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Eileen M. Lafer

Researcher at University of Texas Health Science Center at San Antonio

Publications -  119
Citations -  7667

Eileen M. Lafer is an academic researcher from University of Texas Health Science Center at San Antonio. The author has contributed to research in topics: Clathrin & Chemistry. The author has an hindex of 46, co-authored 105 publications receiving 6997 citations. Previous affiliations of Eileen M. Lafer include University of Pittsburgh & University of Texas System.

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Polyspecific monoclonal lupus autoantibodies reactive with both polynucleotides and phospholipids

TL;DR: The polyspecific reactivity of a single molecular species of lupusAutoantibody suggests that some of the diverse serological abnormalities of SLE may be a result of the binding of certain autoantibodies to a phosphodiester-containing epitope that is present in diverse biological molecules.
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Antibodies to left-handed Z-DNA bind to interband regions of Drosophila polytene chromosomes

TL;DR: This is the first identification of the Z-DNA conformation in material of biological origin and the staining is found in the interband regions and its intensity varies among different interbands in a reproducible manner.
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Structural Basis of Interdomain Communication in the Hsc70 Chaperone

TL;DR: This analysis identifies interdomain interactions critical for chaperone function and supports an allosteric mechanism in which the inter domain linker invades and disrupts the interdomain interface when ATP binds.
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Mitogen-Activated Protein Kinase Regulates Dopamine Transporter Surface Expression and Dopamine Transport Capacity

TL;DR: An involvement of the MAPK cascade in regulating DAT transport capacity in striatum is demonstrated and that inhibition of this cascade decreases DAT cell surface expression in HEK 293 cells is highlighted, highlighting the potential role of MAPK as a presynaptic mechanism that regulates DA signaling.
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Intrinsically disordered proteins drive membrane curvature

TL;DR: It is reported that intrinsically disordered domains of the endocytic adaptor proteins, Epsin1 and AP180 are highly potent drivers of membrane curvature, and a balance of steric pressure on the two surfaces of the membrane drives this exclusion.