Philip Schmiege
University of Texas Southwestern Medical Center
13 Papers
9 Citations
Philip Schmiege is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Chemistry & Transient receptor potential channel. The author has an hindex of 7, co-authored 11 publications. Previous affiliations of Philip Schmiege include Rockefeller University & Boston University.
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Papers
Structures of human Patched and its complex with native palmitoylated sonic hedgehog.
TL;DR: High-resolution structures of the human plasma membrane protein patched 1 alone and in complex with the native form of the ligand sonic hedgehog are determined and atomic insights are provided into the recognition of the N-terminal domain of HH (HH-N) by PTCH1, which offers a structural basis for cooperative binding of HH-N to various receptors and serves as a molecular framework for HH signalling and its malfunction in disease.
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Human TRPML1 channel structures in open and closed conformations
TL;DR: The regulatory mechanism of TRPML channels is revealed, the structure of the agonist-binding site is reported, and insights are provided into the molecular basis of mucolipidosis type IV pathogenesis.
Two patched molecules engage distinct sites on hedgehog yielding a signaling-competent complex
TL;DR: A cryo–electron microscopy structure of a key complex involved in regulating a pathway important in development and cancer is elucidated and demonstrates that one SHH-N molecule concomitantly engages both epitopes and binds two PTCH1 receptors (PTCH1-A and PTCH 1-B) in an asymmetric manner.
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Structural basis for PtdInsP2-mediated human TRPML1 regulation.
TL;DR: The structures and electrophysiological characterizations reveal an allosteric site and provide molecular insight into how lipids regulate TRP channels.
Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1
TL;DR: It is proposed that THO surveys common landmarks in each nuclear mRNP to localize Sub2 for targeted loading of Yra1, and finds that the 25 nm long THO clamps Sub2 in a half-open configuration; in contrast, when bound to the ATP analogue, RNA and Yra 1-C, Sub2 assumes a closed conformation.