Natively unfolded proteins.

By A. Fink. Current Opinion in Structural Biology, 2005

698 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/32ff6759e1c78be931c348097c27537abdd646b0

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In Materials Chemistry

In Molecular Biology

Citations in the corpus

Assessment of disorder predictions in CASP6 (2005, background): “A number of recent reviews have surveyed both experimental and computational approaches to the study of these proteins.(1,2) They are found to participate in many biological processes and commonly occur in cell signaling pathways, DNA transcription and replication, protein translation, and endocytos”
Natively unstructured regions in proteins identified from contact predictions (2007, background): “The better our experimental and computational means of identifying such proteins, the more we realize that they come in a great variety: some adopt regular secondary structure (helix or strand) upon binding, some remain loopy; some proteins are almost entirely unstructured, others have only short un”
Natively Unstructured Loops Differ from Other Loops (2007, background): “Several detailed studies have specifically identified unstructured regions in hub proteins that are involved in signaling [3,5,6,60–62].”
Protein Metamorphosis: The Two-State Behavior of Mad2 (2008, background): “The so-called natively unfolded proteins only adopt defined tertiary folds upon binding to their targets (Dyson and Wright, 2005; Fink, 2005).”
Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell (2019, background): “44 Introduction 45 Over the last two decades, the concept of ‘intrinsic disorder’ has emerged as a prominent and 46 influential topic in protein science [1-6].”
A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, result): “This hypothesis has been confirmed by several comprehensive studies, 1, [11] [12] [13] [14] [71] [72] [73] 78, [130] [131] [132] [133] [134] which revealed that these structure-less members of the protein kingdom are abundantly involved in numerous biological processes, where they are frequently fou”
Sequence-similar, structure-dissimilar protein pairs in the PDB (2007, background): “36–38 However, we believe that the frequency of this phenomenon in the PDB comes as a surprise.”
Protein structure homology modeling using SWISS-MODEL workspace (2008, background): “Intrinsically unstructured regions in proteins have been associated with numerous important biological cellular functions, from cell signalling to transcriptional regulatio”
Missense meanderings in sequence space: a biophysical view of protein evolution (2005, background): “In systems such as cell signalling, where removing a signal is as important as its activation, many proteins are actually NATIVELY UNFOLDED to ensure their rapid degradatio”
The interplay between structure and function in intrinsically unstructured proteins (2005, background): “…of the most interesting recent developments with respect to the evidence of the unfolded character of IUPs in vivo, their distinct and unique functional modes, the functional implications of their residual structure and the functional benefits structural disorder, as opposed to order, provides.”
LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana (2008, background): “It has been estimated that as many as 30% of all proteins are either completely or partially disordered [92].”