Karl E. Kadler mostly deals with Fibril, Extracellular matrix, Biophysics, Biochemistry and Tendon. His study in Fibril is interdisciplinary in nature, drawing from both Crystallography, Procollagen peptidase, Collagen fibril and Electron microscope. Karl E. Kadler combines subjects such as Extracellular and Cartilage, Anatomy with his study of Extracellular matrix.
He interconnects Process, Fibrillins, Epitope mapping and Function in the investigation of issues within Biophysics. His work carried out in the field of Tendon brings together such families of science as Lumican, Biglycan, Decorin and Tension. The various areas that he examines in his Fibrillogenesis study include Fibronectin, Collagen receptor, Morphogenesis and Secretory pathway.
His primary areas of study are Biochemistry, Extracellular matrix, Fibril, Cell biology and Biophysics. His research investigates the connection between Biochemistry and topics such as Procollagen peptidase that intersect with issues in Cleavage, Triple helix and Procollagen N-Endopeptidase. His Extracellular matrix study combines topics from a wide range of disciplines, such as Matrix, Fibroblast and Tendon, Anatomy.
His study of Fibrillogenesis is a part of Fibril. His Cell biology research incorporates themes from Collagen receptor, Wound healing, Mutant and Circadian clock, Circadian rhythm. His work on Collagen fibril as part of general Biophysics study is frequently linked to Tip growth, bridging the gap between disciplines.
His main research concerns Cell biology, Extracellular matrix, Tendon, Anatomy and Biophysics. His Cell biology research includes themes of Fibril, Procollagen peptidase and Circadian clock, Circadian rhythm. He studies Fibrillogenesis, a branch of Fibril.
His biological study spans a wide range of topics, including Wound healing, Fibroblast and Matrix, Pathology. Karl E. Kadler focuses mostly in the field of Anatomy, narrowing it down to matters related to Embryonic stem cell and, in some cases, Microscopy and Resolution. His Collagen fibril study in the realm of Biophysics interacts with subjects such as Mechanism and Structure based.
His primary scientific interests are in Extracellular matrix, Cell biology, Tendon, Anatomy and Fibril. His Extracellular matrix study integrates concerns from other disciplines, such as Fibrosis, Matrix, Pathology and Biophysics. He has included themes like Electron microscope, Mechanical strength and Short tendon in his Biophysics study.
His Cell biology research is multidisciplinary, incorporating perspectives in Molecular biology and Circadian clock, Circadian rhythm. His study in Anatomy is interdisciplinary in nature, drawing from both Endothelium and Bone morphogenesis. His primary area of study in Fibril is in the field of Fibrillogenesis.
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Collagen fibril formation
Karl E. Kadler;David F. Holmes;John A. Trotter;John A. Chapman.
Biochemical Journal (1996)
Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility
Keith G. Danielson;Helene Baribault;David F. Holmes;Helen Graham.
Journal of Cell Biology (1997)
Collagens at a glance
Karl E. Kadler;Clair Baldock;Jordi Bella;Raymond P. Boot-Handford.
Journal of Cell Science (2007)
Procollagen trafficking, processing and fibrillogenesis.
Elizabeth G. Canty;Karl E. Kadler.
Journal of Cell Science (2005)
Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators.
Karl E Kadler;Adele Hill;Elizabeth G Canty-Laird.
Current Opinion in Cell Biology (2008)
Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process.
K E Kadler;Y Hojima;D J Prockop.
Journal of Biological Chemistry (1987)
Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon.
Elizabeth G. Canty;Yinhui Lu;Roger S. Meadows;Michael K. Shaw.
Journal of Cell Biology (2004)
Corneal collagen fibril structure in three dimensions: Structural insights into fibril assembly, mechanical properties, and tissue organization
David F. Holmes;Christopher J. Gilpin;Clair Baldock;Ulrike Ziese.
Proceedings of the National Academy of Sciences of the United States of America (2001)
Cartilage Oligomeric Matrix Protein Interacts with Type IX Collagen, and Disruptions to These Interactions Identify a Pathogenetic Mechanism in a Bone Dysplasia Family
Paul Holden;Roger S. Meadows;Kathryn L. Chapman;Michael E. Grant.
Journal of Biological Chemistry (2001)
Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction.
Helen K Graham;David F Holmes;Rod B Watson;Karl E Kadler.
Journal of Molecular Biology (2000)
Profile was last updated on December 6th, 2021.
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