Conformational flexibility and allosteric regulation of cathepsin K. (Q43070071)

13 November 2017

Conformational flexibility and allosteric regulation of cathepsin K. (English)

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13 November 2017

Marko Novinec

1

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Antonio Baici

object named as

Antonio Baici

series ordinal

4

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author name string

Lidija Kovacic

series ordinal

2

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PubMed ID

20450492

13 November 2017

Brigita Lenarcic

series ordinal

3

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PubMed ID

20450492

13 November 2017

language of work or name

English

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publication date

1 July 2010

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13 November 2017

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13 November 2017

429

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13 November 2017

2

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13 November 2017

379-389

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Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

13 November 2017

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Allosteric proteins and cellular control systems

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Allostery: absence of a change in shape does not imply that allostery is not at play

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Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency

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Biochemical properties and regulation of cathepsin K activity

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Cathepsin K and schizophrenia.

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Deficiency and inhibition of cathepsin K reduce body weight gain and increase glucose metabolism in mice

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Cathepsin K inhibitors: a novel target for osteoporosis therapy

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Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate

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The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex

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Cathepsin B activity regulation. Heparin-like glycosaminogylcans protect human cathepsin B from alkaline pH-induced inactivation.

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Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions

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Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans

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Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme

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Expression in Escherichia coli, refolding, and purification of human procathepsin K, an osteoclast-specific protease

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Paradoxical interactions between modifiers and elastase-2.

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Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification

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Simultaneous interaction of enzymes with two modifiers: reappraisal of kinetic models and new paradigms.

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Application of a Theory of Enzyme Specificity to Protein Synthesis

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The role of dynamics in allosteric regulation

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Regulation of collagenase activities of human cathepsins by glycosaminoglycans

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Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans

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Serglycin--structure and biology

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The effects of heparin and low molecular weight heparins on bone

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Heparan sulphate proteoglycans fine-tune mammalian physiology

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Is allostery an intrinsic property of all dynamic proteins?

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DNA accelerates the inhibition of human cathepsin V by serpins

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The changing landscape of protein allostery

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The specific velocity plot. A graphical method for determining inhibition parameters for both linear and hyperbolic enzyme inhibitors.

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VMD: visual molecular dynamics

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Scalable molecular dynamics with NAMD

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All-atom empirical potential for molecular modeling and dynamics studies of proteins

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Generation of nucleophilic character in the Cys25/His159 ion pair of papain involves Trp177 but not Asp158.

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Structural insights into biological roles of protein-glycosaminoglycan interactions

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Interaction between Human Cathepsins K, L, and S and Elastins

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21 January 2018

Identifiers

DOI

10.1042/BJ20100337

1 reference

13 November 2017

1 reference

PubMed ID

20450492