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Natively unfolded C‐terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin

https://doi.org/10.1002/prot.10481
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What this work says

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

inferredcites →https://doi.org/10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7openalex-snapshot
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
inferredcites →https://doi.org/10.1002/pro.5560041120openalex-snapshot
How to measure and predict the molar absorption coefficient of a protein
inferredcites →https://doi.org/10.1006/jmbi.1999.2952openalex-snapshot
A new set of peptide-based group heat capacities for use in protein stability calculations
inferredcites →https://doi.org/10.1006/jmbi.1999.3110openalex-snapshot
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
inferredcites →https://doi.org/10.1007/978-3-642-16483-5_778openalex-snapshot
Calcium-Binding Proteins
inferredcites →https://doi.org/10.1007/978-94-017-9780-1_101037openalex-snapshot
Small-Angle X-Ray Scattering
inferredcites →https://doi.org/10.1007/bf00124246openalex-snapshot
Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle
inferredcites →https://doi.org/10.1016/0005-2795(77)90050-2openalex-snapshot
Luminescence of phenylalanine residues in superoxide dismutase from green pea
inferredcites →https://doi.org/10.1016/0014-5793(90)80827-6openalex-snapshot
Interaction of smooth muscle caldesmon with phospholipids
inferredcites →https://doi.org/10.1016/0014-5793(95)00868-aopenalex-snapshot
Interaction of smooth muscle calponin with phospholipids
inferredcites →https://doi.org/10.1016/0076-6879(86)31033-4openalex-snapshot
[2]Scanning microcalorimetry in studying temperature-induced changes in proteins
inferredcites →https://doi.org/10.1016/0167-4838(91)90571-gopenalex-snapshot
Acid denatured apo-cytochrome c is a random coil: Evidence from small-angle X-ray scattering and dynamic light scattering
inferredcites →https://doi.org/10.1016/0301-4622(91)87007-ropenalex-snapshot
Spectrofluorimetric studies on C-terminal 34 kDa fragment of caldesmon
inferredcites →https://doi.org/10.1016/b978-0-12-078160-7.x5000-8openalex-snapshot
Biochemistry of Smooth Muscle Contraction
inferredcites →https://doi.org/10.1016/b978-0-12-374984-0.01698-3openalex-snapshot
Intrinsically Disordered Proteins
inferredcites →https://doi.org/10.1016/b978-012078160-7/50011-1openalex-snapshot
Calcium Binding Proteins
inferredcites →https://doi.org/10.1016/s0014-5793(98)00014-3openalex-snapshot
Interaction of isoforms of S100 protein with smooth muscle caldesmon
inferredcites →https://doi.org/10.1016/s0021-9258(18)98864-2openalex-snapshot
Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
inferredcites →https://doi.org/10.1016/s0022-2836(05)80197-4openalex-snapshot
Heat capacity of proteins
inferredcites →https://doi.org/10.1016/s0065-3233(08)60245-4openalex-snapshot
Analytical Gel Chromatography of Proteins
inferredcites →https://doi.org/10.1016/s0065-3233(08)60460-xopenalex-snapshot
Stability of Proteins Small Globular Proteins
inferredcites →https://doi.org/10.1016/s0301-4622(99)00104-0openalex-snapshot
Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10–90°C
inferredcites →https://doi.org/10.1016/s0955-0674(05)80010-9openalex-snapshot
Caldesmon
inferredcites →https://doi.org/10.1016/s0968-0004(00)88949-5openalex-snapshot
Calmodulin-binding domains: just two faced or multi-faceted?
inferredcites →https://doi.org/10.1016/s0968-0004(02)02169-2openalex-snapshot
Intrinsically unstructured proteins
inferredcites →https://doi.org/10.1016/s0968-0004(06)80021-6openalex-snapshot
Calcium binding and conformational response in EF-hand proteins
inferredcites →https://doi.org/10.1016/s1093-3263(00)00138-8openalex-snapshot
Intrinsically disordered protein
inferredcites →https://doi.org/10.1021/bi00176a006openalex-snapshot
"Partly Folded" State, a New Equilibrium State of Protein Molecules: Four-State Guanidinium Chloride-Induced Unfolding of .beta.-Lactamase at Low Temperature
inferredcites →https://doi.org/10.1021/bi00211a042openalex-snapshot
Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
inferredcites →https://doi.org/10.1021/bi00303a047openalex-snapshot
Use of high-speed size-exclusion chromatography for the study of protein folding and stability
inferredcites →https://doi.org/10.1021/bi00417a006openalex-snapshot
Binding of amphiphilic peptides to a carboxy-terminal tryptic fragment of calmodulin
inferredcites →https://doi.org/10.1021/bi012159+openalex-snapshot
Intrinsic Disorder and Protein Function
inferredcites →https://doi.org/10.1021/bi962008kopenalex-snapshot
Tryptophan Residues in Caldesmon Are Major Determinants for Calmodulin Binding
inferredcites →https://doi.org/10.1021/bi962969zopenalex-snapshot
The Inhibitory Complex of Smooth Muscle Caldesmon with Actin and Tropomyosin Involves Three Interacting Segments of the C-Terminal Domain 4
inferredcites →https://doi.org/10.1021/bi963075hopenalex-snapshot
Calmodulin Binds to Caldesmon in an Antiparallel Manner
inferredcites →https://doi.org/10.1021/cr990071kopenalex-snapshot
Changes in Biomolecular Conformation Seen by Small Angle X-ray Scattering
inferredcites →https://doi.org/10.1023/a:1012480829618openalex-snapshot
Some Properties of Caldesmon and Calponin and the Participation of These Proteins in Regulation of Smooth Muscle Contraction and Cytoskeleton Formation
inferredcites →https://doi.org/10.1042/bj2470663openalex-snapshot
Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells
inferredcites →https://doi.org/10.1042/bj2790001openalex-snapshot
The molecular anatomy of caldesmon
inferredcites →https://doi.org/10.1042/bj2840911openalex-snapshot
Caldesmon-phospholipid interaction. Effect of protein kinase C phosphorylation and sequence similarity with other phospholipid-binding proteins
inferredcites →https://doi.org/10.1042/bj2910403openalex-snapshot
Interaction of caldesmon with phospholipids
inferredcites →https://doi.org/10.1042/bj3160413openalex-snapshot
Multiple-sited interaction of caldesmon with Ca2+-calmodulin
inferredcites →https://doi.org/10.1042/bj3240255openalex-snapshot
Mapping of contact sites in the caldesmon–calmodulin complex
inferredcites →https://doi.org/10.1046/j.0014-2956.2001.02649.xopenalex-snapshot
What does it mean to be natively unfolded?
inferredcites →https://doi.org/10.1063/1.1143201openalex-snapshot
Small-angle x-ray scattering/diffraction system for studies of biological and other materials at the Stanford Synchrotron Radiation Laboratory (abstract)a)
inferredcites →https://doi.org/10.1063/1.1143332openalex-snapshot
Small-angle x-ray scattering/diffraction system for studies of biological and other materials at the Stanford Synchrotron Radiation Laboratorya)
inferredcites →https://doi.org/10.1074/jbc.m010907200openalex-snapshot
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
inferredcites →https://doi.org/10.1088/0031-9112/34/7/032openalex-snapshot
Small Angle X-ray Scattering
inferredcites →https://doi.org/10.1110/ps.4210102openalex-snapshot
Natively unfolded proteins: A point where biology waits for physics
inferredcites →https://doi.org/10.1111/j.1751-1097.1996.tb02464.xopenalex-snapshot
Log‐Normal Description of Fluorescence Spectra of Organic Fluorophores
inferredcites →https://doi.org/10.1137/0111030openalex-snapshot
An Algorithm for Least-Squares Estimation of Nonlinear Parameters
inferredcites →https://doi.org/10.1146/annurev.bi.49.070180.004421openalex-snapshot
Regulation and Kinetics of the Actin-Myosin-ATP Interaction

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Spectroscopic studies reveal conformational flexibility of intrinsically unstructured protein HYPK
inferred← citeshttps://doi.org/10.5936/csbj.201304006openalex-snapshot
BIOCHEMICAL AND BIOPHYSICAL CHARACTERIZATION OF RECOMBINANT YEAST PROTEASOME MATURATION FACTOR UMP1
inferred← citeshttps://doi.org/10.70675/c2bbe4a1z18a8z4b91z91c1zbc07621578e0openalex-snapshot
Contribution de la spectrométrie de masse à l'étude des interactions entre les protéines salivaires riche en proline et les tanins.
inferred← citeshttps://doi.org/10.7287/peerj.1265v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.1265v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.1265v0.2/reviews/1openalex-snapshot
Peer Review #1 of "Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism (v0.2)"
inferred← citeshttps://doi.org/10.7717/peerj.1265openalex-snapshot
Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism
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