Publications

Empowering STEM students: A university-wide mentorship program fostering retention and belonging
Empowering STEM students: A university-wide mentorship program fostering retention and belonging
Ravishankar S, Spencer-Drakes TCJ, Fernandes IH, Hayes MI, Coopwood S, Spencer I, Neal SE. (2024) J Cell Physiol. 239(7):e31348
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Proteotoxic stress and the ubiquitin proteasome system
Proteotoxic stress and the ubiquitin proteasome system
Kandel R, Jung J, Neal S. (2023). Semin Cell Dev Biol. 23.
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Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress
Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress
Kandel R, Jung J, Syau D, Kuo T, Songster L, Horn C, Chapman C, Aguayo A, Duttke S, Benner C, Neal SE. (2023). PLoS Biol. 23;21(1)
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An ERAD-independent role for rhomboid pseudoprotease Dfm1 in mediating sphingolipid homeostasis
An ERAD-independent role for rhomboid pseudoprotease Dfm1 in mediating sphingolipid homeostasis
Bhaduri S, Aguayo A, Ohno Y, Proietto M, Jung J, Wang I, Kandel R, Singh N, Ibrahim I, Fulzele A, Neal SE. (2022). EMBO J. 2022 e112275.
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The Role of the Rhomboid Superfamily in ER Protein Quality Control : From Mechanisms and Functions to Diseases
The Role of the Rhomboid Superfamily in ER Protein Quality Control : From Mechanisms and Functions to Diseases
Bhaduri S, Scott NA, Neal SE. (2022). Cold Spring Harb Perspect Biol. In press.
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Quality Control: Maintaining molecular order and preventing cellular chaos
Quality Control: Maintaining molecular order and preventing cellular chaos
Neal SE, Ohtake F, Cuervo AM, Hegde RS, Jakob U, Lazarou M, Gilbert WV, Chen ZJ, Tooze SA, Haber JE, Walters KJ, Hartl FU. (2022). Mol. Cell 82, 1390–1397.
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Decoding Transcription Regulatory Mechanisms Associated with Coccidioides immitis Phase Transition Using Total RNA
Decoding Transcription Regulatory Mechanisms Associated with Coccidioides immitis Phase Transition Using Total RNA
Duttke SH, Beyhan S, Singh R, Neal SE, Viriyakosol S, Fierer J, Kirkland TN, Stajich JE, Benner C, Carlin AF. (2022). MSystems 7
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Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substrates
Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substrates
Nejatfard A, Wauer N, Bhaduri S, Conn A, Gourkanti S, Singh N, Kuo T, Kandel R, Amaro RE, Neal SE. (2021). Cell Rep. 37, 109840.
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Assays for studying normal versus suppressive ERAD-associated retrotranslocation pathways in yeast
Assays for studying normal versus suppressive ERAD-associated retrotranslocation pathways in yeast
Bhaduri S, Neal SE. (2021). STAR Protoc. 2, 100640.
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Inner-nuclear-membrane-associated degradation employs Dfm1-independent retrotranslocation and alleviates misfolded transmembrane-protein toxicity
Inner-nuclear-membrane-associated degradation employs Dfm1-independent retrotranslocation and alleviates misfolded transmembrane-protein toxicity
Flagg MP, Wangeline MA, Holland SR, Duttke SH, Benner C, Neal SE, Hampton RY. (2021). Mol. Biol. Cell 32, 521–537.
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Impaired phosphatidylethanolamine metabolism activates a reversible stress response that detects and resolves mutant mitochondrial precursors
Impaired phosphatidylethanolamine metabolism activates a reversible stress response that detects and resolves mutant mitochondrial precursors
Sam PN, Calzada E, Acoba MG, Zhao T, Watanabe Y, Nejatfard A, Trinidad JC, Shutt TE, Neal SE, Claypool SM. (2021). iScience 24, 102196.
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The role of rhomboid superfamily members in protein homeostasis: Mechanistic insight and physiological implications
The role of rhomboid superfamily members in protein homeostasis: Mechanistic insight and physiological implications
Kandel RR, Neal SE. (2020). Biochim. Biophys. Acta – Mol. Cell Res. 1867, 118793.
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HRD complex self-remodeling enables a novel route of membrane protein retrotranslocation
HRD complex self-remodeling enables a novel route of membrane protein retrotranslocation
Neal SE, Dysau D, Nejatfard A, Nadeau S, Hampton R. (2020). iScience 23, 101493
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Assays for protein retrotranslocation in ERAD
Assays for protein retrotranslocation in ERAD
Neal SE, Duttke SH, Hampton RY. (2019). Methods in Enzymology 619, 1–26.
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Membrane Protein Dislocation by the Rhomboid Pseudoprotease Dfm1: No Pore Needed?
Membrane Protein Dislocation by the Rhomboid Pseudoprotease Dfm1: No Pore Needed?
Avci D, Lemberg MK. Mol Cell. 2018 Jan 18;69(2):161-162
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A Cdc48 “retrochaperone” function is required for the solubility of retrotranslocated, integral membrane Endoplasmic Reticulum-associated Degradation (ERAD-M) substrates
A Cdc48 “retrochaperone” function is required for the solubility of retrotranslocated, integral membrane Endoplasmic Reticulum-associated Degradation (ERAD-M) substrates
Neal SE, Mak R, Bennett EJ, Hampton R. (2017). J. Biol. Chem. 292.
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Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space
Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space
Neal SE, Dabir DV, Wijaya J, Boon C, Koehler CM. (2017). Mol. Biol. Cell 28.
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Direct and essential function for Hrd3 in ER-associated degradation
Direct and essential function for Hrd3 in ER-associated degradation
Vashistha N, Neal SE, Singh A, Carroll SM, Hampton RY. (2016). Proc. Natl. Acad. Sci. U. S. A. 113.
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Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway
Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway
Neal SE, Dabir DV, Tienson HL, Horn DM, Glaeser K, Ogozalek Loo RR, Barrientos A, Koehler CM. (2015). J. Biol. Chem. 290, 20804–20814.
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Reconstitution of the Mia40-Erv1 oxidative folding pathway for the small tim proteins.
Reconstitution of the Mia40-Erv1 oxidative folding pathway for the small tim proteins.
Tienson HL, Dabir DV, Neal SE, Loo R, Hasson SA, Boontheung P, Kim S-K, Loo JA, Koehler CM. (2009). Mol. Biol. Cell 20.
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