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A fuzzy encounter complex precedes formation of the fully-engaged TIR1-Aux/IAA auxin co-receptor system

https://doi.org/10.1101/781922

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0282(19980415)45:5<381::aid-bip6>3.0.co;2-hopenalex-snapshot

Local control of peptide conformation: Stabilization ofcis proline peptide bonds by aromatic proline interactions

inferredcites →https://doi.org/10.1002/bip.1978.360170908openalex-snapshot

Carbon‐13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐ X‐ L ‐ Ala‐OH

inferredcites →https://doi.org/10.1006/jmbi.1998.1770openalex-snapshot

Side-chain effects on peptidyl-prolyl cis/trans isomerisation

inferredcites →https://doi.org/10.1007/978-1-61779-927-3_11openalex-snapshot

Using Chemical Shifts to Assess Transient Secondary Structure and Generate Ensemble Structures of Intrinsically Disordered Proteins

inferredcites →https://doi.org/10.1007/s10858-009-9395-yopenalex-snapshot

Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts

inferredcites →https://doi.org/10.1007/s10858-019-00258-0openalex-snapshot

Tuning a timing device that regulates lateral root development in rice

inferredcites →https://doi.org/10.1016/j.cell.2013.12.027openalex-snapshot

Structural Basis for DNA Binding Specificity by the Auxin-Dependent ARF Transcription Factors

inferredcites →https://doi.org/10.1016/j.febslet.2007.08.039openalex-snapshot

Enhanced stability of cis Pro‐Pro peptide bond in Pro‐Pro‐Phe sequence motif

inferredcites →https://doi.org/10.1016/j.pbi.2007.08.014openalex-snapshot

Auxin response factors

inferredcites →https://doi.org/10.1016/j.pbi.2014.06.006openalex-snapshot

Diversity and specificity: auxin perception and signaling through the TIR1/AFB pathway

inferredcites →https://doi.org/10.1016/j.sbi.2018.09.007openalex-snapshot

Elucidating binding mechanisms and dynamics of intrinsically disordered protein complexes using NMR spectroscopy

inferredcites →https://doi.org/10.1016/j.sbi.2018.09.008openalex-snapshot

Fold or not to fold upon binding — does it really matter?

inferredcites →https://doi.org/10.1016/j.tibs.2007.10.003openalex-snapshot

Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions

inferredcites →https://doi.org/10.1038/35104500openalex-snapshot

Auxin regulates SCFTIR1-dependent degradation of AUX/IAA proteins

inferredcites →https://doi.org/10.1038/nature03542openalex-snapshot

The Arabidopsis F-box protein TIR1 is an auxin receptor

inferredcites →https://doi.org/10.1038/nature03543openalex-snapshot

The F-box protein TIR1 is an auxin receptor

inferredcites →https://doi.org/10.1038/nature05731openalex-snapshot

Mechanism of auxin perception by the TIR1 ubiquitin ligase

inferredcites →https://doi.org/10.1038/nature12294openalex-snapshot

Modulation of allostery by protein intrinsic disorder

inferredcites →https://doi.org/10.1038/nchembio.2007.35openalex-snapshot

Prolyl cis-trans isomerization as a molecular timer

inferredcites →https://doi.org/10.1038/nchembio.2555openalex-snapshot

Chemical hijacking of auxin signaling with an engineered auxin–TIR1 pair

inferredcites →https://doi.org/10.1038/nchembio.926openalex-snapshot

A combinatorial TIR1/AFB–Aux/IAA co-receptor system for differential sensing of auxin

inferredcites →https://doi.org/10.1038/ncomms15706openalex-snapshot

Variation in auxin sensing guides AUX/IAA transcriptional repressor ubiquitylation and destruction

inferredcites →https://doi.org/10.1038/ncomms8395openalex-snapshot

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

inferredcites →https://doi.org/10.1038/nrd748openalex-snapshot

Nmr in drug discovery

inferredcites →https://doi.org/10.1038/nrm3920openalex-snapshot

Intrinsically disordered proteins in cellular signalling and regulation

inferredcites →https://doi.org/10.1038/s41586-018-0699-5openalex-snapshot

The entropic force generated by intrinsically disordered segments tunes protein function

inferredcites →https://doi.org/10.1046/j.1365-313x.1996.10030403.xopenalex-snapshot

Mutations in the AXR3 gene of Arabidopsis result in altered auxin response including ectopic expression from the SAUR‐AC1 promoter

inferredcites →https://doi.org/10.1073/pnas.1419525112openalex-snapshot

Structural basis for the auxin-induced transcriptional regulation by Aux/IAA17

inferredcites →https://doi.org/10.1073/pnas.1424077112openalex-snapshot

Solution structure of the PsIAA4 oligomerization domain reveals interaction modes for transcription factors in early auxin response

inferredcites →https://doi.org/10.1073/pnas.1703054114openalex-snapshot

Structure of the Arabidopsis TOPLESS corepressor provides insight into the evolution of transcriptional repression

inferredcites →https://doi.org/10.1073/pnas.1817038116openalex-snapshot

Quantification of reaction cycle parameters for an essential molecular switch in an auxin-responsive transcription circuit in rice

inferredcites →https://doi.org/10.1093/pcp/pcs035openalex-snapshot

The Interaction and Integration of Auxin Signaling Components

inferredcites →https://doi.org/10.1098/rsob.160139openalex-snapshot

Tomographic docking suggests the mechanism of auxin receptor TIR1 selectivity

inferredcites →https://doi.org/10.1104/pp.15.00587openalex-snapshot

Rate Motifs Tune Auxin/Indole-3-Acetic Acid Degradation Dynamics

inferredcites →https://doi.org/10.1105/tpc.010244openalex-snapshot

Rapid Degradation of Auxin/Indoleacetic Acid Proteins Requires Conserved Amino Acids of Domain II and Is Proteasome Dependent

inferredcites →https://doi.org/10.1105/tpc.13.10.2349openalex-snapshot

Rapid Degradation of Auxin/Indoleacetic Acid Proteins Requires Conserved Amino Acids of Domain II and Is Proteasome Dependent

inferredcites →https://doi.org/10.1111/pce.12662openalex-snapshot

Auxin response factors

inferredcites →https://doi.org/10.1126/sciadv.1500107openalex-snapshot

Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors

inferredcites →https://doi.org/10.1126/science.1151461openalex-snapshot

TOPLESS Mediates Auxin-Dependent Transcriptional Repression During Arabidopsis Embryogenesis

inferredcites →https://doi.org/10.1126/science.279.5355.1371openalex-snapshot

Changes in Auxin Response from Mutations in an AUX/IAA Gene

inferredcites →https://doi.org/10.1146/annurev-arplant-043015-112122openalex-snapshot

Transcriptional Responses to the Auxin Hormone

inferredcites →https://doi.org/10.3389/fphy.2019.00010openalex-snapshot

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.tibs.2022.06.004openalex-snapshot

Intrinsic and extrinsic regulators of Aux/IAA protein degradation dynamics

inferred← citeshttps://doi.org/10.1021/acssynbio.4c00186openalex-snapshot

Genetically Encoded, Noise-Tolerant, Auxin Biosensors in Yeast

inferred← citeshttps://doi.org/10.1039/d2cb00207hopenalex-snapshot

Protein–protein interfaces in molecular glue-induced ternary complexes: classification, characterization, and prediction

inferred← citeshttps://doi.org/10.1101/2023.03.21.533585openalex-snapshot

Genetically encoded, noise-tolerant, auxin biosensors in yeast facilitate metabolic engineering and directed evolution

inferred← citeshttps://doi.org/10.1101/cshperspect.a039891openalex-snapshot

No Time for Transcription—Rapid Auxin Responses in Plants

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