FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W3171867852> ?p ?o ?g. }

• W3171867852 abstract "There is an increasing prevalence of neurodegenerative diseases such as Parkinson's Disease (PD). According to the Parkinson's Foundation, more than 10 million people live with PD around the world with 60,000 Americans being diagnosed each year (Parkinson's Foundation; Marras et al., 2018). Alpha-synuclein (α-syn) is a membrane binding protein whose function is not completely understood but has been identified with an increased risk of developing PD. Intrinsically disordered in solution, membrane-bound α-syn has distinct pathological and physiological states. Pathologically, it has been observed to aggregate, leading to the formation of Lewy bodies, plaque build-up, and eventually the development of PD (Spinelli et al., 2014) Physiologically, α-syn is believed to be involved in the transport of neurotransmitters (Ramakrishnan et al., 2012). To better understand the pathological state of α-syn, a deeper understanding of the physiological structure was needed. Previous studies had found two different conformations of α-syn: a horseshoe and an extended helix (Ulmer et al., 2005; Trexler and Rhoades, 2009). In this proposal, distance measurements will be performed to distinguish between the two conformations using an electron paramagnetic resonance spectroscopy experiment known as double electron-electron resonance (DEER). DEER measures the dipolar interaction between two unpaired electrons in a system. To accomplish this, α-syn was mutated in order to introduce unpaired electrons. Site-directed mutagenesis and site-directed spin labeling were employed to prepare double spin-labeled mutants of α-syn for DEER experiments. The ultimate goal of this proposal is to model and generate double mutants of α-syn to perform distance measurements on using DEER. With carefully designed placement of the spin labeled sites, the distance constraints should be able to be used to predict if the horseshoe or extended conformation is being sampled as α-syn binds to lipid vesicles of different sizes. Marras, C.; Beck, J.C.; Bower, J.H.; Roberts, E.; Ritz, B.; Ross, G.W.; Abbott, R.D.; Savica, R.; Van Den Eeden, S.K.; Willis, A.W.; Tanner, C.M. Prevalence of Parkinson's Disease across North America. npj Parkinson's Disease 2018, 4(21). Parkinson's Foundation. “Statistics.” Parkinson's Foundation. Ramakrishnan, N.A.; Drescher, M.J.; Drescher, D.G. The SNARE Complex in Neuronal and Sensory Cells. Mol Cell Neurosci. 2012, 50(1), 58-69. Trexler, A.J. and Elizabeth Rhoades. &[alpha]-Synuclein Binds Large Unilamellar Vesicles as an Extended Helix. Biochemistry 2009, 48, 2304-2306. Ulmer, T.S.; Bax, A.; Cole, N.B.; Nussbaum, R.L. Structure and Dynamics of Micelle-Bound Human Alpha-Synuclein. J Biol Chem 2005, 280(10), 9595-9603. Spinelli, K.J.; Taylor, J.K.; Osterberg, V.R.; Churchill, M.J.; Pollock, E.; Moore, C.; Meshul, C.K.; Unni, V.K. Presynaptic Alpha-Synuclein Aggregation in a Mouse Model of Parkinson's Disease. Journal of Neuroscience 2014, 34(6), 2037-2050." @default.
• W3171867852 created "2021-06-22" @default.
• W3171867852 creator A5007633243 @default.
• W3171867852 creator A5057810632 @default.
• W3171867852 date "2021-05-01" @default.
• W3171867852 modified "2023-09-23" @default.
• W3171867852 title "Distinguishing Different Conformations of Membrane‐Bound Alpha‐Synuclein through Distance Measurements" @default.
• W3171867852 doi "https://doi.org/10.1096/fasebj.2021.35.s1.02890" @default.
• W3171867852 hasPublicationYear "2021" @default.
• W3171867852 type Work @default.
• W3171867852 sameAs 3171867852 @default.
• W3171867852 citedByCount "0" @default.
• W3171867852 crossrefType "journal-article" @default.
• W3171867852 hasAuthorship W3171867852A5007633243 @default.
• W3171867852 hasAuthorship W3171867852A5057810632 @default.
• W3171867852 hasBestOaLocation W31718678521 @default.
• W3171867852 hasConcept C104317684 @default.
• W3171867852 hasConcept C121332964 @default.
• W3171867852 hasConcept C143065580 @default.
• W3171867852 hasConcept C177462420 @default.
• W3171867852 hasConcept C185592680 @default.
• W3171867852 hasConcept C186927785 @default.
• W3171867852 hasConcept C187961010 @default.
• W3171867852 hasConcept C46141821 @default.
• W3171867852 hasConcept C55493867 @default.
• W3171867852 hasConcept C8010536 @default.
• W3171867852 hasConceptScore W3171867852C104317684 @default.
• W3171867852 hasConceptScore W3171867852C121332964 @default.
• W3171867852 hasConceptScore W3171867852C143065580 @default.
• W3171867852 hasConceptScore W3171867852C177462420 @default.
• W3171867852 hasConceptScore W3171867852C185592680 @default.
• W3171867852 hasConceptScore W3171867852C186927785 @default.
• W3171867852 hasConceptScore W3171867852C187961010 @default.
• W3171867852 hasConceptScore W3171867852C46141821 @default.
• W3171867852 hasConceptScore W3171867852C55493867 @default.
• W3171867852 hasConceptScore W3171867852C8010536 @default.
• W3171867852 hasIssue "S1" @default.
• W3171867852 hasLocation W31718678521 @default.
• W3171867852 hasOpenAccess W3171867852 @default.
• W3171867852 hasPrimaryLocation W31718678521 @default.
• W3171867852 hasRelatedWork W1978023710 @default.
• W3171867852 hasRelatedWork W1980471129 @default.
• W3171867852 hasRelatedWork W2021457525 @default.
• W3171867852 hasRelatedWork W2053945339 @default.
• W3171867852 hasRelatedWork W2066203003 @default.
• W3171867852 hasRelatedWork W2269523337 @default.
• W3171867852 hasRelatedWork W2401548005 @default.
• W3171867852 hasRelatedWork W2504256629 @default.
• W3171867852 hasRelatedWork W2886038472 @default.
• W3171867852 hasRelatedWork W2952789362 @default.
• W3171867852 hasVolume "35" @default.
• W3171867852 isParatext "false" @default.
• W3171867852 isRetracted "false" @default.
• W3171867852 magId "3171867852" @default.
• W3171867852 workType "article" @default.