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Natively unfolded proteins: A point where biology waits for physics
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Why are ?natively unfolded? proteins unstructured under physiologic conditions?
inferredcites →https://doi.org/10.1002/1097-0134(20010101)42:1<38::aid-prot50>3.0.co;2-3openalex-snapshot
Sequence complexity of disordered protein
inferredcites →https://doi.org/10.1002/1097-0282(200102)58:2<138::aid-bip30>3.0.co;2-wopenalex-snapshot
Solution structure of native proteins with irregular folds from Raman optical activity
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The Role of Mobility in the Substrate Binding and Catalytic Machinery of Enzymes
inferredcites →https://doi.org/10.1002/bip.360310111openalex-snapshot
Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe
inferredcites →https://doi.org/10.1002/cber.18940270364openalex-snapshot
Einfluss der Configuration auf die Wirkung der Enzyme
inferredcites →https://doi.org/10.1002/pro.5560010808openalex-snapshot
Spectroscopic and chemical studies of the interaction between nerve growth factor (NGF) and the extracellular domain of the low affinity NGF receptor
inferredcites →https://doi.org/10.1002/pro.5560030505openalex-snapshot
Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
inferredcites →https://doi.org/10.1002/pro.5560050210openalex-snapshot
Yeast heat shock transcription factor N‐terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy
inferredcites →https://doi.org/10.1002/pro.5560060219openalex-snapshot
Structural characterization of the molten globule of α‐lactalbumin by solution X‐ray scattering
inferredcites →https://doi.org/10.1002/prot.1061openalex-snapshot
Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin
inferredcites →https://doi.org/10.1002/prot.1089openalex-snapshot
Denatured collapsed states in protein folding: Example of apomyoglobin
inferredcites →https://doi.org/10.1002/prot.340040204openalex-snapshot
Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences
inferredcites →https://doi.org/10.1006/abbi.1993.1130openalex-snapshot
Sequential Proton NMR Resonance Assignments, Circular Dichroism, and Structural Properties of a 50-Residue Substrate-Binding Peptide from DNA Polymerase I
inferredcites →https://doi.org/10.1006/bbrc.1999.1803openalex-snapshot
Structural and Functional Analysis of the N-Terminal Extracellular Region of β-Dystroglycan
inferredcites →https://doi.org/10.1006/bbrc.1999.2013openalex-snapshot
Zn2+-Mediated Structure Formation and Compaction of the “Natively Unfolded” Human Prothymosin α
inferredcites →https://doi.org/10.1006/bbrc.2000.4146openalex-snapshot
Flexible Structures of SIBLING Proteins, Bone Sialoprotein, and Osteopontin
inferredcites →https://doi.org/10.1006/jmbi.1993.1064openalex-snapshot
Molten Globule of Cytochrome c Studied by Small Angle X-ray Scattering
inferredcites →https://doi.org/10.1006/jmbi.1994.1173openalex-snapshot
Structural Characterization of the FK506 Binding Protein Unfolded in Urea and Guanidine Hydrochloride
inferredcites →https://doi.org/10.1006/jmbi.1996.0018openalex-snapshot
Further Evidence on the Equilibrium “Pre-molten Globule State”: Four-state Guanidinium Chloride-induced Unfolding of Carbonic Anhydrase B at Low Temperature
inferredcites →https://doi.org/10.1006/jmbi.1996.0535openalex-snapshot
Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray Scattering
inferredcites →https://doi.org/10.1006/jmbi.1997.0953openalex-snapshot
Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
inferredcites →https://doi.org/10.1006/jmbi.1997.0954openalex-snapshot
Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. paramagnetic relaxation enhancement by nitroxide spin labels
inferredcites →https://doi.org/10.1006/jmbi.1997.1369openalex-snapshot
NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein
inferredcites →https://doi.org/10.1006/jmbi.1997.1485openalex-snapshot
Equilibrium and kinetic binding analysis of the N-terminal domain of the Pf1 gene 5 protein and its interaction with single-stranded DNA
inferredcites →https://doi.org/10.1006/jmbi.1998.1741openalex-snapshot
Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates
inferredcites →https://doi.org/10.1006/jmbi.1998.2355openalex-snapshot
The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro , but not for chromatin remodelling 1 1Edited by M. Yaniv
inferredcites →https://doi.org/10.1006/jmbi.1999.2711openalex-snapshot
Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding
inferredcites →https://doi.org/10.1006/jmbi.1999.2740openalex-snapshot
Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1 1Edited by A. R. Fersht
inferredcites →https://doi.org/10.1006/jmbi.1999.3110openalex-snapshot
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
inferredcites →https://doi.org/10.1006/jmbi.2000.3545openalex-snapshot
Conformation of the RNA polymerase II C-terminal domain: circular dichroism of long and short fragments
inferredcites →https://doi.org/10.1007/978-1-4757-2508-7openalex-snapshot
Circular Dichroism and the Conformational Analysis of Biomolecules
inferredcites →https://doi.org/10.1007/978-94-017-9780-1_101037openalex-snapshot
Small-Angle X-Ray Scattering
inferredcites →https://doi.org/10.1007/bf00398413openalex-snapshot
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
inferredcites →https://doi.org/10.1007/s002490050218openalex-snapshot
Conformation of bovine myelin basic protein purified with bound lipids
inferredcites →https://doi.org/10.1016/0014-5793(94)80231-9openalex-snapshot
The molten globule is a third thermodynamical state of protein molecules
inferredcites →https://doi.org/10.1016/0022-2836(78)90246-2openalex-snapshot
The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding
inferredcites →https://doi.org/10.1016/0022-2836(90)90200-6openalex-snapshot
High-resolution three-dimensional structure of horse heart cytochrome c
inferredcites →https://doi.org/10.1016/0097-8485(93)85006-xopenalex-snapshot
Statistics of local complexity in amino acid sequences and sequence databases
inferredcites →https://doi.org/10.1016/0097-8485(94)85023-2openalex-snapshot
Non-globular domains in protein sequences: Automated segmentation using complexity measures
inferredcites →https://doi.org/10.1016/0168-9452(96)04332-4openalex-snapshot
The embryo-specific EMB-1 protein of Daucus carota is flexible and unstructured in solution
inferredcites →https://doi.org/10.1016/0301-4622(96)00009-9openalex-snapshot
Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state
inferredcites →https://doi.org/10.1016/0968-0004(79)90298-6openalex-snapshot
Conformational flexibility and its functional significance in some protein molecules
inferredcites →https://doi.org/10.1016/0968-0004(93)90111-yopenalex-snapshot
Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association
inferredcites →https://doi.org/10.1016/b978-0-12-374984-0.01698-3openalex-snapshot
Intrinsically Disordered Proteins
inferredcites →https://doi.org/10.1016/b978-0-444-89372-7.50017-8openalex-snapshot
Molecular Aspects of Proteolysis of Globular Proteins
inferredcites →https://doi.org/10.1016/s0006-3495(93)81124-xopenalex-snapshot
Evidence of an associative intermediate on the myoglobin refolding pathway
inferredcites →https://doi.org/10.1016/s0014-5793(97)00238-xopenalex-snapshot
Nucleotide and calcium‐induced conformational changes in histone H1
inferredcites →https://doi.org/10.1016/s0014-5793(97)01091-0openalex-snapshot
Formation of a yeast SNARE complex is accompanied by significant structural changes
inferredcites →https://doi.org/10.1016/s0014-5793(99)01260-0openalex-snapshot
Heme binding and polymerization by Plasmodium falciparum histidine rich protein II: influence of pH on activity and conformation
inferredcites →https://doi.org/10.1016/s0021-9258(17)30555-0openalex-snapshot
Zinc-induced secondary structure transitions in human sperm protamines
inferredcites →https://doi.org/10.1016/s0021-9258(18)45957-1openalex-snapshot
Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1.
inferredcites →https://doi.org/10.1016/s0021-9258(18)47294-8openalex-snapshot
Structural and functional analysis of the NF-kappa B p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation.
inferredcites →https://doi.org/10.1016/s0021-9258(18)48255-5openalex-snapshot
Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sulfhydryl cross-linking. A mechanism for caldesmon's F-actin bundling activity.
inferredcites →https://doi.org/10.1016/s0021-9258(18)77318-3openalex-snapshot
Ca2(+)-induced conformational change and aggregation of chromogranin A.
inferredcites →https://doi.org/10.1016/s0021-9258(18)99105-2openalex-snapshot
Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase
inferredcites →https://doi.org/10.1016/s0021-9258(19)51080-8openalex-snapshot
Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.
inferredcites →https://doi.org/10.1016/s0021-9258(19)69635-3openalex-snapshot
A specific substrate from rabbit cerebellum for guanosine 3‘:5‘-monophosphate-dependent protein kinase. I. Purification and characterization.
inferredcites →https://doi.org/10.1016/s0021-9258(19)74487-1openalex-snapshot
Structural and functional characterization of the HPV16 E7 protein expressed in bacteria.
inferredcites →https://doi.org/10.1016/s0021-9258(19)74513-xopenalex-snapshot
Ca(2+)-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin. The involvement of the trifluoperazine-binding site.
inferredcites →https://doi.org/10.1016/s0021-9258(19)83582-2openalex-snapshot
Conformation-specific antibodies as probes of the gamma-carboxyglutamic acid-rich region of bovine prothrombin. Studies of metal-induced structural changes.
inferredcites →https://doi.org/10.1016/s0021-9258(20)81811-0openalex-snapshot
The Conformation of Horse Heart Apocytochrome c
inferredcites →https://doi.org/10.1016/s0021-9258(20)82133-4openalex-snapshot
Size and shape of rabbit skeletal muscle calsequestrin.
inferredcites →https://doi.org/10.1016/s0065-3233(08)60460-xopenalex-snapshot
Stability of Proteins Small Globular Proteins
inferredcites →https://doi.org/10.1016/s0065-3233(08)60546-xopenalex-snapshot
Molten Globule and Protein Folding
inferredcites →https://doi.org/10.1016/s0076-6879(73)27030-1openalex-snapshot
[27] Circular dichroism and optical rotatory dispersion of proteins and polypeptides
inferredcites →https://doi.org/10.1016/s0076-6879(96)66035-2openalex-snapshot
[33] Analysis of compositionally biased regions in sequence databases
inferredcites →https://doi.org/10.1016/s0092-8674(00)81037-5openalex-snapshot
Identification of a Protein That Interacts with Tubulin Dimers and Increases the Catastrophe Rate of Microtubules
inferredcites →https://doi.org/10.1016/s0092-8674(00)81599-8openalex-snapshot
Solution Structure of a TBP–TAFII230 Complex
inferredcites →https://doi.org/10.1016/s0167-4838(96)00190-2openalex-snapshot
The application of circular dichroism to studies of protein folding and unfolding
inferredcites →https://doi.org/10.1016/s0167-4838(97)00092-7openalex-snapshot
A circular dichroism study of preferential hydration and alcohol effects on a denatured protein, pig calpastatin domain I
inferredcites →https://doi.org/10.1016/s0167-4838(97)00175-1openalex-snapshot
The structural aspects of limited proteolysis of native proteins
inferredcites →https://doi.org/10.1016/s0167-4838(99)00209-5openalex-snapshot
Conformational studies of the C-terminal domain of bacteriophage Pf1 gene 5 protein
inferredcites →https://doi.org/10.1016/s0196-9781(98)00132-6openalex-snapshot
The conformation of peptide thymosin α1 in solution and in a membrane-like environment by circular dichroism and NMR spectroscopy. a possible model for its interaction with the lymphocyte membrane
inferredcites →https://doi.org/10.1016/s0925-4439(00)00094-6openalex-snapshot
The effect of Pb2+ on the structure and hydroxyapatite binding properties of osteocalcin
inferredcites →https://doi.org/10.1016/s1074-5521(99)80075-1openalex-snapshot
The amyloidogenicity of gelsolin is controlled by proteolysisand pH
inferredcites →https://doi.org/10.1016/s1093-3263(00)00125-xopenalex-snapshot
Evolution of functionality in lattice proteins
inferredcites →https://doi.org/10.1016/s1093-3263(00)00136-4openalex-snapshot
NMR spin relaxation methods for characterization of disorder and folding in proteins
inferredcites →https://doi.org/10.1016/s1093-3263(00)00138-8openalex-snapshot
Intrinsically disordered protein
inferredcites →https://doi.org/10.1016/s1097-2765(00)80027-1openalex-snapshot
Independent Ligand-Induced Folding of the RNA-Binding Domain and Two Functionally Distinct Antitermination Regions in the Phage λ N Protein
inferredcites →https://doi.org/10.1016/s1359-0278(96)00020-xopenalex-snapshot
All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins
inferredcites →https://doi.org/10.1021/bi00040a037openalex-snapshot
Prothymosin .alpha.: A Biologically Active Protein with Random Coil Conformation
inferredcites →https://doi.org/10.1021/bi00072a025openalex-snapshot
Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange study
inferredcites →https://doi.org/10.1021/bi00089a050openalex-snapshot
A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c
inferredcites →https://doi.org/10.1021/bi00093a012openalex-snapshot
Metal ion binding to dog osteocalcin studied by proton NMR spectroscopy
inferredcites →https://doi.org/10.1021/bi00171a004openalex-snapshot
Structure and Dynamics of a Denatured 131-Residue Fragment of Staphylococcal Nuclease: A Heteronuclear NMR Study
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/bi0019545openalex-snapshot
Probing the Three-Dimensional Structure of Human Calreticulin
inferredcites →https://doi.org/10.1021/bi001975zopenalex-snapshot
A Comparative Study of Peptide Models of the α-Domain of α-Lactalbumin, Lysozyme, and α-Lactalbumin/Lysozyme Chimeras Allows the Elucidation of Critical Factors That Contribute to the Ability to Form Stable Partially Folded States
inferredcites →https://doi.org/10.1021/bi002078yopenalex-snapshot
Linked Folding and Anion Binding of the Bacillus subtilis Ribonuclease P Protein
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/bi0024005openalex-snapshot
Solution Structure of the p53 Regulatory Domain of the p19Arf Tumor Suppressor Protein
inferredcites →https://doi.org/10.1021/bi0026472openalex-snapshot
Stability and Global Fold of the Mouse Prohormone Convertase 1 Pro-Domain
inferredcites →https://doi.org/10.1021/bi00315a030openalex-snapshot
Immunochemical studies of conformational alterations in bone .gamma.-carboxyglutamic acid containing protein
inferredcites →https://doi.org/10.1021/bi00396a015openalex-snapshot
Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues
inferredcites →https://doi.org/10.1021/bi00427a002openalex-snapshot
Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin
inferredcites →https://doi.org/10.1021/bi00429a003openalex-snapshot
Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions
inferredcites →https://doi.org/10.1021/bi00476a026openalex-snapshot
On the nature of the structural change of the colicin E1 channel peptide necessary for its translocation-competent state
inferredcites →https://doi.org/10.1021/bi00498a001openalex-snapshot
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
inferredcites →https://doi.org/10.1021/bi00504a006openalex-snapshot
Estimation of globular protein secondary structure from circular dichroism
inferredcites →https://doi.org/10.1021/bi961799nopenalex-snapshot
NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded
inferredcites →https://doi.org/10.1021/bi970561bopenalex-snapshot
Zinc Binding Properties of the DNA Binding Domain of the 1,25-Dihydroxyvitamin D3 Receptor
inferredcites →https://doi.org/10.1021/bi971952topenalex-snapshot
The C-Terminal Half of the Anti-Sigma Factor FlgM Contains a Dynamic Equilibrium Solution Structure Favoring Helical Conformations
inferredcites →https://doi.org/10.1021/bi972494ropenalex-snapshot
4E Binding Proteins Inhibit the Translation Factor eIF4E without Folded Structure
inferredcites →https://doi.org/10.1021/bi9811157openalex-snapshot
Ligand Binding Is the Principal Determinant of Stability for the p21H-ras Protein
inferredcites →https://doi.org/10.1021/bi990752+openalex-snapshot
Natively Unfolded Human Prothymosin α Adopts Partially Folded Collapsed Conformation at Acidic pH
inferredcites →https://doi.org/10.1021/bi991105lopenalex-snapshot
Characterization of the Structure and Function of W → F WW Domain Variants: Identification of a Natively Unfolded Protein That Folds upon Ligand Binding
inferredcites →https://doi.org/10.1021/bi991433lopenalex-snapshot
Metal and DNA Binding Properties of a Two-Domain Fragment of Neural Zinc Finger Factor 1, a CCHC-type Zinc Binding Protein
inferredcites →https://doi.org/10.1021/bi991599mopenalex-snapshot
Leucine 245 Is a Critical Residue for Folding and Function of the Manganese Stabilizing Protein of Photosystem II
inferredcites →https://doi.org/10.1021/bi9923555openalex-snapshot
Intrinsic Structural Disorder of the C-Terminal Activation Domain from the bZIP Transcription Factor Fos
inferredcites →https://doi.org/10.1021/bi992770xopenalex-snapshot
Statistical Conformation of Human Plasma Fibronectin
inferredcites →https://doi.org/10.1021/cr60108a003openalex-snapshot
The Chemistry of Protein Denaturation.
inferredcites →https://doi.org/10.1021/pr0155127openalex-snapshot
Effect of Zinc and Temperature on the Conformation of the γ Subunit of Retinal Phosphodiesterase: A Natively Unfolded Protein
inferredcites →https://doi.org/10.1023/a:1006678623815openalex-snapshot
Intelligent Data Analysis for Protein Disorder Prediction
inferredcites →https://doi.org/10.1023/a:1008382027065openalex-snapshot
NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
inferredcites →https://doi.org/10.1023/a:1021031227197openalex-snapshot
Spectroscopic Characterization of Two Soluble Transducers from the Archaeon Halobacterium salinarum
inferredcites →https://doi.org/10.1038/276362a0openalex-snapshot
Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits
inferredcites →https://doi.org/10.1038/313156a0openalex-snapshot
Three-dimensional structure of an antigen–antibody complex at 6 Å resolution
inferredcites →https://doi.org/10.1038/347575a0openalex-snapshot
Folding transition in the DMA-binding domain of GCN4 on specific binding to DNA
inferredcites →https://doi.org/10.1038/363038a0openalex-snapshot
Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
inferredcites →https://doi.org/10.1038/381335a0openalex-snapshot
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
inferredcites →https://doi.org/10.1038/5803openalex-snapshot
Folding intermediates of SNARE complex assembly.
inferredcites →https://doi.org/10.1038/nsb0298-148openalex-snapshot
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
inferredcites →https://doi.org/10.1042/0264-6021:3560151openalex-snapshot
Molten-globule structure and membrane binding of the N-terminal protease-resistant domain (63-193) of the steroidogenic acute regulatory protein (StAR)
inferredcites →https://doi.org/10.1042/bj3290395openalex-snapshot
Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains
inferredcites →https://doi.org/10.1042/bst0060017openalex-snapshot
The Purification and Characterization of Protein Phosphatase Inhibitor-1 from Rabbit Skeletal Muscle
inferredcites →https://doi.org/10.1042/bst0151009openalex-snapshot
Flexibility and rigidity, requirements for the function of proteins and protein pigment complexes
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/10.1046/j.1432-1327.2000.01738.xopenalex-snapshot
Domain structure of tropomodulin
inferredcites →https://doi.org/10.1063/1.4823390openalex-snapshot
Statistical Physics of Macromolecules
inferredcites →https://doi.org/10.1073/pnas.111145098openalex-snapshot
Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45
inferredcites →https://doi.org/10.1073/pnas.22.7.439openalex-snapshot
On the Structure of Native, Denatured, and Coagulated Proteins
inferredcites →https://doi.org/10.1073/pnas.47.9.1309openalex-snapshot
THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN
inferredcites →https://doi.org/10.1073/pnas.54.1.253openalex-snapshot
Protein substrate conformation and proteolysis.
inferredcites →https://doi.org/10.1073/pnas.82.16.5255openalex-snapshot
Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.
inferredcites →https://doi.org/10.1073/pnas.93.21.11504openalex-snapshot
Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity.
inferredcites →https://doi.org/10.1073/pnas.93.24.13659openalex-snapshot
Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
inferredcites →https://doi.org/10.1073/pnas.94.25.13452openalex-snapshot
Structure of the recombinant full-length hamster prion protein PrP(29–231): The N terminus is highly flexible
inferredcites →https://doi.org/10.1073/pnas.96.13.7250openalex-snapshot
The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule
inferredcites →https://doi.org/10.1073/pnas.97.23.12391openalex-snapshot
Are denatured proteins ever random coils?
inferredcites →https://doi.org/10.1073/pnas.97.23.12565openalex-snapshot
The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
inferredcites →https://doi.org/10.1074/jbc.270.21.12578openalex-snapshot
pH- and Ca2+-induced Conformational Change and Aggregation of Chromogranin B.
inferredcites →https://doi.org/10.1074/jbc.270.34.19853openalex-snapshot
Reconstitution of Escherichia coli RNase HI from the N-fragment with High Helicity and the C-fragment with a Disordered Structure
inferredcites →https://doi.org/10.1074/jbc.271.13.7593openalex-snapshot
Biochemical and Biophysical Analyses of Recombinant Forms of Human Topoisomerase I
inferredcites →https://doi.org/10.1074/jbc.271.23.13716openalex-snapshot
Analysis of the Structural Properties of cAMP-responsive Element-binding Protein (CREB) and Phosphorylated CREB
inferredcites →https://doi.org/10.1074/jbc.271.3.1379openalex-snapshot
Conformational Changes in the Fibronectin Binding MSCRAMMs Are Induced by Ligand Binding
inferredcites →https://doi.org/10.1074/jbc.273.47.31145openalex-snapshot
The Binding of Calcium to the B-repeat Segment of SdrD, a Cell Surface Protein of Staphylococcus aureus
inferredcites →https://doi.org/10.1074/jbc.273.6.3718openalex-snapshot
Conformation-dependent Antibacterial Activity of the Naturally Occurring Human Peptide LL-37
inferredcites →https://doi.org/10.1074/jbc.273.9.4831openalex-snapshot
Forcing Thermodynamically Unfolded Proteins to Fold
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Trimethylamine N-Oxide-induced Cooperative Folding of an Intrinsically Unfolded Transcription-activating Fragment of Human Glucocorticoid Receptor
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Molecular Chaperone-like Properties of an Unfolded Protein, αs-Casein
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The Cap-binding Protein eIF4E Promotes Folding of a Functional Domain of Yeast Translation Initiation Factor eIF4G1
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Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
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Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein
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THE EFFECT OF DENATURATION ON THE VISCOSITY OF PROTEIN SYSTEMS
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Small Angle X-ray Scattering
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Crystal structure of ribosomal protein L4 shows RNA‐binding sites for ribosome incorporation and feedback control of the S10 operon
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Dimerization and DNA Binding Facilitate aaa-Helix Formation of Max in Solution
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Conformation of the Fowl Protamine, Galline, and Its Binding Properties to DNA
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Native and Non-Native Conformation-Specific Antibodies Directed to the Loop Region of Hen Egg-White Lysozyme
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Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa
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The Basic Subdomain of the c‐Jun Oncoprotein
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Crystal Structure of the Ribosome at 5.5 Å Resolution
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Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
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Structural Characterization of a Partly Folded Apomyoglobin Intermediate
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Crystal Structure of the Lactose Operon Repressor and Its Complexes with DNA and Inducer
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Coupling of Local Folding to Site-Specific Binding of Proteins to DNA
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Hydrodynamic and optical properties of the wheat germ Em protein
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Secondary Structure of Proteins Through Circular Dichroism Spectroscopy
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Flexible Docking and Design
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DENATURED STATES OF PROTEINS
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The Recombinant Dehydrin-Like Desiccation Stress Protein from the Resurrection PlantCraterostigma plantagineumDisplays No Defined Three-Dimensional Structure in Its Native State
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DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus
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DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. III. Immunocytochemical localization
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Diversity of equilibrium compact forms of denatured globular proteins
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Principles of polymer chemistry
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Physical chemistry of macromolecules
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inferred← citeshttps://doi.org/10.1002/pro.4968openalex-snapshot
Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure
inferred← citeshttps://doi.org/10.1002/pro.534openalex-snapshot
Cryoprotective mechanism of a small intrinsically disordered dehydrin protein
inferred← citeshttps://doi.org/10.1002/pro.547openalex-snapshot
Characterization of the disordered‐to‐α‐helical transition of IA3 by SDSL‐EPR spectroscopy
inferred← citeshttps://doi.org/10.1002/pro.59openalex-snapshot
Dematin exhibits a natively unfolded core domain and an independently folded headpiece domain
inferred← citeshttps://doi.org/10.1002/pro.603openalex-snapshot
Probing the self‐association, intermolecular contacts, and folding propensity of amelogenin
inferred← citeshttps://doi.org/10.1002/pro.70068openalex-snapshot
Unraveling the molecular grammar and the structural transitions underlying the fibrillation of a viral fibrillogenic domain
inferred← citeshttps://doi.org/10.1002/pro.739openalex-snapshot
Fractal dimension of an intrinsically disordered protein: Small‐angle X‐ray scattering and computational study of the bacteriophage λ N protein
inferred← citeshttps://doi.org/10.1002/prot.10471openalex-snapshot
The intracellular domain of the Drosophila cholinesterase‐like neural adhesion protein, gliotactin, is natively unfolded
inferred← citeshttps://doi.org/10.1002/prot.10481openalex-snapshot
Natively unfolded C‐terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin
inferred← citeshttps://doi.org/10.1002/prot.20279openalex-snapshot
Sequence patterns associated with disordered regions in proteins
inferred← citeshttps://doi.org/10.1002/prot.20351openalex-snapshot
Protein conformational transitions coupled to binding in molecular recognition of unstructured proteins: Deciphering the effect of intermolecular interactions on computational structure prediction of the p27Kip1 protein bound to the cyclin A–cyclin‐dependent kinase 2 complex
inferred← citeshttps://doi.org/10.1002/prot.20446openalex-snapshot
Addressing the intrinsic disorder bottleneck in structural proteomics
inferred← citeshttps://doi.org/10.1002/prot.20448openalex-snapshot
Does structural and chemical divergence play a role in precluding undesirable protein interactions?
inferred← citeshttps://doi.org/10.1002/prot.20587openalex-snapshot
Protein flexibility and rigidity predicted from sequence
inferred← citeshttps://doi.org/10.1002/prot.20750openalex-snapshot
Assessing protein disorder and induced folding
inferred← citeshttps://doi.org/10.1002/prot.20792openalex-snapshot
Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses
inferred← citeshttps://doi.org/10.1002/prot.20888openalex-snapshot
Intrinsic disorder is a key characteristic in partners that bind 14‐3‐3 proteins
inferred← citeshttps://doi.org/10.1002/prot.20989openalex-snapshot
Role of lysine versus arginine in enzyme cold‐adaptation: Modifying lysine to homo‐arginine stabilizes the cold‐adapted α‐amylase from Pseudoalteramonas haloplanktis
inferred← citeshttps://doi.org/10.1002/prot.21032openalex-snapshot
Phosphorylation‐induced transient intrinsic structure in the kinase‐inducible domain of CREB facilitates its recognition by the KIX domain of CBP
inferred← citeshttps://doi.org/10.1002/prot.21055openalex-snapshot
Insights into protein structure and function from disorder–complexity space
inferred← citeshttps://doi.org/10.1002/prot.21075openalex-snapshot
A practical overview of protein disorder prediction methods
inferred← citeshttps://doi.org/10.1002/prot.21089openalex-snapshot
Intrinsically unstructured N‐terminal domain of bZIP transcription factor HY5
inferred← citeshttps://doi.org/10.1002/prot.21328openalex-snapshot
Dynamic α‐helices: Conformations that do not conform
inferred← citeshttps://doi.org/10.1002/prot.21364openalex-snapshot
Identifying long‐range structure in the intrinsically unstructured transactivation domain of p53
inferred← citeshttps://doi.org/10.1002/prot.21385openalex-snapshot
The N‐ and C‐termini of the human Nogo molecules are intrinsically unstructured: Bioinformatics, CD, NMR characterization, and functional implications
inferred← citeshttps://doi.org/10.1002/prot.21497openalex-snapshot
Intrinsic disorder in yeast transcriptional regulatory network
inferred← citeshttps://doi.org/10.1002/prot.21593openalex-snapshot
Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data
inferred← citeshttps://doi.org/10.1002/prot.21621openalex-snapshot
Computational analysis of folding and mutation properties of C5 domain of myosin binding protein C
inferred← citeshttps://doi.org/10.1002/prot.21721openalex-snapshot
Modeling the accessible conformations of the intrinsically unstructured transactivation domain of p53
inferred← citeshttps://doi.org/10.1002/prot.21798openalex-snapshot
Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature
inferred← citeshttps://doi.org/10.1002/prot.21856openalex-snapshot
Huntingtin interacting protein HYPK is intrinsically unstructured
inferred← citeshttps://doi.org/10.1002/prot.21924openalex-snapshot
On defining the dynamics of hydrophobic patches on protein surfaces
inferred← citeshttps://doi.org/10.1002/prot.21974openalex-snapshot
Apo‐parvalbumin as an intrinsically disordered protein
inferred← citeshttps://doi.org/10.1002/prot.21978openalex-snapshot
Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants
inferred← citeshttps://doi.org/10.1002/prot.22063openalex-snapshot
Isoform‐specific variation in the intrinsic disorder of troponin I
inferred← citeshttps://doi.org/10.1002/prot.22117openalex-snapshot
A robust approach for analyzing a heterogeneous structural ensemble
inferred← citeshttps://doi.org/10.1002/prot.22125openalex-snapshot
Mapping α‐helical induced folding within the intrinsically disordered C‐terminal domain of the measles virus nucleoprotein by site‐directed spin‐labeling EPR spectroscopy
inferred← citeshttps://doi.org/10.1002/prot.22135openalex-snapshot
Human FEZ1 has characteristics of a natively unfolded protein and dimerizes in solution
inferred← citeshttps://doi.org/10.1002/prot.22205openalex-snapshot
Zn2+‐linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation
inferred← citeshttps://doi.org/10.1002/prot.22342openalex-snapshot
Isoform‐specific variation in the intrinsic disorder of the ecdysteroid receptor N‐terminal domain
inferred← citeshttps://doi.org/10.1002/prot.22385openalex-snapshot
Order propensity of an intrinsically disordered protein, the cyclin‐dependent‐kinase inhibitor Sic1
inferred← citeshttps://doi.org/10.1002/prot.22504openalex-snapshot
Modularity of intrinsic disorder in the human proteome
inferred← citeshttps://doi.org/10.1002/prot.22661openalex-snapshot
UV and X‐ray structural studies of a 101‐residue long Tat protein from a HIV‐1 primary isolate and of its mutated, detoxified, vaccine candidate
inferred← citeshttps://doi.org/10.1002/prot.22820openalex-snapshot
Smoothing molecular interactions: The “kinetic buffer” effect of intrinsically disordered proteins
inferred← citeshttps://doi.org/10.1002/prot.22887openalex-snapshot
Intrinsic disorder of Drosophila melanogaster hormone receptor 38 N‐terminal domain
inferred← citeshttps://doi.org/10.1002/prot.23077openalex-snapshot
Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides
inferred← citeshttps://doi.org/10.1002/prot.23193openalex-snapshot
Molecular dynamics simulation of conformational heterogeneity in transportin 1
inferred← citeshttps://doi.org/10.1002/prot.24128openalex-snapshot
Kinesin tail domains are intrinsically disordered
inferred← citeshttps://doi.org/10.1002/prot.24464openalex-snapshot
A molten globule intermediate of the Von Willebrand factor A1 domain firmly tethers platelets under shear flow
inferred← citeshttps://doi.org/10.1002/prot.24822openalex-snapshot
Intrinsic disorder of human Y in Y ang 1 protein
inferred← citeshttps://doi.org/10.1002/prot.25255openalex-snapshot
Thermodynamic and structural effect of urea and guanidine chloride on the helical and on a hairpin fragment of GB1 from molecular simulations
inferred← citeshttps://doi.org/10.1002/prot.25307openalex-snapshot
Soft interactions and volume exclusion by polymeric crowders can stabilize or destabilize transient structure in disordered proteins depending on polymer concentration
inferred← citeshttps://doi.org/10.1002/prot.25527openalex-snapshot
A method for partitioning the information contained in a protein sequence between its structure and function
inferred← citeshttps://doi.org/10.1002/prot.25646openalex-snapshot
The influence of intrinsic folding mechanism of an unfolded protein on the coupled folding‐binding process during target recognition
inferred← citeshttps://doi.org/10.1002/prot.25656openalex-snapshot
Ramachandran maps for side chains in globular proteins
inferred← citeshttps://doi.org/10.1002/prot.26261openalex-snapshot
Conservation and coevolution determine evolvability of different classes of disordered residues in human intrinsically disordered proteins
inferred← citeshttps://doi.org/10.1002/psc.1344openalex-snapshot
Probing structural transitions in both structured and disordered proteins using site‐directed spin‐labeling EPR spectroscopy
inferred← citeshttps://doi.org/10.1002/psc.3362openalex-snapshot
Self‐assembling systems comprising intrinsically disordered protein polymers like elastin‐like recombinamers
inferred← citeshttps://doi.org/10.1002/rcm.2192openalex-snapshot
Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: a possible regulatory role within a PRK/GAPDH/CP12 complex
inferred← citeshttps://doi.org/10.1002/smll.200800585openalex-snapshot
Nanopore Analysis of the Folding of Zinc Fingers
inferred← citeshttps://doi.org/10.1002/wcms.1685openalex-snapshot
Rational drug design targeting intrinsically disordered proteins
inferred← citeshttps://doi.org/10.1002/wnan.1160openalex-snapshot
Ordered and disordered proteins as nanomaterial building blocks
inferred← citeshttps://doi.org/10.1002/yea.1608openalex-snapshot
Structure–function analysis of Knr4/Smi1, a newly member of intrinsically disordered proteins family, indispensable in the absence of a functional PKC1–SLT2 pathway in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1007/0-306-48662-8_12openalex-snapshot
A Microscopic Study of Disorder-Order Transitions in Molecular Recognition of Unstructured Proteins: Hierarchy of Structural Loss and the Transition State Determination from Monte Carlo Simulations of P27KIP1 Protein Coupled Unfolding and Unbinding
inferred← citeshttps://doi.org/10.1007/0-387-25919-8_1openalex-snapshot
Structural and Conformational Prerequisites of Amyloidogenesis
inferred← citeshttps://doi.org/10.1007/0-387-25919-8_3openalex-snapshot
Relative Importance of Hydrophobicity, Net Charge, and Secondary Structure Propensities in Protein Aggregation
inferred← citeshttps://doi.org/10.1007/978-0-387-36534-3_4openalex-snapshot
α-Synuclein Aggregation and Parkinson’s Disease
inferred← citeshttps://doi.org/10.1007/978-0-387-85766-4_21openalex-snapshot
Tropomodulin/Tropomyosin Interactions Regulate Actin Pointed End Dynamics
inferred← citeshttps://doi.org/10.1007/978-1-0716-1546-1_6openalex-snapshot
Contact-Based Analysis of Aggregation of Intrinsically Disordered Proteins
inferred← citeshttps://doi.org/10.1007/978-1-0716-2095-3_4openalex-snapshot
Predicting Protein Conformational Disorder and Disordered Binding Sites
inferred← citeshttps://doi.org/10.1007/978-1-0716-4828-5_3openalex-snapshot
Predictive Model for Single-Site Mutations That Change Intrinsically Disordered Protein Binding Energetics
inferred← citeshttps://doi.org/10.1007/978-1-4020-9058-5_5openalex-snapshot
Bioinformatics Approaches to the Structure and Function of Intrinsically Disordered Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4020-9434-7openalex-snapshot
Protein Folding and Misfolding: Neurodegenerative Diseases
inferred← citeshttps://doi.org/10.1007/978-1-4020-9434-7_1openalex-snapshot
Structural Disorder and Its Connection with Misfolding Diseases
inferred← citeshttps://doi.org/10.1007/978-1-4020-9434-7_10openalex-snapshot
TPPP/p25: A New Unstructured Protein Hallmarking Synucleinopathies
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