182 resultados para melinda
Resumo:
X-ray diffraction and other biophysical tools reveal features of the atomic structure of an amyloid-like crystal. Sup35, a prion-like protein in yeast, forms fibrillar amyloid assemblies intrinsic to its prion function. We have identified a polar peptide from the N-terminal prion-determining domain of Sup35 that exhibits the amyloid properties of full-length Sup35, including cooperative kinetics of aggregation, fibril formation, binding of the dye Congo red, and the characteristic cross-β x-ray diffraction pattern. Microcrystals of this peptide also share the principal properties of the fibrillar amyloid, including a highly stable, β-sheet-rich structure and the binding of Congo red. The x-ray powder pattern of the microcrystals, extending to 0.9-Å resolution, yields the unit cell dimensions of the well-ordered structure. These dimensions restrict possible atomic models of this amyloid-like structure and demonstrate that it forms packed, parallel-stranded β-sheets. The unusually high density of the crystals shows that the packed β-sheets are dehydrated, despite the polar character of the side chains. These results suggest that amyloid is a highly intermolecularly bonded, dehydrated array of densely packed β-sheets. This dry β-sheet could form as Sup35 partially unfolds to expose the peptide, permitting it to hydrogen-bond to the same peptide of other Sup35 molecules. The implication is that amyloid-forming units may be short segments of proteins, exposed for interactions by partial unfolding.
Resumo:
Puede ser de gran valor crear un espacio dentro de la respuesta humanitaria para invertir en intervenciones que vayan más allá del abordaje de las necesidades y los riesgos inmediatos. Esto ocurre, en particular, en relación con el empoderamiento de las mujeres.
Resumo:
Heme, iron (Fe) protoporphyrin IX, functions as a prosthetic group in a range of hemoproteins essential to support life under aerobic conditions. The Fe contained within the prosthetic heme groups of these hemoproteins can catalyze the production of reactive oxygen species. Presumably for this reason, heme must be sequestered within those hemoproteins, thereby shielding the reactivity of its Fe-heme. However, under pathologic conditions associated with oxidative stress, some hemoproteins can release their prosthetic heme groups. While this heme is not necessarily damaging per se, it becomes highly cytotoxic in the presence of a range of inflammatory mediators such as tumor necrosis factor. This can lead to tissue damage and, as such, exacerbate the pathologic outcome of several immune-mediated inflammatory conditions. Presumably, targeting "free heme" may be used as a therapeutic intervention against these diseases.
Resumo:
front row: Janet Wilson, Jan Karzen, Barb Selden, Missy Pollick, Melinda Fertig
back row: Judy Boyle, Elaine Crosby, Debbie Rentschler, Ann Kercher, Kathy Karzen, coach John Atwood
Resumo:
Front Row: Karmen Lappo, Jamie Gillies, Melissa Gentile (co-captain), Pam Kosanke (co-captain),
Second Row: Kate Eiland, Marissa Young, Courtney Murdock, Melinda Moulden, Meghan Doe, Marie Barda, Mary Conner.
Third Row: Liz Elsner, Chrissy Garza, Rebecca Tune, Kelsey Kollen, Stefanie Volpe,
Top Row: Melissa Taylor, Lisa Mack, Kim Bugel.
Resumo:
Back Row: head coach Carmel Borders, Terry Conlin, Linda Gardener, Kathryn Young, Karen Gilhooly, Sheila Butler, ass't coach Jane Bennett
Front Row: trainer Polly Germanout, Peggy Kopmeyer, Melinda Fertig, Carol Klomparens, Lydia Sims, Jeanmarie Otto, Denise Cameron, Laura Pierie
Resumo:
National Highway Traffic Safety Administration, Washington, D.C.
Resumo:
National Highway Traffic Safety Administration, Washington, D.C.
Resumo:
National Highway Traffic Safety Administration, Washington, D.C.
Resumo:
National Highway Traffic Safety Administration, Washington, D.C.
Resumo:
Mode of access: Internet.
Resumo:
Mode of access: Internet.