User:Steven J. Koch/Articles to read

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Articles can be added either by categorizing other pages, or by just manually adding below.
Articles can be added either by categorizing other pages, or by just manually adding below.
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* PMID 16604065 "Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro."
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* PMID 16604065 "Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro." Valentine MT, Fordyce PM, Krzysiak TC, Gilbert SP, Block SMNat Cell Biol 2006 May 8(5):470-6  
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Valentine MT, Fordyce PM, Krzysiak TC, Gilbert SP, Block SM
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Nat Cell Biol 2006 May 8(5):470-6  
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Revision as of 13:44, 17 May 2009

Articles can be added either by categorizing other pages, or by just manually adding below.

  • PMID 16604065 "Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro." Valentine MT, Fordyce PM, Krzysiak TC, Gilbert SP, Block SM. Nat Cell Biol 2006 May 8(5):470-6


  • PMID 7698310 Phase separation in cytoplasm, due to macromolecular crowding, is the basis for microcompartmentation. Walter H, Brooks DE.Laboratory of Chemical Biology 151, Veterans Affairs Medical Center, Long Beach, CA 90822-5201. "The macromolecular diversity and concentrations in the fluid phase of cytoplasm constitute conditions necessary and sufficient for aqueous phase separation. Consequences of phase separation in cytoplasm, including its 'compartmentation', are inferred from analogies with the physicochemical properties of aqueous two-phase systems and with the partitioning behavior of biomaterials in them."
  • PMID 16100275 Radial compression of microtubules and the mechanism of action of taxol and associated proteins. Needleman DJ, Ojeda-Lopez MA, Raviv U, Ewert K, Miller HP, Wilson L, Safinya CR. Materials Department, University of California, Santa Barbara, CA 93106, USA. Microtubules (MTs) are hollow cylindrical polymers composed of alphabeta-tubulin heterodimers that align head-to-tail in the MT wall, forming linear protofilaments that interact laterally. We introduce a probe of the interprotofilament interactions within MTs and show that this technique gives insight into the mechanisms by which MT-associated proteins (MAPs) and taxol stabilize MTs. In addition, we present further measurements of the mechanical properties of MT walls, MT-MT interactions, and the entry of polymers into the MT lumen. These results are obtained from a synchrotron small angle x-ray diffraction (SAXRD) study of MTs under osmotic stress. Above a critical osmotic pressure, P(cr), we observe rectangular bundles of MTs whose cross sections have buckled to a noncircular shape; further increases in pressure continue to distort MTs elastically. The P(cr) of approximately 600 Pa provides, for the first time, a measure of the bending modulus of the interprotofilament bond within an MT. The presence of neuronal MAPs greatly increases P(cr), whereas surprisingly, the cancer chemotherapeutic drug taxol, which suppresses MT dynamics and inhibits MT depolymerization, does not affect the interprotofilament interactions. This SAXRD-osmotic stress technique, which has enabled measurements of the mechanical properties of MTs, should find broad application for studying interactions between MTs and of MTs with MAPs and MT-associated drugs.
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