376 research outputs found

    Does relevancy matter?

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    Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/138329/1/bmb21052.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/138329/2/bmb21052_am.pd

    Neurodegeneration - Good riddance to bad rubbish

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    Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/62887/1/441819a.pd

    Teaching the telephone book

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    Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/147825/1/bmb21193_am.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/147825/2/bmb21193.pd

    The yeast F1-ATPase beta subunit precursor contains functionally redundant mitochondrial protein import information

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    The NH2 terminus of the yeast F1-ATPase beta subunit precursor directs the import of this protein into mitochondria. To define the functionally important components of this import signal, oligonucleotide-directed mutagenesis was used to introduce a series of deletion and missense mutations into the gene encoding the F1-beta subunit precursor. Among these mutations were three nonoverlapping deletions, two within the 19-amino-acid presequence (delta 5-12 and delta 16-19) and one within the mature protein (delta 28-34). Characterization of the mitochondrial import properties of various mutant F1-beta subunit proteins containing different combinations of these deletions showed that import was blocked only when all three deletions were combined. Mutant proteins containing all possible single and pairwise combinations of these deletions were found to retain the ability to direct mitochondrial import of the F1-beta subunit. These data suggest that the F1-beta subunit contains redundant import information at its NH2 terminus. In fact, we found that deletion of the entire F1-beta subunit presequence did not prevent import, indicating that a functional mitochondrial import signal is present near the NH2 terminus of the mature protein. Furthermore, by analyzing mitochondrial import of the various mutant proteins in [rho-] yeast, we obtained evidence that different segments of the F1-beta subunit import signal may act in an additive or cooperative manner to optimize the import properties of this protein

    Wait, can you remind me just why we need another journal focused on autophagy?

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    Well, because you ask that question, we are going to attempt to explain exactly why we do indeed need another journal focused on autophagy. If you are reading this far, you presumably know what “autophagy” means, so we do not have to impress upon you the importance of this topic, and how autophagic dysfunction is associated with numerous diseases in humans (okay, we felt compelled to slip that in anyway). Nor do we think that you need to be introduced to the journal Autophagy, which is just starting its eighteenth year and publishes papers on pretty much any topic; at least any topic that is connected to autophagy, which, after all, means pretty much any topic, if you get our drift. So, if Autophagy has done so well and serves such an important purpose, why do we need another journal? To find the answer, read on

    Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae

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    AbstractThe disaccharide trehalose plays a critical role in yeast cell survival during conditions of environmental stress. The vacuole of the yeast Saccharomyces cerevisiae contains an enzyme, acid trehalose (ATH), that is capable of degrading trehalose. Recently, a gene required for ATH activity, ATH1, was cloned and sequenced [Destruelle et al., (1995) Yeast 11, 1015–1025]. The relationship between ATH1 and ATH, however, was not determined. We have purified ATH and shown that it is the ATH1 gene product; peptide sequences from the purified protein correspond to the deduced amino acid sequence of Ath1p. In addition, antiserum to Ath1p specifically recognizes purified ATH

    The Cytoplasm-to-Vacuole Targeting Pathway: A Historical Perspective

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    From today's perspective, it is obvious that macroautophagy (hereafter autophagy) is an important pathway that is connected to a range of developmental and physiological processes. This viewpoint, however, is relatively recent, coinciding with the molecular identification of autophagy-related (Atg) components that function as the protein machinery that drives the dynamic membrane events of autophagy. It may be difficult, especially for scientists new to this area of research, to appreciate that the field of autophagy long existed as a “backwater” topic that attracted little interest or attention. Paralleling the development of the autophagy field was the identification and analysis of the cytoplasm-to-vacuole targeting (Cvt) pathway, the only characterized biosynthetic route that utilizes the Atg proteins. Here, we relate some of the initial history, including some never-before-revealed facts, of the analysis of the Cvt pathway and the convergence of those studies with autophagy

    Autophagy: research topic, painting, poem, dance…

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    Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/111807/1/embr201540400.pd

    Autophagy Works Out

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    Autophagy is generally considered to be a cytoprotective response to stress, whether in the form of nutrient deprivation or the presence of dysfunctional organelles. He et al. now show in Nature that exercise-induced autophagy is needed for some of the beneficial effects of exercise on metabolism (He et al., 2012)
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