(Q27654095)

7

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Igor Polikarpov

object named as

Igor Polikarpov

8

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Laure Dumoutier

5

object named as

Laure Dumoutier

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author name string

Patricia Ribeiro de Moura

1

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Leandra Watanabe

2

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Didier Colau

4

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Muriel M Lemaire

Interleukin-10 therapy--review of a new approach

6

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language of work or name

English

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publication date

2 April 2009

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published in

FEBS Letters

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volume

583

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page(s)

1072-7

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issue

7

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cites work

1 reference

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Class II cytokine receptors and their ligands: key antiviral and inflammatory modulators

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Interleukin-22: a potential immunomodulatory molecule in the lung.

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Expression of interleukin-22 in rheumatoid arthritis: potential role as a proinflammatory cytokine.

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Interleukin-22 but not interleukin-17 provides protection to hepatocytes during acute liver inflammation

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Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation

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IL-22 increases the innate immunity of tissues

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Interleukin-22, a T(H)17 cytokine, mediates IL-23-induced dermal inflammation and acanthosis

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Human interleukin-10-related T cell-derived inducible factor: molecular cloning and functional characterization as an hepatocyte-stimulating factor

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Interleukin-22: a novel T- and NK-cell derived cytokine that regulates the biology of tissue cells

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Interleukin (IL)-22 and IL-17 are coexpressed by Th17 cells and cooperatively enhance expression of antimicrobial peptides

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Identification of the functional interleukin-22 (IL-22) receptor complex: the IL-10R2 chain (IL-10Rbeta ) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes

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Temporal associations between interleukin 22 and the extracellular domains of IL-22R and IL-10R2

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Crystal structure of the IL-22/IL-22R1 complex and its implications for the IL-22 signaling mechanism

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Structure of IL-22 bound to its high-affinity IL-22R1 chain

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The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation

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A soluble class II cytokine receptor, IL-22RA2, is a naturally occurring IL-22 antagonist

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Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to its soluble decoy receptor IL-22BP.

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Coot: model-building tools for molecular graphics

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Recent developments in the PHENIX software for automated crystallographic structure determination

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PROCHECK: a program to check the stereochemical quality of protein structures

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Inference of macromolecular assemblies from crystalline state

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Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site

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IL-22R, IL-10R2, and IL-22BP binding sites are topologically juxtaposed on adjacent and overlapping surfaces of IL-22.

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Electrostatics of nanosystems: application to microtubules and the ribosome

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