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Research paper thumbnail of Inhibition of Protein Phosphatase Activity Induces p53-dependent Apoptosis in the Absence of p53 Transactivation

Journal of Biological Chemistry, 1997

Research paper thumbnail of Inhibition of Protein Phosphatase Activity Induces p53-dependent Apoptosis in the Absence of p53 Transactivation

Journal of Biological Chemistry, 1997

Research paper thumbnail of Mass flow measurement of bulk solids in pneumatic pipelines

Research paper thumbnail of Crystal Structure of the Repetitive Segments of Spectrin

Science, 1993

The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain t... more The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.

Research paper thumbnail of Structure of simian virus 40 at 3.8-Å resolution

Nature, 1991

The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of v... more The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of viral protein VP1, which form the outer shell, have identical conformations except for the C-terminal arms of their subunits. Five arms emerge from each pentamer and insert into neighbouring pentamers. This tying together of standard building blocks allows for the required variability in packing geometry without sacrificing specificity.

Research paper thumbnail of Inhibition of Protein Phosphatase Activity Induces p53-dependent Apoptosis in the Absence of p53 Transactivation

Journal of Biological Chemistry, 1997

Research paper thumbnail of Inhibition of Protein Phosphatase Activity Induces p53-dependent Apoptosis in the Absence of p53 Transactivation

Journal of Biological Chemistry, 1997

Research paper thumbnail of Mass flow measurement of bulk solids in pneumatic pipelines

Research paper thumbnail of Crystal Structure of the Repetitive Segments of Spectrin

Science, 1993

The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain t... more The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.

Research paper thumbnail of Structure of simian virus 40 at 3.8-Å resolution

Nature, 1991

The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of v... more The crystallographically determined structure of simian virus 40 shows that the 72 pentamers of viral protein VP1, which form the outer shell, have identical conformations except for the C-terminal arms of their subunits. Five arms emerge from each pentamer and insert into neighbouring pentamers. This tying together of standard building blocks allows for the required variability in packing geometry without sacrificing specificity.

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