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Prevalence Estimates of Predicted Pathogenic COL4A3-COL4A5 Variants in a Population Sequencing Database and Their Implications for Alport Syndrome

Journal of the American Society of Nephrology, 2021-09, Vol.32 (9), p.2273-2290

2021

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Variation in the helical structure of native collagen

PloS one, 2014-02, Vol.9 (2), p.e89519-e89519

2014

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Pervasive variation of transcription factor orthologs contributes to regulatory network evolution

PLoS genetics, 2015-03, Vol.11 (3), p.e1005011-e1005011

2015

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Prediction of Collagen Stability from Amino Acid Sequence

The Journal of biological chemistry, 2005-05, Vol.280 (19), p.19343-19349

2005

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Predicting DNA recognition by Cys2His2 zinc finger proteins

Bioinformatics, 2009-01, Vol.25 (1), p.22-29

2009

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A systematic survey of the Cys2His2 zinc finger DNA-binding landscape

Nucleic acids research, 2015-02, Vol.43 (3), p.1965-1984

2015

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X-Linked and Autosomal Recessive Alport Syndrome: Pathogenic Variant Features and Further Genotype-Phenotype Correlations

PloS one, 2016-09, Vol.11 (9), p.e0161802-e0161802

2016

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The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

PloS one, 2017, Vol.12 (7), p.e0175582-e0175582

2017

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Equilibrium thermal transitions of collagen model peptides

Protein science, 2004-04, Vol.13 (4), p.893-902

2004

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Electrostatic Interactions Involving Lysine Make Major Contributions to Collagen Triple-Helix Stability

Biochemistry (Easton), 2005-02, Vol.44 (5), p.1414-1422

2005

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De novo prediction of DNA-binding specificities for Cys2His2 zinc finger proteins

Nucleic acids research, 2014-01, Vol.42 (1), p.97-108

2014

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Deep sequencing of large library selections allows computational discovery of diverse sets of zinc fingers that bind common targets

Nucleic acids research, 2014-02, Vol.42 (3), p.1497-1508

2014

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Amino Acid Propensities for the Collagen Triple-Helix

Biochemistry (Easton), 2000-12, Vol.39 (48), p.14960-14967

2000

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An expanded binding model for Cys2His2 zinc finger protein–DNA interfaces

Physical biology, 2011-06, Vol.8 (3), p.035010-035010

2011

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Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disorders

Human mutation, 2004-10, Vol.24 (4), p.330-337

2004

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Unstable Molecules Form Stable Tissues

Proceedings of the National Academy of Sciences - PNAS, 2002-02, Vol.99 (3), p.1101-1103

2002

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Triple-Helix Propensity of Hydroxyproline and Fluoroproline: Comparison of Host−Guest and Repeating Tripeptide Collagen Models

Journal of the American Chemical Society, 2003-09, Vol.125 (38), p.11500-11501

2003

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Designed Coiled Coils Promote Folding of a Recombinant Bacterial Collagen

The Journal of biological chemistry, 2011-05, Vol.286 (20), p.17512-17520

2011

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Peptide investigations of pairwise interactions in the collagen triple-helix

Journal of molecular biology, 2002-02, Vol.316 (2), p.385-394

2002

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Y-position cysteine substitution in type I collagen (α1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype

Human mutation, 2007-04, Vol.28 (4), p.396-405

2007

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Molecular Structure of the Collagen Triple Helix

Advances in Protein Chemistry, 2005, Vol.70, p.301-339

2005

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Self-association of Collagen Triple Helic Peptides into Higher Order Structures

The Journal of biological chemistry, 2006-11, Vol.281 (44), p.33283-33290

2006

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Pervasive Variation of Transcription Factor Orthologs Contributes to Regulatory Network Evolution: e1005011

PLoS genetics, 2015-03, Vol.11 (3)

2015

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Collagen model peptides: Sequence dependence of triple-helix stability

Biopolymers, 2000, Vol.55 (6), p.436-450

2000

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The coll[alpha]gen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

PloS one, 2017-07, Vol.12 (7), p.e0175582

2017

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Prevalence Estimates of Predicted Pathogenic COL4A3-COL4A5 Variants in a Population Sequencing Database and Their Implications for Alport Syndrome

Variation in the helical structure of native collagen

Pervasive variation of transcription factor orthologs contributes to regulatory network evolution

Prediction of Collagen Stability from Amino Acid Sequence

Predicting DNA recognition by Cys2His2 zinc finger proteins

A systematic survey of the Cys2His2 zinc finger DNA-binding landscape

X-Linked and Autosomal Recessive Alport Syndrome: Pathogenic Variant Features and Further Genotype-Phenotype Correlations

The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

Equilibrium thermal transitions of collagen model peptides

Electrostatic Interactions Involving Lysine Make Major Contributions to Collagen Triple-Helix Stability

De novo prediction of DNA-binding specificities for Cys2His2 zinc finger proteins

Deep sequencing of large library selections allows computational discovery of diverse sets of zinc fingers that bind common targets

Amino Acid Propensities for the Collagen Triple-Helix

An expanded binding model for Cys2His2 zinc finger protein–DNA interfaces

Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disorders

Unstable Molecules Form Stable Tissues

Triple-Helix Propensity of Hydroxyproline and Fluoroproline: Comparison of Host−Guest and Repeating Tripeptide Collagen Models

Designed Coiled Coils Promote Folding of a Recombinant Bacterial Collagen

Peptide investigations of pairwise interactions in the collagen triple-helix

Y-position cysteine substitution in type I collagen (α1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype

Molecular Structure of the Collagen Triple Helix

Self-association of Collagen Triple Helic Peptides into Higher Order Structures

Pervasive Variation of Transcription Factor Orthologs Contributes to Regulatory Network Evolution: e1005011

Collagen model peptides: Sequence dependence of triple-helix stability

The coll[alpha]gen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

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