James M. Hogle

Details der Publikationsliste

Zeitraum

2005 - 2007

Anzahl

29

Co-Autoren

Imaging Poliovirus Entry in Live Cells (2007)

Boerries Brandenburg, Lily Y. Lee, Melike Lakadamyali, Michael J. Rust, Xiaowei Zhuang, James M. Hogle

Viruses initiate infection by transferring their genetic material across a cellular membrane and into the appropriate compartment of the cell. The mechanisms by which animal viruses, especially...

Binding of herpes simplex virus-1 US11 to specific RNA sequences (2005)

Bryant, Kevin F., Cox, J. Colin, Wang, Hongming, Hogle, James M., Ellington, Andrew D., Coen, Donald M.

Herpes simplex virus-1 US11 is a RNA-binding protein with a novel RNA-binding domain. US11 has been reported to exhibit sequence- and conformation-specific RNA-binding, but the sequences and...

Three-dimensional structure of poliovirus receptor bound to poliovirus

Belnap, David M., McDermott, Brian M., Filman, David J., Cheng, Naiqian, Trus, Benes L., Zuccola, Harmon J., ...

Poliovirus initiates infection by binding to its cellular receptor (Pvr). We have studied this interaction by using cryoelectron microscopy to determine the structure, at 21-Å resolution, of...

The Poliovirus Empty Capsid Specifically Recognizes the Poliovirus Receptor and Undergoes Some, but Not All, of the Transitions Associated with Cell Entry

Basavappa, Ravi, Gómez-Yafal, Alicia, Hogle, James M.

Experimental results presented here demonstrate that the poliovirus empty capsid binds with saturable character to poliovirus-susceptible cells, binds preferentially to susceptible cells, and...

Molecular Tectonic Model of Virus Structural Transitions: the Putative Cell Entry States of Poliovirus

Belnap, David M., Filman, David J., Trus, Benes L., Cheng, Naiqian, Booy, Frank P., Conway, James F., ...

Upon interacting with its receptor, poliovirus undergoes conformational changes that are implicated in cell entry, including the externalization of the viral protein VP4 and the N terminus of VP1. We...

Poliovirus Mutants at Histidine 195 of VP2 Do Not Cleave VP0 into VP2 and VP4

Hindiyeh, Musa, Li, Qi-Han, Basavappa, Ravi, Hogle, James M., Chow, Marie

The final stage of poliovirus assembly is characterized by a cleavage of the capsid precursor protein VP0 into VP2 and VP4. This cleavage is thought to be autocatalytic and dependent on RNA...

Molecular Genetic Analysis of Revertants from a Poliovirus Mutant That Is Specifically Adapted to the Mouse Spinal Cord

Jia, Qingmei, Hogle, James M., Hashikawa, Tsutomu, Nomoto, Akio

SA virus, a mutant of the Mahoney strain of type 1 poliovirus (PV1/Mahoney), replicates specifically in the spinal cords of mice and causes paralysis, although the PV1/Mahoney strain does not show...

Kinetic Analysis of the Effect of Poliovirus Receptor on Viral Uncoating: the Receptor as a Catalyst

Tsang, Simon K., McDermott, Brian M., Racaniello, Vincent R., Hogle, James M.

We examined the role of soluble poliovirus receptor on the transition of native poliovirus (160S or N particle) to an infectious intermediate (135S or A particle). The viral receptor behaves as a...

Is the 135S Poliovirus Particle an Intermediate during Cell Entry?

Huang, Yan, Hogle, James M., Chow, Marie

Poliovirus binding to its receptor (PVR) on the cell surface induces a conformational transition which generates an altered particle with a sedimentation value of 135S versus the 160S of the native...

Residues of Human Cytomegalovirus DNA Polymerase Catalytic Subunit UL54 That Are Necessary and Sufficient for Interaction with the Accessory Protein UL44

Loregian, Arianna, Appleton, Brent A., Hogle, James M., Coen, Donald M.

The human cytomegalovirus DNA polymerase contains a catalytic subunit, UL54, and an accessory protein, UL44. Recent studies suggested that UL54 might interact via its extreme C terminus with UL44 (A....

Specific Residues in the Connector Loop of the Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 Are Crucial for Interaction with the UL54 Catalytic Subunit

Loregian, Arianna, Appleton, Brent A., Hogle, James M., Coen, Donald M.

The human cytomegalovirus DNA polymerase includes an accessory protein, UL44, which has been proposed to act as a processivity factor for the catalytic subunit, UL54. How UL44 interacts with UL54 has...

The Structure of the Poliovirus 135S Cell Entry Intermediate at 10-Angstrom Resolution Reveals the Location of an Externalized Polypeptide That Binds to Membranes†

Bubeck, Doryen, Filman, David J., Cheng, Naiqian, Steven, Alasdair C., Hogle, James M., Belnap, David M.

Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational...

Binding of herpes simplex virus-1 US11 to specific RNA sequences

Bryant, Kevin F., Cox, J. Colin, Wang, Hongming, Hogle, James M., Ellington, Andrew D., Coen, Donald M.

Herpes simplex virus-1 US11 is a RNA-binding protein with a novel RNA-binding domain. US11 has been reported to exhibit sequence- and conformation-specific RNA-binding, but the sequences and...

Characterization of Early Steps in the Poliovirus Infection Process: Receptor-Decorated Liposomes Induce Conversion of the Virus to Membrane-Anchored Entry-Intermediate Particles

Tuthill, Tobias J., Bubeck, Doryen, Rowlands, David J., Hogle, James M.

The mechanism by which poliovirus infects the cell has been characterized by a combination of biochemical and structural studies, leading to a working model for cell entry. Upon receptor binding at...

Three-dimensional structure of poliovirus receptor bound to poliovirus

Belnap, David M., McDermott, Brian M., Filman, David J., Cheng, Naiqian, Trus, Benes L., Zuccola, Harmon J., ...

Poliovirus initiates infection by binding to its cellular receptor (Pvr). We have studied this interaction by using cryoelectron microscopy to determine the structure, at 21-Å resolution, of...

The Poliovirus Empty Capsid Specifically Recognizes the Poliovirus Receptor and Undergoes Some, but Not All, of the Transitions Associated with Cell Entry

Basavappa, Ravi, Gómez-Yafal, Alicia, Hogle, James M.

Experimental results presented here demonstrate that the poliovirus empty capsid binds with saturable character to poliovirus-susceptible cells, binds preferentially to susceptible cells, and...

Molecular Tectonic Model of Virus Structural Transitions: the Putative Cell Entry States of Poliovirus

Belnap, David M., Filman, David J., Trus, Benes L., Cheng, Naiqian, Booy, Frank P., Conway, James F., ...

Upon interacting with its receptor, poliovirus undergoes conformational changes that are implicated in cell entry, including the externalization of the viral protein VP4 and the N terminus of VP1. We...

Poliovirus Mutants at Histidine 195 of VP2 Do Not Cleave VP0 into VP2 and VP4

Hindiyeh, Musa, Li, Qi-Han, Basavappa, Ravi, Hogle, James M., Chow, Marie

The final stage of poliovirus assembly is characterized by a cleavage of the capsid precursor protein VP0 into VP2 and VP4. This cleavage is thought to be autocatalytic and dependent on RNA...

Molecular Genetic Analysis of Revertants from a Poliovirus Mutant That Is Specifically Adapted to the Mouse Spinal Cord

Jia, Qingmei, Hogle, James M., Hashikawa, Tsutomu, Nomoto, Akio

SA virus, a mutant of the Mahoney strain of type 1 poliovirus (PV1/Mahoney), replicates specifically in the spinal cords of mice and causes paralysis, although the PV1/Mahoney strain does not show...

Kinetic Analysis of the Effect of Poliovirus Receptor on Viral Uncoating: the Receptor as a Catalyst

Tsang, Simon K., McDermott, Brian M., Racaniello, Vincent R., Hogle, James M.

We examined the role of soluble poliovirus receptor on the transition of native poliovirus (160S or N particle) to an infectious intermediate (135S or A particle). The viral receptor behaves as a...

Is the 135S Poliovirus Particle an Intermediate during Cell Entry?

Huang, Yan, Hogle, James M., Chow, Marie

Poliovirus binding to its receptor (PVR) on the cell surface induces a conformational transition which generates an altered particle with a sedimentation value of 135S versus the 160S of the native...

Residues of Human Cytomegalovirus DNA Polymerase Catalytic Subunit UL54 That Are Necessary and Sufficient for Interaction with the Accessory Protein UL44

Loregian, Arianna, Appleton, Brent A., Hogle, James M., Coen, Donald M.

The human cytomegalovirus DNA polymerase contains a catalytic subunit, UL54, and an accessory protein, UL44. Recent studies suggested that UL54 might interact via its extreme C terminus with UL44 (A....

Specific Residues in the Connector Loop of the Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 Are Crucial for Interaction with the UL54 Catalytic Subunit

Loregian, Arianna, Appleton, Brent A., Hogle, James M., Coen, Donald M.

The human cytomegalovirus DNA polymerase includes an accessory protein, UL44, which has been proposed to act as a processivity factor for the catalytic subunit, UL54. How UL44 interacts with UL54 has...

The Structure of the Poliovirus 135S Cell Entry Intermediate at 10-Angstrom Resolution Reveals the Location of an Externalized Polypeptide That Binds to Membranes†

Bubeck, Doryen, Filman, David J., Cheng, Naiqian, Steven, Alasdair C., Hogle, James M., Belnap, David M.

Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational...

Binding of herpes simplex virus-1 US11 to specific RNA sequences

Bryant, Kevin F., Cox, J. Colin, Wang, Hongming, Hogle, James M., Ellington, Andrew D., Coen, Donald M.

Herpes simplex virus-1 US11 is a RNA-binding protein with a novel RNA-binding domain. US11 has been reported to exhibit sequence- and conformation-specific RNA-binding, but the sequences and...

Characterization of Early Steps in the Poliovirus Infection Process: Receptor-Decorated Liposomes Induce Conversion of the Virus to Membrane-Anchored Entry-Intermediate Particles

Tuthill, Tobias J., Bubeck, Doryen, Rowlands, David J., Hogle, James M.

The mechanism by which poliovirus infects the cell has been characterized by a combination of biochemical and structural studies, leading to a working model for cell entry. Upon receptor binding at...

Imaging Poliovirus Entry in Live Cells

Brandenburg, Boerries, Lee, Lily Y, Lakadamyali, Melike, Rust, Michael J, Zhuang, Xiaowei, Hogle, James M

Viruses initiate infection by transferring their genetic material across a cellular membrane and into the appropriate compartment of the cell. The mechanisms by which animal viruses, especially...

Crystal Structure of Poliovirus 3CD Protein: Virally Encoded Protease and Precursor to the RNA-Dependent RNA Polymerase▿

Marcotte, Laura L., Wass, Amanda B., Gohara, David W., Pathak, Harsh B., Arnold, Jamie J., Filman, David J., ...

Poliovirus 3CD is a multifunctional protein that serves as a precursor to the protease 3Cpro and the viral polymerase 3Dpol and also plays a role in the control of viral replication. Although 3CD is...

Biochemical, Biophysical, and Mutational Analyses of Subunit Interactions of the Human Cytomegalovirus Nuclear Egress Complex▿

Sam, My D., Evans, Brady T., Coen, Donald M., Hogle, James M.

Nuclear egress, the trafficking of herpesvirus nucleocapsids from the nucleus to the cytoplasm, involves two conserved viral proteins that form a complex at the nuclear envelope, referred to as the...