What does it mean to be natively unfolded?

By Vladimir N Uversky. European Journal of Biochemistry, 2002

919 citations recorded by the source corpus.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6704776615f6c355134da5c2f2ff187d5f0bbd5d

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Materials Chemistry

In Molecular Biology

Citations in the corpus

Plasma membrane phosphoinositide organization by protein electrostatics (2005, background): “Although many researchers — particularly structural biologists — often tacitly assume that function requires structure, more than 100 ‘natively unfolded’ or ‘intrinsically unstructured’ proteins have been identified; their evolutionary persistence strongly implies that they have an important functio”
Assessing protein disorder and induced folding (2005, background): “temperature-induced formation of secondary structure.(3,16,42) This was observed for such natively disordered proteins as -synuclein,(86) phosphodiesterase -subunit,(87) 636–771 fragment of caldesmon,(20) extracellular domain of the nerve growth factor receptor,(88) and -casein.”
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling (2005, background): “Uversky VN. 2002a. Natively unfolded proteins: a point where biology waits for physics.”
Identification, Analysis and Prediction of Protein Ubiquitination Sites (2010, background): “Interestingly, disordered proteins/regions are also characterized by similar properties, such as a high absolute value of the net charge and low hydrophobicity.83 Anotherinteresting feature is the absence of additional lysines at positions that are immediately adjacent to the Ub site.”
p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept (2016, background): “Although they are without stable 3D structures, IDPs/IDPRs play a number of crucial functional roles in living organisms, especially in vital biological processes, such as control, signaling, recognition, and regulation [2,3,7,20,21,25,26].”
Length-dependent prediction of protein intrinsic disorder (2006, background): “D) structures under physiological conditions; they instead exist as ensembles of non-cooperatively inter-changing conformations in which the atom coordinates and backbone Ramachandran angles vary significantly over time with no specific equilibrium values [1-5].”
A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, background): “into two major structural classes, proteins with compact and extended disorder.(1,4,12,13,73) Based on these observations, the protein functionality was ascribed to at least three major protein conformational states, ordered, molten globular, and coil-like,(13,79) indicating that functional IDPs can”
Optimizing Long Intrinsic Disorder Predictors with Protein Evolutionary Information (2005, background): “(5) we can see that pia is the averaged log-odds of amino acid a in the neighborhood of sequence position i.”
Intrinsic disorder in cell-signaling and cancer-associated proteins. (2002, neutral): “( 3 ) The eukaryotic fraction of SWISS-PROT (EU_SW); a non-redundant dataset of 53,630 protein sequences was extracted from SWISS-PROT by query “eukaryota” in the organism field.”
Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, methodology): “Thus, there is no single gold standard for order/disorder assignment; instead, we need to use several experimental methods in concert [5,12,13,14,15,16,17].”