Patrick G. Needham
University of Pittsburgh
21 Papers
68 Citations
Patrick G. Needham is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Endoplasmic reticulum & Endoplasmic-reticulum-associated protein degradation. The author has an hindex of 14, co-authored 21 publications. Previous affiliations of Patrick G. Needham include University of Toledo & Ohio University.
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Papers
RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43.
Jacob R. Mann,Amanda M. Gleixner,Jocelyn C. Mauna,Edward Gomes,Michael R. DeChellis-Marks,Patrick G. Needham,Katie E. Copley,Bryan Hurtle,Bede Portz,Noah J. Pyles,Lin Guo,Christopher B. Calder,Zachary P. Wills,Udai Bhan Pandey,Julia Kofler,Jeffrey L. Brodsky,Amantha Thathiah,James Shorter,Christopher J. Donnelly +18 more
TL;DR: The formation of pathologically relevant inclusions is driven by aberrant interactions between low-complexity domains of TDP-43 that are antagonized by RNA binding, and it is shown that aberrant phase transitions of cytoplasmic TTP are neurotoxic and that treatment with oligonucleotides composed of T DP-43 target sequences prevent inclusions and rescue neurotoxicity.
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A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation
Yixian Cui,Smriti Parashar,Muhammad Zahoor,Patrick G. Needham,Muriel Mari,Ming Zhu,Shuliang Chen,Hsuan-Chung Ho,Fulvio Reggiori,Hesso Farhan,Jeffrey L. Brodsky,Susan Ferro-Novick +11 more
TL;DR: In budding yeast, it is discovered that the Sec24 paralog Lst1, which forms a COPII cargo adaptor complex with Sec23, is essential for ER-phagy, a disposal pathway that targets ER domains and sequesters them into autophagosomes for delivery to the vacuole or lysosome for degradation.
Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases.
TL;DR: The factors that constitute the ERAD machinery are discussed and detail how each step in the pathway occurs, and the underlying pathophysiology of protein conformational diseases associated with ERAD is highlighted.
Adeno-associated virus interactions with B23/Nucleophosmin: identification of sub-nucleolar virion regions.
Joyce M. Bevington,Patrick G. Needham,Kristin C. Verrill,Roy F. Collaco,Venkatesh Basrur,James P. Trempe +5 more
TL;DR: Using Rep68 column chromatography and mass spectrometry, the nucleolar, B23/Nucleophosmin (NPM) protein is identified as an Rep-interacting partner and suggests that NPM plays a role in AAV amplification affecting Rep function and virion assembly.
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The Thiazide-sensitive NaCl Cotransporter Is Targeted for Chaperone-dependent Endoplasmic Reticulum-associated Degradation
Patrick G. Needham,Kasia Mikoluk,Pradeep Dhakarwal,Shaheen Khadem,Shaheen Khadem,Avin C. Snyder,Arohan R. Subramanya,Jeffrey L. Brodsky +7 more
TL;DR: This work confirmed that NCC was a bona fide ERAD substrate in yeast, as the majority of NCC polypeptide was integrated into ER membranes, and its turnover rate was sensitive to proteasome inhibition.
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