F. Jon Kull

Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium (2002)

Tsiavaliaris,Georgios, Fujita-Becker,Setsuko, Batra,Renu, Levitsky,Dmitrii I., Kull,F. Jon, Geeves,Michael A., ...

Dominant-negative inhibition is a powerful genetic tool for the characterization of gene function in vivo, based on the specific impairment of a gene product by the coexpression of a mutant version...

Crystal structure of the motor domain of a class-I myosin (2002)

Kollmar,Martin, Dürrwang,Ulrike, Kliche,Werner, Manstein,Dietmar J., Kull,F. Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Switch 1 opens on strong binding to actin (2002)

Holmes,Kenneth C., Kull,F. Jon, Schröder,Rasmus R.

The 50K domain of the myosin cross bridge is split into two subdomains (upper and lower) by the major cleft that connects the actin binding site with the nucleotide binding site. A number of lines of...

Crystal structure of the motor domain of a class-I myosin (2002)

Kollmar, Martin, Dürrwang, Ulrike, Kliche, Werner, Manstein, Dietmar J., Kull, F. Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Switch 1 opens on strong binding to actin (2002)

Holmes, Kenneth C., Kull, F. Jon, Schröder, Rasmus R.

The 50K domain of the myosin cross bridge is split into two subdomains (upper and lower) by the major cleft that connects the actin binding site with the nucleotide binding site. A number of lines of...

Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium (2002)

Tsiavaliaris, Georgios, Fujita-Becker, Setsuko, Batra, Renu, Levitsky, Dmitrii I., Kull, F. Jon, Geeves, Michael A., ...

Dominant-negative inhibition is a powerful genetic tool for the characterization of gene function in vivo, based on the specific impairment of a gene product by the coexpression of a mutant version...

Structure of a genetically engineered molecular motor (2001)

Kliche,Werner, Fujita-Becker,Setsuko, Kollmar,Martin, Manstein,Dietmar J., Kull,F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of a dynamin GTPase domain (2001)

Niemann,Hartmut H., Knetsch,Menno L. W., Scherer,Anna, Manstein,Dietmar J., Kull,F. Jon

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating...

Structure of a genetically engineered molecular motor (2001)

Kliche,Werner, Fujita-Becker,Setsuko, Kollmar,Martin, Manstein,Dietmar J., Kull,F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of a dynamin GTPase domain (2001)

Niemann,Hartmut H., Knetsch,Menno L. W., Scherer,Anna, Manstein,Dietmar J., Kull,F. Jon

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating...

Structure of a genetically engineered molecular motor (2001)

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of a dynamin GTPase domain (2001)

Niemann, Hartmut H., Knetsch, Menno L. W., Scherer, Anna, Manstein, Dietmar J., Kull, F. Jon

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating...

Structure of a genetically engineered molecular motor (2001)

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F. Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of a dynamin GTPase domain (2001)

Niemann, Hartmut H., Knetsch, Menno L. W., Scherer, Anna, Manstein, Dietmar J., Kull, F. Jon

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating...

Motor proteins of the kinesin superfamily: structure and mechanism (2000)

Kull, F. Jon

Motor proteins of the kinesin family: Structures, variations, and nucleotide binding sites (1999)

Sack,S., Kull,F. Jon, Mandelkow,Eckhart

Motor proteins of the kinesin family: Structures, variations, and nucleotide binding sites (1999)

Sack, S., Kull, F. Jon, Mandelkow, Eckhart

Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms

Niemann, Hartmut H., Knetsch, Menno L.W., Scherer, Anna, Manstein, Dietmar J., Kull, F.Jon

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating...

Crystal structure of the motor domain of a class-I myosin

Kollmar, Martin, Dürrwang, Ulrike, Kliche, Werner, Manstein, Dietmar J., Kull, F.Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Structure of a genetically engineered molecular motor

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F.Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of the GTPase domain of rat dynamin 1

Reubold, Thomas F., Eschenburg, Susanne, Becker, Andreas, Leonard, Marilyn, Schmid, Sandra L., Vallee, Richard B., ...

Here, we present the 1.9-Å crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold...

Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium

Tsiavaliaris, Georgios, Fujita-Becker, Setsuko, Batra, Renu, Levitsky, Dmitrii I., Kull, F. Jon, Geeves, Michael A., ...

Dominant-negative inhibition is a powerful genetic tool for the characterization of gene function in vivo, based on the specific impairment of a gene product by the coexpression of a mutant version...

Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium

Tsiavaliaris, Georgios, Fujita-Becker, Setsuko, Batra, Renu, Levitsky, Dmitrii I., Kull, F. Jon, Geeves, Michael A., ...

Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms

Niemann, Hartmut H., Knetsch, Menno L.W., Scherer, Anna, Manstein, Dietmar J., Kull, F.Jon

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating...

Crystal structure of the motor domain of a class-I myosin

Kollmar, Martin, Dürrwang, Ulrike, Kliche, Werner, Manstein, Dietmar J., Kull, F.Jon

The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently...

Structure of a genetically engineered molecular motor

Kliche, Werner, Fujita-Becker, Setsuko, Kollmar, Martin, Manstein, Dietmar J., Kull, F.Jon

Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the...

Crystal structure of the GTPase domain of rat dynamin 1

Reubold, Thomas F., Eschenburg, Susanne, Becker, Andreas, Leonard, Marilyn, Schmid, Sandra L., Vallee, Richard B., ...

Here, we present the 1.9-Å crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold...

Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium

Tsiavaliaris, Georgios, Fujita-Becker, Setsuko, Batra, Renu, Levitsky, Dmitrii I., Kull, F. Jon, Geeves, Michael A., ...

Dominant-negative inhibition is a powerful genetic tool for the characterization of gene function in vivo, based on the specific impairment of a gene product by the coexpression of a mutant version...

Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium

Tsiavaliaris, Georgios, Fujita-Becker, Setsuko, Batra, Renu, Levitsky, Dmitrii I., Kull, F. Jon, Geeves, Michael A., ...

Crystal Structure of the Vibrio cholerae Quorum-Sensing Regulatory Protein HapR▿

De Silva, Rukman S., Kovacikova, Gabriela, Lin, Wei, Taylor, Ronald K., Skorupski, Karen, Kull, F. Jon

Quorum sensing in Vibrio cholerae involves signaling between two-component sensor protein kinases and the response regulator LuxO to control the expression of the master regulator HapR. HapR, in...