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UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding

Biochimica et Biophysica Acta (BBA) - General Subjects(2022)10.1016/j.bbagen.2022.130284Source: DataRank Database

UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding is a research paper published in Biochimica et Biophysica Acta (BBA) - General Subjects (2022). On theSindex it has a DataRank of 0. It has been cited 4 times.

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Enrichment:Funding (8 grants)OA: greenTopics (25)IDs (PubMed, PMC)Annotations (1)

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Authors (3)

Micaela Tatman ORCID,Mervyn J. Monteiro ORCID,Trong H. Phung ORCID

Live enrichment

PubMed:36423739 PMC:PMC9792439

National Institute of Neurological Disorders and Stroke

Grant: R01NS100008

National Institute of Neurological Disorders and Stroke

Grant: RF1NS098243

NINDS NIH HHS

Grant: R01 NS098243

National Institutes of Health

Grant: 5R01NS100008-02

Deciphering the role of ER stress in ALS pathogenesis caused by UBQLN2 mutations

National Institutes of Health

Grant: 2RF1NS098243-06

Mechanistic studies and therapeutics for ALS/FTD linked to UBQLN2 mutations

National Institutes of Health

National Institute on Aging

Robert Packard Center for ALS Research, Johns Hopkins University

greenLicense: Elsevier TDM

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/9792439

publisherhttps://api.elsevier.com/content/article/PII:S0304416522002021?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0304416522002021?httpAccept=text/plain

https://doi.org/10.1016/j.bbagen.2022.130284

https://pubmed.ncbi.nlm.nih.gov/36423739

Fields of Study

0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

HumansAmyotrophic Lateral SclerosisTryptophanAdaptor Proteins, Signal TransducingTemperatureMutationHSP70 Heat-Shock ProteinsFrontotemporal DementiaAutophagy-Related Proteins

Keywords

Amyotrophic Lateral SclerosisUbqln2Ubiquitin ChainsHspa1bIntrinsic Tryptophan FluorescenceFrontotemporal DementiaMutationTemperatureTryptophanHumansAutophagy-Related ProteinsHSP70 Heat-Shock ProteinsAdaptor Proteins, Signal Transducing

UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding

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Authors (3)

Funding (8 grants)

Open Access

Topics

Annotations (Europe PMC)