spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Summary Freely available
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Belmont, L. D.
Right arrow Articles by Drubin, D. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Belmont, L. D.
Right arrow Articles by Drubin, D. G.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?
Amberg, D. C., Basart, E. and Botstein, D (1995). Defining protein interactions with yeast actin in vivo. Nature Struct. Biol 2, 28-35.[Medline]

Ayscough, K. R., Stryker, J., Pokala, N., Sanders, M., Crews, P. and Drubin, D. G (1997). High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol 137, 399-416.[Abstract/Free Full Text]

Belmont, L. D. and Drubin, D. G (1998). The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol 142, 1289-1299.[Abstract/Free Full Text]

Belmont, L. D., Orlova, A., Drubin, D. G. and Egelman, E. H (1999). a change in actin conformation associated with filament instability after Pirelease. Proc. Nat. Acad. Sci. USA 96, 29-34.[Abstract/Free Full Text]

Bork, P., Sander, C. and Valencia, A (1992). An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin and hsp70 heat shock proteins. Proc. Nat. Acad. Sci. USA 89, 7290-7294.[Abstract/Free Full Text]

Buchberger, A., Valencia, A., McMacken, R., Sander, C. and Bukau, B (1994). The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J 13, 1687-1695.[Medline]

Carmeli, S., Moore, R. E. and Patterson, G. M (1990). Tolytoxin and new scytophycins from three species of Scytonema. J. Natural Products 53, 1533-1542.[Medline]

Chen, X., Cook, R. K. and Rubenstein, P. A (1993). Yeast actin with a mutation in the \324hydrophobic plug' between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect. J. Cell Biol 123, 1185-1195.[Abstract/Free Full Text]

Chen, X. and Rubenstein, P. A (1995). A mutation in an ATP-binding loopof Saccharomyces cerevisiae actin (S14A) causes a temperature-sensitive phenotype in vivo and in vitro. J. Biol Chem 270, 11406-11414.[Abstract/Free Full Text]

Coue, M., Brenner, S. L., Spector, I. and Korn, E. D (1987). Inhibition of actin polymerization by latrunculin A. FEBS Lett 213, 316-318.[Medline]

Doyle, T. and Botstein, D (1996). Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc. Nat. Acad. Sci. USA 93, 3886-3891.[Abstract/Free Full Text]

Drubin, D. G., Jones, H. D. and Wertman, K. F (1993). Actin structure andfunction: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell 4, 1277-1294.[Abstract]

Flaherty, K. M., McKay, D. B., Kabsch, W. and Holmes, K. C (1991). Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Nat. Acad. Sci. USA 88, 5041-5045.[Abstract/Free Full Text]

Holmes, K. C., Popp, D., Gebhard, W. and Kabsch, W (1990). Atomic model of the actin filament. Nature 347, 44-49.[Medline]

Holtzman, D. A., Wertman, K. F. and Drubin, D. G (1994). Mapping actin surfaces required for functional interactions in vivo. J. Cell Biol 126, 423-432.[Abstract/Free Full Text]

Honts, J. E., Sandrock, T. S., Brower, S. M., O'Dell, J. L. and Adams, A. E (1994). Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin. J. Cell Biol 126, 413-422.[Abstract/Free Full Text]

Ishibashi, M., Moore, R. E., Patterson, G. M. L., Xu, C. and Clardy, J (1986). Scytophycins, cytotoxic antimitotic agents from the cyanophyte Scytonema psuedohofmanni. J. Organic Chem 51, 5300-5306.

Johannes, F. J. and Gallwitz, D (1991). Site-directed mutagenesis of theyeast actin gene: a test for actin function in vivo. EMBO J 10, 3951-3958.[Medline]

Jordan, M. A. and Wilson, L (1998). Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr. Opin. Cell Biol 10, 123-130.[Medline]

Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F. and Holmes, K. C (1990). Atomic structure of the actin: DNase I complex [see comments]. Nature 347, 37-44.[Medline]

Karpova, T. S., McNally, J. G., Moltz, S. L. and Cooper, J. A (1998). Assembly and function of the actin cytoskeleton of yeast: Relationships between cables and patches. J. Cell Biol 142, 1501-1517.[Abstract/Free Full Text]

Kuang, B. and Rubenstein, P. A (1997). Beryllium fluoride and phalloidin restore polymerizability of a mutant yeast actin (V266G, L267G) with severely decreased hydrophobicity in a subdomain 3/4 loop. J. Biol. Chem 272, 1237-1247.[Abstract/Free Full Text]

Kuang, B. and Rubenstein, P. A (1997). The effects of severely decreased hydrophobicity in a subdomain 3/4 loop on the dynamics and stability of yeast G-actin. J. Biol. Chem 272, 4412-4418.[Abstract/Free Full Text]

Lappalainen, P. and Drubin, D. G (1997). Cofilin promotes rapid actin filament turnover in vivo. Nature 388, 78-82.[Medline]

Lappalainen, P., Fedorov, E. V., Fedorov, A. A., Almo, S. C. and Drubin,D. G (1997). Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J 16, 5520-5530.[Medline]

Lorenz, M., Popp, D. and Holmes, K (1993). Refinement of the F-actin model against the X-ray fiber diffraction data by the use of a directed mutation algorithm. J.Mol. Biol 234, 826-836.[Medline]

Miller, C. J., Cheung, P., White, P. and Reisler, E (1995). Actin's view of actomyosin interface. Biophys. J 68, 50-.

Mossakowska, M., Moraczewska, J., Khaitlina, S. and Strzelecka-Golaszewska, H (1993). Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions. Biochem. J 289, 897-902.

Mulholland, J., Preuss, D., Moon, A., Wong, A., Drubin, D., Botstein, D (1994). Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol 125, 381-391.[Abstract/Free Full Text]

Orlova, A., Prochniewicz, E. and Egelman, E. H (1995). Structural dynamics of F-actin: II. Cooperativity in structural transitions. J. Mol. Biol 245, 598-607.[Medline]

Orlova, A., Chen, X., Rubenstein, P. A. and Egelman, E. H (1997). Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. J. Mol. Biol 271, 235-243.[Medline]

Patterson, G. M. and Carmeli, S (1992). Biological effects of tolytoxin (6-hydroxy-7-O-methyl-scytophycin b), a potent bioactive metabolite from cyanobacteria. Arch. Microbiol 157, 406-410.[Medline]

Patterson, G. M., Smith, C. D., Kimura, L. H., Britton, B. A. and Carmeli, S (1993). Action of tolytoxin on cell morphology, cytoskeletal organization and actin polymerization. Cell Motil. Cytoskel 24, 39-48.[Medline]

Ramachandran, N. G. and Sasisekharan, V (1968). Conformation of polypeptides and proteins. Advan. Protein Chem 23, 283-437.[Medline]

Smith, C. D., Carmeli, S., Moore, R. E. and Patterson, G. M (1993). Scytophycins, novel microfilament-depolymerizing agents which circumvent P-glycoprotein-mediated multidrug resistance. Cancer Res 53, 1343-1347.[Abstract/Free Full Text]

Steinmetz, M. O, Stoffler, D., Muller, S., Jahn, W., Wolpensinger, B., Goldie, K., Engel, A., Faulstich, H. and Aebi, A (1998). Evaluating atomic models of F-actin with an unadecagold-tagged phalloidin derivative. J. Mol. Biol 276, 1-6.[Medline]

Strzelecka-Golaszewska, H., Mossakowska, M., Wolzniak, A., Moraczewska, J. and Nakayama, H (1995). Long-range conformational effects of proteolytic removal of the last three residues of actin. Biochem. J 307, 527-534.

Vandekerckhove, J., Debonen, A., Nasssal, M., Wieland, T (1985). The phalloidin binding site of F-actin. EMBO J 4, 2815-2818.[Medline]

Wertman, K. F., Drubin, D. G. and Botstein, D (1992). Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350.[Abstract]


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
Mol. Biol. CellHome page
S. A. Dighe and K. G. Kozminski
Swf1p, a Member of the DHHC-CRD Family of Palmitoyltransferases, Regulates the Actin Cytoskeleton and Polarized Secretion Independently of Its DHHC Motif
Mol. Biol. Cell, October 1, 2008; 19(10): 4454 - 4468.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Iwasa, K. Maeda, A. Narita, Y. Maeda, and T. Oda
Dual Roles of Gln137 of Actin Revealed by Recombinant Human Cardiac Muscle {alpha}-Actin Mutants
J. Biol. Chem., July 25, 2008; 283(30): 21045 - 21053.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
R. S. O'Connor, C. M. Steeds, R. W. Wiseman, and G. K. Pavlath
Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion
J. Physiol., June 15, 2008; 586(12): 2841 - 2853.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. M. Gheorghe, S. Aghamohammadzadeh, I. I. S.-d. Rooij, E. G. Allwood, S. J. Winder, and K. R. Ayscough
Interactions between the Yeast SM22 Homologue Scp1 and Actin Demonstrate the Importance of Actin Bundling in Endocytosis
J. Biol. Chem., May 30, 2008; 283(22): 15037 - 15046.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
G. Ren, P. Vajjhala, J. S. Lee, B. Winsor, and A. L. Munn
The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy
Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 37 - 120.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
E. E. Ganusova, L. N. Ozolins, S. Bhagat, G. P. Newnam, R. D. Wegrzyn, M. Y. Sherman, and Y. O. Chernoff
Modulation of Prion Formation, Aggregation, and Toxicity by the Actin Cytoskeleton in Yeast
Mol. Cell. Biol., January 15, 2006; 26(2): 617 - 629.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
S. W. Clark and M. D. Rose
Alanine Scanning of Arp1 Delineates a Putative Binding Site for Jnm1/Dynamitin and Nip100/p150Glued
Mol. Biol. Cell, September 1, 2005; 16(9): 3999 - 4012.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
A. C. Martin, X.-P. Xu, I. Rouiller, M. Kaksonen, Y. Sun, L. Belmont, N. Volkmann, D. Hanein, M. Welch, and D. G. Drubin
Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function
J. Cell Biol., January 17, 2005; 168(2): 315 - 328.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
J. Karagiannis, A. Bimbo, S. Rajagopalan, J. Liu, and M. K. Balasubramanian
The Nuclear Kinase Lsk1p Positively Regulates the Septation Initiation Network and Promotes the Successful Completion of Cytokinesis in Response to Perturbation of the Actomyosin Ring in Schizosaccharomyces pombe
Mol. Biol. Cell, January 1, 2005; 16(1): 358 - 371.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
B. K. Haarer and D. C. Amberg
Old Yellow Enzyme Protects the Actin Cytoskeleton from Oxidative Stress
Mol. Biol. Cell, October 1, 2004; 15(10): 4522 - 4531.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
C. W. Gourlay, L. N. Carpp, P. Timpson, S. J. Winder, and K. R. Ayscough
A role for the actin cytoskeleton in cell death and aging in yeast
J. Cell Biol., March 15, 2004; 164(6): 803 - 809.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. W. Krauss, C. Chen, S. Penman, and R. Heald
Nuclear actin and protein 4.1: Essential interactions during nuclear assembly in vitro
PNAS, September 16, 2003; 100(19): 10752 - 10757.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. Kubanek, P. R. Jensen, P. A. Keifer, M. C. Sullards, D. O. Collins, and W. Fenical
Seaweed resistance to microbial attack: A targeted chemical defense against marine fungi
PNAS, June 10, 2003; 100(12): 6916 - 6921.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Pendleton, B. Pope, A. Weeds, and A. Koffer
Latrunculin B or ATP Depletion Induces Cofilin-dependent Translocation of Actin into Nuclei of Mast Cells
J. Biol. Chem., April 11, 2003; 278(16): 14394 - 14400.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
B. W. Bernstein and J. R. Bamburg
Actin-ATP Hydrolysis Is a Major Energy Drain for Neurons
J. Neurosci., January 1, 2003; 23(1): 1 - 6.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
G. Posern, A. Sotiropoulos, and R. Treisman
Mutant Actins Demonstrate a Role for Unpolymerized Actin in Control of Transcription by Serum Response Factor
Mol. Biol. Cell, December 1, 2002; 13(12): 4167 - 4178.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
G. Eitzen, L. Wang, N. Thorngren, and W. Wickner
Remodeling of organelle-bound actin is required for yeast vacuole fusion
J. Cell Biol., August 28, 2002; 158(4): 669 - 679.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
D. A. Ammar, P. N. B. Nguyen, and J. G. Forte
Functionally distinct pools of actin in secretory cells
Am J Physiol Cell Physiol, August 1, 2001; 281(2): C407 - C417.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
J. A. Lunn, H. Wong, E. Rozengurt, and J. H. Walsh
Requirement of cortical actin organization for bombesin, endothelin, and EGF receptor internalization
Am J Physiol Cell Physiol, December 1, 2000; 279(6): C2019 - C2027.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
A. K. Wolven, L. D. Belmont, N. M. Mahoney, S. C. Almo, and D. G. Drubin
In Vivo Importance of Actin Nucleotide Exchange Catalyzed by Profilin
J. Cell Biol., August 21, 2000; 150(4): 895 - 904.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. G. Yarmola, T. Somasundaram, T. A. Boring, I. Spector, and M. R. Bubb
Actin-Latrunculin A Structure and Function. DIFFERENTIAL MODULATION OF ACTIN-BINDING PROTEIN FUNCTION BY LATRUNCULIN A
J. Biol. Chem., September 1, 2000; 275(36): 28120 - 28127.
[Abstract] [Full Text] [PDF]


This Article
Right arrow Summary Freely available
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Belmont, L. D.
Right arrow Articles by Drubin, D. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Belmont, L. D.
Right arrow Articles by Drubin, D. G.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?