Irena Roterman-Konieczna

Irena Roterman-Konieczna's AcademicInfluence.com Rankings

Biology

#15534

World Rank

#19538

Historical Rank

Biochemistry

#2767

World Rank

#2957

Historical Rank

biology Degrees

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Biology

Irena Roterman-Konieczna's Degrees

PhD Biochemistry University of Warsaw
Masters Biotechnology University of Warsaw

Why Is Irena Roterman-Konieczna Influential?

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According to Wikipedia, Irena Roterman-Konieczna is a Polish biochemist and a professor at the Jagiellonian University Medical College. Biography Irena Roterman-Konieczna was born on 13 March 1950 in Kraków. She received a master's degree in chemistry in 1973 at the Jagiellonian University, her doctorate in 1985 at the Medical College there, and a postdoctoral degree there in 1996. In 2005 she received the title of professor. She has been the head of the Department of Bioinformatics and Telemedicine at the Jagiellonian University, and an editor in chief of the Bio-Algorithms and Med-Systems journal.

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Irena Roterman-Konieczna's Published Works

Number of citations in a given year to any of this author's works

Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author

Published Works

A comparison of the CHARMM, AMBER and ECEPP potentials for peptides. II. Phi-psi maps for N-acetyl alanine N'-methyl amide: comparisons, contrasts and simple experimental tests. (1989) (155)
Self‐assembly of Congo Red—A theoretical and experimental approach to identify its supramolecular organization in water and salt solutions (1998) (89)
A comparison of the CHARMM, AMBER and ECEPP potentials for peptides. I. Conformational predictions for the tandemly repeated peptide (Asn-Ala-Asn-Pro)9. (1989) (88)
The structure and protein binding of amyloid-specific dye reagents. (2003) (63)
Supramolecular ligands: monomer structure and protein ligation capability. (1998) (53)
Why Congo red binding is specific for amyloid proteins - model studies and a computer analysis approach. (2001) (51)
Conformational subspace in simulation of early‐stage protein folding (2004) (47)
Congo red-stabilized intermediates in the lambda light chain transition from native to molten state. (1996) (44)
Bis azo dyes--studies on the mechanism of complex formation with IgG modulated by heating or antigen binding. (1993) (43)
Modelling the optimal simulation path in the peptide chain folding--studies based on geometry of alanine heptapeptide. (1995) (39)
The fuzzy oil drop model, based on hydrophobicity density distribution, generalizes the influence of water environment on protein structure and function. (2014) (39)
Two-intermediate model to characterize the structure of fast-folding proteins. (2011) (35)
Heat‐induced formation of a specific binding site for self‐assembled congo red in the V domain of immunoglobulin L chain λ (2001) (35)
Albumin binds self-assembling dyes as specific polymolecular ligands. (2006) (32)
Fuzzy oil drop model to interpret the structure of antifreeze proteins and their mutants (2011) (32)
Antifreeze proteins (2017) (32)
Early-Stage Folding in Proteins (In Silico) Sequence-to-Structure Relation (2005) (31)
Is the hydrophobic core a universal structural element in proteins? (2017) (30)
Research Article: The Use of Rigid, Fibrillar Congo Red Nanostructures for Scaffolding Protein Assemblies and Inducing the Formation of Amyloid‐like Arrangement of Molecules (2007) (30)
Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein Complexes (2016) (30)
The effect of azo dyes on the formation of immune complexes. (1991) (29)
Ligation site in proteins recognized in silico (2006) (28)
The geometrical analysis of peptide backbone structure and its local deformations. (1995) (28)
The use of congo red as a lyotropic liquid crystal to carry stains in a model immunotargeting system--microscopic studies. (1997) (27)
Fuzzy-Oil-Drop Hydrophobic Force Field—A Model to Represent Late-stage Folding (In Silico) of Lysozyme (2006) (27)
Effect of self association of bis-ANS and bis-azo dyes on protein binding. (1997) (26)
Why do antifreeze proteins require a solenoid? (2018) (25)
Supramolecularity creates nonstandard protein ligands. (1999) (24)
Local and long‐range structural effects caused by the removal of the N‐terminal polypeptide fragment from immunoglobulin L chain λ (2003) (22)
Localization of ligand binding site in proteins identified in silico (2007) (22)
Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model (2018) (22)
Lysozyme Folded In Silico According to the Limited Conformational Sub-space (2004) (21)
An approach to understand the complexation of supramolecular dye Congo red with immunoglobulin L chain λ (2005) (21)
Structural analysis of the Aβ(15-40) amyloid fibril based on hydrophobicity distribution. (2018) (20)
Analysis of correlated domain motions in IgG light chain reveals possible mechanisms of immunological signal transduction (2005) (20)
The Indirect Generation of Long‐distance Structural Changes in Antibodies upon their Binding to Antigen (2006) (19)
Structure of the Hydrophobic Core Determines the 3D Protein Structure—Verification by Single Mutation Proteins (2020) (18)
Hydrophobic collapse in late-stage folding (in silico) of bovine pancreatic trypsin inhibitor. (2006) (17)
In vivo accumulation of self-assembling dye Congo red in an area marked by specific immune complexes: possible relevance to chemotherapy. (2004) (16)
Influence of the electric field on supramolecular structure and properties of amyloid-specific reagent Congo red (2011) (16)
Evidence that supramolecular Congo red is the sole ligation form of this dye for L chain lambda derived amyloid proteins. (2001) (16)
Contribution to the Prediction of the Fold Code: Application to Immunoglobulin and Flavodoxin Cases (2015) (16)
The use of supramolecular structures as protein ligands (2013) (16)
Intramolecular signaling in immunoglobulins -- new evidence emerging from the use of supramolecular protein ligands. (2004) (15)
The Increased Flexibility of CDR Loops Generated in Antibodies by Congo Red Complexation Favors Antigen Binding (2006) (13)
Intrinsically disordered proteins--relation to general model expressing the active role of the water environment. (2014) (13)
Application of the fuzzy‐oil‐drop model to membrane protein simulation (2009) (13)
Heat-induced structural changes in the Fab fragment of IgG recognized by molecular dynamics stimulation--implications for signal transduction in antibodies. (1994) (13)
The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins (2019) (12)
Bis azo dye liquid crystalline micelles as possible drug carriers in immunotargeting technique. (1994) (12)
The melting of native domain structure in effector activation of IgG studied by using congo red as a specific probe. (1994) (12)
Dispersion of single-wall carbon nanotubes with supramolecular Congo red – properties of the complexes and mechanism of the interaction (2017) (12)
Instability of monoclonal myeloma protein may be identified as susceptibility to penetration and binding by newly synthesized Congo red derivatives. (2004) (12)
Intramolecular Immunological Signal Hypothesis Revived - Structural Background of Signalling Revealed by Using Congo Red as a Specific Tool (2014) (12)
Intermediates in the Protein Folding Process: A Computational Model (2011) (11)
Limitation of conformational space for proteins -- early stage folding simulation of human alpha and beta hemoglobin chains (2004) (11)
In silico Structural Study of Random Amino Acid Sequence Proteins Not Present in Nature (2009) (11)
The formation of soluble heat IgG aggregates for immunological studies. (1988) (11)
Protein distorsion-derived mechanism of signal discrimination in monocytes revealed using Congo red to stain activated cells. (2003) (11)
“Fuzzy oil drop” model applied to individual small proteins built of 70 amino acids (2010) (10)
Propagation of Fibrillar Structural Forms in Proteins Stopped by Naturally Occurring Short Polypeptide Chain Fragments (2017) (10)
Self-Assembled Molecules – New Kind of Protein Ligands (2018) (10)
Functional Characteristics of Small Proteins (70 Amino Acid Residues) Forming Protein-Nucleic Acid Complexes (2009) (10)
Model of Environmental Membrane Field for Transmembrane Proteins (2021) (10)
Ligand binding cavity encoded as a local hydrophobicity deficiency (2020) (9)
Egg yolk platelet proteins from Xenopus laevis are amyloidogenic. (2002) (9)
The aqueous environment as an active participant in the protein folding process. (2019) (9)
LIMITATION OF CONFORMATIONAL SPACE FOR PROTEINS – EARLY STAGE FOLDING SIMULATION OF HUMAN α AND β HEMOGLOBIN (2004) (9)
Towards the design of anti-amyloid short peptide helices (2018) (9)
Fuzzy Oil Drop Model Application—From Globular Proteins to Amyloids (2018) (9)
The detection of specific acute phase serum protein complexes and immune complexes by congo red binding. (1995) (9)
Downhill, Ultrafast and Fast Folding Proteins Revised (2020) (8)
In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model (2021) (8)
The Structure of Amyloid Versus the Structure of Globular Proteins (2020) (8)
Conservative secondary structure motifs already present in early-stage folding (in silico) as found in serpines family. (2008) (8)
Alternative Structures of α-Synuclein (2020) (7)
Hypothetical in silico model of the early-stage intermediate in protein folding (2013) (7)
The structural abnormality of myeloma immunoglobulins tested by Congo red binding. (2003) (7)
Geometric Parameters Defining the Structure of Proteins—Relation to Early-Stage Folding Step (2011) (7)
Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface (2020) (7)
Chaperonin Structure – The Large Multi-Subunit Protein Complex (2009) (7)
Description of the fuzzy oil drop model (2020) (7)
Serum albumin complexation of acetylsalicylic acid metabolites. (2009) (6)
The Functional Significance of Hydrophobic Residue Distribution in Bacterial Beta-Barrel Transmembrane Proteins (2021) (6)
Hydrophobic core formation in protein complex of cathepsin (2014) (6)
Determining protein similarity by comparing hydrophobic core structure (2017) (6)
Secondary and Supersecondary Structure of Proteins in Light of the Structure of Hydrophobic Cores. (2019) (6)
Structural role of exon-coded fragment of polypeptide chains in selected enzymes. (2013) (6)
Interaction of Supramolecular Congo Red and Congo Red-Doxorubicin Complexes with Proteins for Drug Carrier Design (2021) (6)
Internal force field in proteins seen by divergence entropy (2011) (6)
“Fuzzy oil drop” model verified positively (2011) (5)
Folding with active participation of water (2020) (5)
Sequence-to-Structure Relation in Proteins-Amyloidogenic Proteins with Chameleon Sequences (2016) (5)
Model of Early Stage Intermediate in Respect to Its Final Structure (2019) (5)
A tabular approach to the sequence-to-structure relation in proteins (tetrapeptide representation) for de novo protein design. (2006) (5)
Hydrophobic core in domains of immunoglobulin-like fold (2014) (5)
On the Dependence of Prion and Amyloid Structure on the Folding Environment. (2021) (5)
Silver ions as em marker of congo red ligation sites in amyloids and amyloid-like aggregates. (2017) (5)
Contingency Table Browser − prediction of early stage protein structure (2015) (5)
Never born proteins as a test case for ab initio protein structures prediction (2008) (5)
Impact of Doxorubicin on Self-Organization of Congo Red: Quantum Chemical Calculations and Molecular Dynamics Simulations (2020) (4)
Possible Mechanism of Amyloidogenesis of V Domains (2018) (4)
Amyloids, Congo red and the apple-green effect. (2019) (4)
INTEGRATION SCENARIOS OF VIRTUAL LEARNING ENVIRONMENTS WITH VIRTUAL PATIENTS SYSTEMS (2010) (4)
Solubility and Aggregation of Selected Proteins Interpreted on the Basis of Hydrophobicity Distribution (2021) (4)
Tandemly repeated trinucleotides - comparative analysis. (2006) (4)
Recognition of protein complexation based on hydrophobicity distribution (2009) (4)
Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins (2021) (4)
Globular or ribbon-like micelle (2020) (3)
On the need to introduce environmental characteristics in ab initio protein structure prediction using a coarse-grained UNRES force field. (2022) (3)
Structural Role of Hydrophobic Core in Proteins-Selected Examples (2016) (3)
Contribution to the Understanding of Protein–Protein Interface and Ligand Binding Site Based on Hydrophobicity Distribution—Application to Ferredoxin I and II Cases (2021) (3)
Information encoded in protein structure (2020) (3)
Formation of amyloid-like aggregates through the attachment of protein molecules to a Congo red scaffolding framework ordered under the influence of an electric field (2010) (3)
Supramolecular Structures as Carrier Systems Enabling the Use of Metal Ions in Antibacterial Therapy -- Self-Assembled Molecules – New Kind of Protein Ligands: Supramolecular Ligands (2018) (3)
Supramolecular Systems as Protein Ligands (2018) (3)
Solenoid – An amyloid under control (2020) (2)
Analysis of alternative conformations of the Aβ(1–40) amyloid protein (2020) (2)
In Silico Modeling of COVID-19 Pandemic Course Differentiation Using the FOD Model (2022) (2)
Proteins structured as spherical micelles (2020) (2)
Protein Conditioning for Binding Congo Red and Other Supramolecular Ligands (2018) (2)
Connexins and Pannexins—Similarities and Differences According to the FOD-M Model (2022) (2)
E-infrastructure technologies triggering of Bioinformatics development (2007) (2)
Different Synergy in Amyloids and Biologically Active Forms of Proteins (2019) (2)
Globular proteins, GU wobbling, and the evolution of the genetic code (2005) (2)
The COVID-19 Puzzle (2020) (2)
Summary: Protein is an intelligent micelle (2020) (1)
The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins (2022) (1)
Identification of tunnels as in potato hydrolases (2020) (1)
Anti-amyloid drug design (2020) (1)
The use of the Congo red-related dye DBACR to recognize the heavy chain-derived abnormality of myeloma immunoglobulins (2006) (1)
Local discordance (2020) (1)
The active site in a single-chain enzyme (2020) (1)
Internal force field in selected proteins. (2019) (1)
Amyloid as a ribbon-like micelle (2020) (1)
Composite structures (2020) (1)
Metal Ions Introduced to Proteins by Supramolecular Ligands (2018) (1)
New insights into disordered proteins and regions according to the FOD-M model (2022) (1)
[Clinical pattern of secondary dental caries in relation to tissue defect class and type of filling material]. (1990) (1)
Non-amyloid structure of the Aβ(1–42) polypeptide in presence of a permanent chaperone (2020) (1)
The Possible Mechanism of Amyloid Transformation Based on the Geometrical Parameters of Early-Stage Intermediate in Silico Model for Protein Folding (2022) (1)
2. Negative feedback inhibition – Fundamental biological regulation in cells and organisms (2015) (1)
Antibodies and drug-carriers in targeted therapy - progress and limitations (2001) (0)
Congo Red as a Supramolecular Carrier System for Doxorubicin: An Approach to Understanding the Mechanism of Action (2022) (0)
1 Filamentous aggregates of tau proteins fulfil standard 2 amyloid criteria 3 (2018) (0)
Amyloids identification based on fuzzy oil drop model (2020) (0)
Ig-like fold (2015) (0)
The hypothetical amyloid transformation of transthyretin (2020) (0)
Specificity of amino acid sequence and its role in secondary and supersecondary structure generation (2020) (0)
Convolutional ProteinUnetLM competitive with long short‐term memory‐based protein secondary structure predictors (2022) (0)
Lightweight ProteinUnet2 network for protein secondary structure prediction: a step towards proper evaluation (2022) (0)
Complexes Aβ(1–42) polypeptide with non-protein molecules (2020) (0)
ProteinUnet2 for Fast Protein Secondary Structure Prediction: A Step Towards Proper Evaluation (2021) (0)
Identification of the folding nucleus of globular protein: application to immunoglobulin-like and flavodoxin fold domains (2014) (0)
Secondary Structure in Amyloids in Relation to Their Wild Type Forms (2022) (0)
The Influence of Proteins Surface on the Ordering of Surrounded Water (2018) (0)
The XV century patients (as presented on Wit Stwosz altar) diagnozed. (2009) (0)
Hydrophobic core in β-sandwich-like domains (2020) (0)
Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid (2023) (0)
[Microorganisms isolated from clinical specimens in the Department of Bacteriology, Institute of Microbiology, Medical Academy, in Cracow 1980-1981]. (1985) (0)
In Search for the Definition of Life (2018) (0)
Prediction of ligand binding site and functionally important residues based on fuzzy-oil-drop model (2005) (0)
Antifreeze Compounds to Allow Survival at Temperatures below 0 C Deg. (2013) (0)
Early-stage folding in proteins-in silico model (2004) (0)
New insights on the catalytic center of proteins from peptidylprolyl isomerase group based on the FOD-M model. (2023) (0)
Structure of selected fragments of Aβ(1–42) in complex with other proteins (2020) (0)
The structure of the hinge region in Fab-Fc recombinant immunoglobulins and its relation to the effector activity of these molecules. (1987) (0)
Active site recognition in silico (2010) (0)
Divergence entropy to characterize the stability in selected enzymes – The role of disulfide bonds in respect to the structure of hydrophobic core (2015) (0)

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Irena Roterman-Konieczna's Academic­Influence.com Rankings