice | MicroRNAs - genetics | Carcinoma, Non-Small-Cell Lung - drug therapy | MICRORNA-137 | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | CELL BIOLOGY | BIOPHYSICS | GROWTH | GENE-EXPRESSION | MICRO | CYCLE | Methylation | Cancer cells | Index Medicus
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10. Full Text Rapid Remodeling of Invadosomes by Gi-coupled Receptors: DISSECTING THE ROLE OF Rho GTPases
by Kedziora, K.M and Leyton-Puig, D and Argenzio, E and Boumeester, A.J and Butselaar, B. van and Yin, T and Wu, Y.I and Leeuwen, F.N. van and Innocenti, M and Jalink, K and Moolenaar, W.H
Journal of Biological Chemistry, ISSN 0021-9258, 2016, Volume 291, Issue 9, pp. 4323 - 4333
Invadosomes are actin-rich membrane protrusions that degrade the extracellular matrix to drive tumor cell invasion. Key players in invadosome formation are... 
Receptors, Lysophosphatidic Acid - metabolism | Lysophospholipids - metabolism | Receptors, G-Protein-Coupled - metabolism | Humans | Extracellular Matrix - metabolism | Melanoma - enzymology | Podosomes - enzymology | Neoplasm Proteins - antagonists & inhibitors | Receptors, Lysophosphatidic Acid - agonists | Receptors, Lysophosphatidic Acid - genetics | cdc42 GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - genetics | Endothelins - metabolism | Neoplasm Proteins - metabolism | Time-Lapse Imaging | Podosomes - metabolism | RNA Interference | cdc42 GTP-Binding Protein - antagonists & inhibitors | Fluorescence Resonance Energy Transfer | Receptors, Lysophosphatidic Acid - antagonists & inhibitors | Neoplasm Proteins - genetics | Biomarkers - metabolism | Melanoma - metabolism | Recombinant Proteins - metabolism | rac1 GTP-Binding Protein - agonists | rhoA GTP-Binding Protein - antagonists & inhibitors | Recombinant Proteins - genetics | Melanoma - pathology | cdc42 GTP-Binding Protein - agonists | Hydrolysis | Podosomes - pathology | Microscopy, Confocal | Neoplasm Proteins - agonists | cdc42 GTP-Binding Protein - genetics | Receptors, G-Protein-Coupled - antagonists & inhibitors | rac1 GTP-Binding Protein - antagonists & inhibitors | Cell Line, Tumor | Luminescent Proteins - genetics | Receptors, G-Protein-Coupled - genetics | Extracellular Matrix - pathology | Microscopy, Fluorescence | rac1 GTP-Binding Protein - metabolism | Luminescent Proteins - metabolism | rac1 GTP-Binding Protein - genetics | CDC42 | invadopodia | biosensor | fluorescence resonance energy transfer (FRET) | calcium intracellular release | G protein-coupled receptor (GPCR) | Rho (Rho GTPase) | phosphatidylinositide 3-kinase (PI 3-kinase) | imaging | Rac (Rac GTPase) | Cell Biology
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11. Full Text PAK5 is auto-activated by a central domain that promotes kinase oligomerization
by Tabanifar, Bahareh and Zhao, Zhuoshen and Manser, Ed
Biochemical Journal, ISSN 0264-6021, 06/2016, Volume 473, Issue 12, pp. 1777 - 1789
Activation | Localization | PAK5 | Cdc42
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12. Full Text Characterization of a Cdc42 protein inhibitor and its use as a molecular probe
by Hong, Lin and Kenney, S. Ray and Phillips, Genevieve K and Simpson, Denise and Schroeder, Chad E and Nöth, Julica and Romero, Elsa and Swanson, Scarlett and Waller, Anna and Strouse, J. Jacob and Carter, Mark and Chigaev, Alexandre and Ursu, Oleg and Oprea, Tudor and Hjelle, Brian and Golden, Jennifer E and Aubé, Jeffrey and Hudson, Laurie G and Buranda, Tione and Sklar, Larry A and Wandinger-Ness, Angela
Journal of Biological Chemistry, ISSN 0021-9258, 03/2013, Volume 288, Issue 12, pp. 8531 - 8543
Cdc42 plays important roles in cytoskeleton organization, cell cycle progression, signal transduction, and vesicle trafficking. Overactive Cdc42 has been... 
LUNG-CANCER | REAL-TIME MEASUREMENT | DIRECTED MIGRATION | RAS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEOTIDE-BINDING | ACTIN DYNAMICS | FLOW-CYTOMETRY | CELL MIGRATION | E-CADHERIN | RHO-GTPASES | Allosteric Regulation | Humans | Molecular Probes - pharmacology | cdc42 GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - metabolism | Structure-Activity Relationship | Virus Internalization - drug effects | Pseudopodia - drug effects | cdc42 GTP-Binding Protein - antagonists & inhibitors | Phenylurea Compounds - metabolism | Pyrazoles - pharmacology | Cell Survival - drug effects | Antiviral Agents - pharmacology | Enzyme Inhibitors - pharmacology | Sin Nombre virus - physiology | Oligopeptides - metabolism | Enzyme Activation - drug effects | Sulfonamides - pharmacology | Cell Movement - drug effects | Animals | Integrin alpha4beta1 - physiology | Integrin alpha4beta1 - antagonists & inhibitors | Cell Line, Tumor | Protein Binding | cdc42 GTP-Binding Protein - chemistry | Mice | 3T3 Cells | rac1 GTP-Binding Protein - metabolism | Index Medicus | Cytoskeleton | Integrin | GTPase | Migration | Cell Biology | Cdc42
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13. Full Text Characterization of a dual Rac/Cdc42 Inhibitor MBQ-167 in metastatic cancer
by Humphries-Bickley, Tessa and Castillo-Pichardo, Linette and Hernandez-O'Farrill, Eliud and Borrero-Garcia, Luis D and Forestier-Roman, Ingrid and Gerena, Yamil and Blanco, Manuel and Rivera-Robles, Michael J and Rodriguez-Medina, José R and Cubano, Luis A and Vlaar, Cornelis P and Dharmawardhane, Suranganie
Molecular Cancer Therapeutics, ISSN 1535-7163, 05/2017, Volume 16, Issue 5, pp. 805 - 818
The Rho GTPases Rac (Ras-related C3 botulinum toxin substrate) and Cdc42 (cell division control protein 42 homolog) regulate cell functions governing cancer... 
P21-ACTIVATED KINASE | EHOP-016 | CELLS | ACTIVATION | ACTIN | ONCOLOGY | RAC | STAT3 | PAK | HUMAN BREAST-CANCER | SMALL-MOLECULE INHIBITOR | Cell Survival - drug effects | Pyrimidines - administration & dosage | Humans | Carbazoles - administration & dosage | Breast Neoplasms - drug therapy | Neovascularization, Pathologic - pathology | Cell Movement - drug effects | Neoplasm Metastasis | Animals | Breast Neoplasms - genetics | Signal Transduction - drug effects | Breast Neoplasms - pathology | Neovascularization, Pathologic - drug therapy | cdc42 GTP-Binding Protein - genetics | cdc42 GTP-Binding Protein - antagonists & inhibitors | rac1 GTP-Binding Protein - antagonists & inhibitors | Cell Line, Tumor | Female | Neovascularization, Pathologic - genetics | Antineoplastic Agents - pharmacology | Cell Proliferation - drug effects | Mice | rac1 GTP-Binding Protein - genetics | Cdc42 protein | Mesenchyme | Epithelial cells | Downstream effects | Homology | AKT protein | Malignancy | Metastasis | Kinases | Cell surface | Metastases | Cell adhesion & migration | Angiogenesis | Actin | Polarity | Mammary gland | Incubation | Stat3 protein | Cell division | p21-activated kinase | MAP kinase | Breast cancer | Botulinum toxin | Substrates | Signaling | Detachment | Inhibitors | Viability | Cell migration | Cancer | Tumors | Apoptosis | anoikis | breast cancer | Rac | Cdc42 inhibitor | Cdc42
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14. Full Text Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation
by Kang, Rujun and Wan, Junmei and Arstikaitis, Pamela and Takahashi, Hideto and Huang, Kun and Bailey, Aaron O and Thompson, James X and Roth, Amy F and Drisdel, Renaldo C and Mastro, Ryan and Green, William N and Yates Iii, John R and Davis, Nicholas G and El-Husseini, Alaa
Nature, ISSN 0028-0836, 12/2008, Volume 456, Issue 7224, pp. 904 - 909
Palmitoylation regulates diverse aspects of neuronal protein trafficking and function. Here a global characterization of rat neural palmitoyl- proteomes... 
CDC42 | RHO-FAMILY GTPASES | MORPHOGENESIS | DENDRITIC SPINE DEVELOPMENT | SYNAPSES | STABILITY | MULTIDISCIPLINARY SCIENCES | TRAFFICKING | PROTEIN PALMITOYLATION | NEURONAL EXCITABILITY | PLASTICITY | Dendrites - metabolism | Lipoylation | Alternative Splicing - genetics | Cells, Cultured | Rats | cdc42 GTP-Binding Protein - metabolism | Organ Specificity | Cerebral Cortex - cytology | Animals | Synapses - metabolism | Cerebral Cortex - embryology | cdc42 GTP-Binding Protein - genetics | Proteomics | Neurons - metabolism | Models, Neurological | Proteome - metabolism | Control | Synthesis | Research | Health aspects | Fatty acids | Protein-protein interactions
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15. Cdc42: helping endothelial cells on the move
Development, ISSN 0950-1991, 07/2018, Volume 145, Issue 13, pp. e1301 - e1301
Cdc42 protein | Endothelial cells
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16. Full Text Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking
by BendezĂș, Felipe O and Vincenzetti, Vincent and Vavylonis, Dimitrios and Wyss, Romain and Vogel, Horst and Martin, Sophie G
PLoS Biology, ISSN 1544-9173, 04/2015, Volume 13, Issue 4, p. e1002097
The small Rho-family GTPase Cdc42 is critical for cell polarization and polarizes spontaneously in absence of upstream spatial cues. Spontaneous polarization... 
SPONTANEOUS CELL POLARIZATION | ELEGANS EMBRYOS | BIOCHEMISTRY & MOLECULAR BIOLOGY | FISSION YEAST-CELL | POLARITY ESTABLISHMENT | FORMIN FOR3P | BIOLOGY | NUCLEOTIDE EXCHANGE FACTOR | FLUORESCENT PROTEIN | NEGATIVE FEEDBACK | SCHIZOSACCHAROMYCES-POMBE | SYMMETRY-BREAKING | Cell Polarity | Schizosaccharomyces - metabolism | cdc42 GTP-Binding Protein - genetics | Guanine Nucleotide Dissociation Inhibitors - metabolism | Actins - metabolism | Alleles | cdc42 GTP-Binding Protein - metabolism | Fluorescent Dyes | Schizosaccharomyces - cytology | Protein Transport | Proteins | Plasma | Kinases | Feedback | Experiments
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