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Journal Articles

Linking Ras to myosin function: RasGEF Q, a Dictyostelium exchange factor for RasB, affects myosin II functions

Subhanjan Mondal, Deenadayalan Bakthavatsalam, Paul Steimle, Berthold Gassen, Francisco Rivero, Angelika A. Noegel

J Cell Biol (2008) 181 (5): 747–760.

DOI: https://doi.org/10.1083/jcb.200710111

Published: 26 May 2008

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Includes: Supplementary data

Journal Articles

Identification of a Suppressor of the Dictyostelium Profilin-minus Phenotype as a CD36/LIMP-II Homologue

Iakowos Karakesisoglou, Klaus-Peter Janssen, Ludwig Eichinger, Angelika A. Noegel, Michael Schleicher

J Cell Biol (1999) 145 (1): 167–181.

DOI: https://doi.org/10.1083/jcb.145.1.167

Published: 05 April 1999

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Journal Articles

Interaptin, an Actin-binding Protein of the α-Actinin Superfamily in Dictyostelium discoideum, Is Developmentally and cAMP-regulated and Associates with Intracellular Membrane Compartments

Francisco Rivero, Adam Kuspa, Regine Brokamp, Monika Matzner, Angelika A. Noegel

J Cell Biol (1998) 142 (3): 735–750.

DOI: https://doi.org/10.1083/jcb.142.3.735

Published: 10 August 1998

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Journal Articles

Dictyostelium discoideum cells lacking the 34,000-dalton actin-binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy.

F Rivero, R Furukawa, A A Noegel, M Fechheimer

J Cell Biol (1996) 135 (4): 965–980.

DOI: https://doi.org/10.1083/jcb.135.4.965

Published: 15 November 1996

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Journal Articles

Lack of beta 1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts.

R Fässler, M Pfaff, J Murphy, A A Noegel, S Johansson, R Timpl, R Albrecht

J Cell Biol (1995) 128 (5): 979–988.

DOI: https://doi.org/10.1083/jcb.128.5.979

Published: 01 March 1995

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Journal Articles

The actin-binding protein comitin (p24) is a component of the Golgi apparatus.

O H Weiner, J Murphy, G Griffiths, M Schleicher, A A Noegel

J Cell Biol (1993) 123 (1): 23–34.

DOI: https://doi.org/10.1083/jcb.123.1.23

Published: 01 October 1993

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Journal Articles

The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis.

W Witke, A Hofmann, B Köppel, M Schleicher, A A Noegel

J Cell Biol (1993) 121 (3): 599–606.

DOI: https://doi.org/10.1083/jcb.121.3.599

Published: 01 May 1993

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Journal Articles

Domain structure in actin-binding proteins: expression and functional characterization of truncated severin.

L Eichinger, A A Noegel, M Schleicher

J Cell Biol (1991) 112 (4): 665–676.

DOI: https://doi.org/10.1083/jcb.112.4.665

Published: 15 February 1991

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Journal Articles

A Dictyostelium mutant lacking an F-actin cross-linking protein, the 120-kD gelation factor.

M Brink, G Gerisch, G Isenberg, A A Noegel, J E Segall, E Wallraff, M Schleicher

J Cell Biol (1990) 111 (4): 1477–1489.

DOI: https://doi.org/10.1083/jcb.111.4.1477

Published: 01 October 1990

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Journal Articles

Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases.

L Bomblies, E Biegelmann, V Döring, G Gerisch, H Krafft-Czepa, A A Noegel, M Schleicher, B M Humbel

J Cell Biol (1990) 110 (3): 669–679.

DOI: https://doi.org/10.1083/jcb.110.3.669

Published: 01 March 1990

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Journal Articles

The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation.

A A Noegel, S Rapp, F Lottspeich, M Schleicher, M Stewart

J Cell Biol (1989) 109 (2): 607–618.

DOI: https://doi.org/10.1083/jcb.109.2.607

Published: 01 August 1989

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Journal Articles

A Dictyostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis.

E André, M Brink, G Gerisch, G Isenberg, A Noegel, M Schleicher, J E Segall, E Wallraff

J Cell Biol (1989) 108 (3): 985–995.

DOI: https://doi.org/10.1083/jcb.108.3.985

Published: 01 March 1989

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Journal Articles

Studies on the transcription, translation, and structure of alpha-actinin in Dictyostelium discoideum.

W Witke, M Schleicher, F Lottspeich, A Noegel

J Cell Biol (1986) 103 (3): 969–975.

DOI: https://doi.org/10.1083/jcb.103.3.969

Published: 01 September 1986

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NARROW

Linking Ras to myosin function: RasGEF Q, a Dictyostelium exchange factor for RasB, affects myosin II functions

Identification of a Suppressor of the Dictyostelium Profilin-minus Phenotype as a CD36/LIMP-II Homologue

Interaptin, an Actin-binding Protein of the α-Actinin Superfamily in Dictyostelium discoideum, Is Developmentally and cAMP-regulated and Associates with Intracellular Membrane Compartments

Dictyostelium discoideum cells lacking the 34,000-dalton actin-binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy.

Lack of beta 1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts.

The actin-binding protein comitin (p24) is a component of the Golgi apparatus.

The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis.

Domain structure in actin-binding proteins: expression and functional characterization of truncated severin.

A Dictyostelium mutant lacking an F-actin cross-linking protein, the 120-kD gelation factor.

Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases.

The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation.

A Dictyostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxis.

Studies on the transcription, translation, and structure of alpha-actinin in Dictyostelium discoideum.

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