Results 11 to 20 of about 7,902,914 (332)

An intrinsically disordered protein region encoded by the human disease gene CLEC16A regulates mitophagy [PDF]

open access: yesAutophagy, 2022
CLEC16A regulates mitochondrial health through mitophagy and is associated with over 20 human diseases. However, the key structural and functional regions of CLEC16A, and their relevance for human disease, remain unknown.
Morgan A. Gingerich   +12 more
semanticscholar   +2 more sources

IDP–CRF: Intrinsically Disordered Protein/Region Identification Based on Conditional Random Fields [PDF]

open access: yesInt J Mol Sci, 2018
Accurate prediction of intrinsically disordered proteins/regions is one of the most important tasks in bioinformatics, and some computational predictors have been proposed to solve this problem. How to efficiently incorporate the sequence-order effect is
Yumeng Liu, Xiaolong Wang, Bin Liu
semanticscholar   +2 more sources

Design of intrinsically disordered region binding proteins

open access: yesScience
INTRODUCTION: Intrinsically disordered proteins and peptides play key roles in biology, but the lack of defined structures and high variability in sequence and conformational preferences has made targeting such systems challenging.
Ke-Jia Wu   +28 more
semanticscholar   +6 more sources

ProtBert-BFD token classification improves intrinsically disordered protein region prediction [PDF]

open access: yesBrief Bioinform
Background Intrinsically disordered regions (IDRs) lack stable tertiary structures yet are crucial to transcriptional regulation, signal transduction, and molecular recognition.
Le Quoc Khanh Nguyen
semanticscholar   +2 more sources

Adenosine triphosphate as a modulator of protein interactions and stability. [PDF]

open access: yesFEBS Open Bio
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Tan S, Curtis R.
europepmc   +2 more sources

Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.

open access: yesPLoS ONE, 2014
An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins.
Swagata Das   +6 more
doaj   +3 more sources

Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]

open access: yes, 2009
Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core   +6 more sources

The human disease gene CLEC16A encodes an intrinsically disordered protein region required for mitochondrial quality control

open access: yesbioRxiv, 2021
CLEC16A regulates mitochondrial health through mitophagy and is associated with over 20 human diseases. While CLEC16A has ubiquitin ligase activity, the key structural and functional regions of CLEC16A, and their relevance for human disease, remain ...
Morgan A. Gingerich   +12 more
semanticscholar   +1 more source

Intrinsically disordered regions in autophagy proteins [PDF]

open access: yesProteins: Structure, Function, and Bioinformatics, 2013
ABSTRACTAutophagy is an essential eukaryotic pathway required for cellular homeostasis. Numerous key autophagy effectors and regulators have been identified, but the mechanism by which they carry out their function in autophagy is not fully understood.
Yang, Mei   +5 more
openaire   +2 more sources

Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins [PDF]

open access: yesFrontiers in Plant Science, 2012
Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signaling proteins such as receptor-like kinases and may dynamically modulate their lateral segregation within plasma membranes.
Marín, Macarena, Ott, Thomas
openaire   +5 more sources

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