Pathogenic mutations in UBQLN2 exhibit diverse aggregation propensity and neurotoxicity

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: Pathogenic mutations in UBQLN2 exhibit diverse aggregation propensity and neurotoxicity ; volume:14 ; number:1 ; day:13 ; month:3 ; year:2024 ; pages:1-18 ; date:12.2024
Scientific reports ; 14, Heft 1 (13.3.2024), 1-18, 12.2024

Creator: Safren, Nathaniel
Dao, Thuy P.
Mohan, Harihar Milaganur
Huang, Camellia
Trotter, Bryce
Castañeda, Carlos A.
Paulson, Henry
Barmada, Sami
Sharkey, Lisa M.

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-024-55582-9

URN: urn:nbn:de:101:1-2405152107365.299583237754

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:53 AM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

Safren, Nathaniel
Dao, Thuy P.
Mohan, Harihar Milaganur
Huang, Camellia
Trotter, Bryce
Castañeda, Carlos A.
Paulson, Henry
Barmada, Sami
Sharkey, Lisa M.
SpringerLink (Online service)

Other Objects (12)

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Adults with septic shock and extreme hyperferritinemia exhibit pathogenic immune variation

Spreading of Tau Protein Does Not Depend on Aggregation Propensity

Selective neurotoxicity

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Tripartite Biosensors to Assess Protein Stability and Aggregation Propensity in Yeast

Prion protein insertional mutations increase aggregation propensity but not fiber stability

AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

Hochschulschrift

In silico and experimental approaches to determining the aggregation propensity of biopharmaceutical products

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Prostate cancer lesions in transition zone exhibit a higher propensity for pathological upgrading in radical prostatectomy

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Adults with septic shock and extreme hyperferritinemia exhibit pathogenic immune variation

Spreading of Tau Protein Does Not Depend on Aggregation Propensity

Selective neurotoxicity

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Tripartite Biosensors to Assess Protein Stability and Aggregation Propensity in Yeast

Prion protein insertional mutations increase aggregation propensity but not fiber stability

AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

Hochschulschrift

In silico and experimental approaches to determining the aggregation propensity of biopharmaceutical products

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Prostate cancer lesions in transition zone exhibit a higher propensity for pathological upgrading in radical prostatectomy

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Adults with septic shock and extreme hyperferritinemia exhibit pathogenic immune variation

Spreading of Tau Protein Does Not Depend on Aggregation Propensity

Selective neurotoxicity

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Tripartite Biosensors to Assess Protein Stability and Aggregation Propensity in Yeast

Prion protein insertional mutations increase aggregation propensity but not fiber stability

AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

Hochschulschrift

In silico and experimental approaches to determining the aggregation propensity of biopharmaceutical products

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Prostate cancer lesions in transition zone exhibit a higher propensity for pathological upgrading in radical prostatectomy

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

Pathogenic mutations in UBQLN2 exhibit diverse aggregation propensity and neurotoxicity

Object Details

References and Relationships

Contributors, Places and Time

Further information

Data provider

Associated

Other Objects (12)

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Adults with septic shock and extreme hyperferritinemia exhibit pathogenic immune variation

Spreading of Tau Protein Does Not Depend on Aggregation Propensity

Selective neurotoxicity

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Tripartite Biosensors to Assess Protein Stability and Aggregation Propensity in Yeast

Prion protein insertional mutations increase aggregation propensity but not fiber stability

AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

In silico and experimental approaches to determining the aggregation propensity of biopharmaceutical products

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Prostate cancer lesions in transition zone exhibit a higher propensity for pathological upgrading in radical prostatectomy

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Adults with septic shock and extreme hyperferritinemia exhibit pathogenic immune variation

Spreading of Tau Protein Does Not Depend on Aggregation Propensity

Selective neurotoxicity

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Tripartite Biosensors to Assess Protein Stability and Aggregation Propensity in Yeast

Prion protein insertional mutations increase aggregation propensity but not fiber stability

AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

In silico and experimental approaches to determining the aggregation propensity of biopharmaceutical products

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Prostate cancer lesions in transition zone exhibit a higher propensity for pathological upgrading in radical prostatectomy

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Adults with septic shock and extreme hyperferritinemia exhibit pathogenic immune variation

Spreading of Tau Protein Does Not Depend on Aggregation Propensity

Selective neurotoxicity

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Tripartite Biosensors to Assess Protein Stability and Aggregation Propensity in Yeast

Prion protein insertional mutations increase aggregation propensity but not fiber stability

AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

In silico and experimental approaches to determining the aggregation propensity of biopharmaceutical products

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Prostate cancer lesions in transition zone exhibit a higher propensity for pathological upgrading in radical prostatectomy

Related objects

Reset password