14.462 is the second semester of the second-year Ph.D. macroeconomics sequence. The …
14.462 is the second semester of the second-year Ph.D. macroeconomics sequence. The course is intended to introduce the students, not only to particular areas of current research, but also to some very useful analytical tools. It covers a selection of topics that varies from year to year. Recent topics include:
Growth and Fluctuations Heterogeneity and Incomplete Markets Optimal Fiscal Policy Time Inconsistency Reputation Coordination Games and Macroeconomic Complementarities Information
This resource is a video abstract of a research paper created by …
This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:
"Alzheimer’s disease (AD) is the leading cause of dementia in the aged population. The key feature of AD is the deposition of two different kinds of protein aggregates in the brain, and at the point of aggregate formation, treatment becomes difficult. A recent study focused on how to prevent the aggregation of one protein: the microtubule-associated protein Tau, which forms neurofibrillary tangles. Following up on research indicating that polyphenolic compounds can serve as neuroprotective agents, researchers analyzed the ability of the polyphenol Baicalein to inhibit the aggregation of Tau. In vitro, Baicalein blocked Tau aggregation and paired helical filament dissolution via an oligomer capture and dissociation mechanism. It also dissolved preformed mature fibrils of Tau, creating Tau oligomers, with no effect on the viability of neuronal cells..."
The rest of the transcript, along with a link to the research itself, is available on the resource itself.
This resource is a video abstract of a research paper created by …
This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:
"Alzheimer’s disease (AD) is associated with the misfolding of two major proteins, causing the accumulation of toxic protein aggregates. Amyloid-β aggregates extracellularly, forming plaques, and Tau aggregates intracellularly, forming neurofibrillary tangles. Post-translational modifications (PTMs) are important for the regulation of Tau’s function, but an imbalance in PTMs may lead to abnormal Tau function and aggregation. While methylation is an important PTM for Tau in its physiological state, the lysine methylation signature changes in Tau’s pathological form. These alterations may affect the intramolecular forces within the Tau molecule, resulting in altered conformations, and methylation can also interact with other PTMs, affecting Tau function and stability. Although more investigation is needed, it appears that in addition to post-translational methylation, DNA methylation also affects Tau regulation..."
The rest of the transcript, along with a link to the research itself, is available on the resource itself.
Of all the animals in the oceans, the hammerhead shark may be …
Of all the animals in the oceans, the hammerhead shark may be one of the strangest looking. The exact purpose of the wide, flat head is a mystery, but several theories abound. In this video, we travel to the shark-infested waters of the Galapagos in Ecuador and to a research station in Hawaii to learn about the unusual habits of these sinister-looking sharks. Jonathan swims in schools of hundreds of hammerheads, and yet the sharks ignore him. What are the sharks up to? Please see the accompanying study guide for educational objectives and discussion points.
This course covers amino acid sequence control of protein folding, misfolding, amyloid …
This course covers amino acid sequence control of protein folding, misfolding, amyloid polymerization and aggregation. Readings and discussions address topics such as chaperone structure and function, folding and assembly of fibrous proteins, and pathologies associated with protein misfolding and aggregation in Alzheimer's, Parkinson's, Huntington's and other protein deposition diseases. Students are required to write and present a research paper.
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