(Q24674457)

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Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models

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scholarly article

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Structure-based modeling of the ligand binding domain of the human cell surface receptor CD23 and comparison of two independently derived molecular models (English)

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1 reference

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author name string

J Bajorath

1

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A Aruffo

2

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publication date

February 1996

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Protein Science

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5

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2

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240-7

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The relation between the divergence of sequence and structure in proteins

2 references

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7 April 2017

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7 January 2021

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Trimeric structure of a C-type mannose-binding protein

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Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil

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Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains

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Structure of the Calcium-Dependent Lectin Domain from a Rat Mannose-Binding Protein Determined by MAD Phasing

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Structure of a C-type mannose-binding protein complexed with an oligosaccharide

1 reference

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7 April 2017

The Protein Data Bank: a computer-based archival file for macromolecular structures

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7 April 2017

Modeling of the lectin-homology domains of the human and murine low-affinity Fc epsilon receptor (Fc epsilon RII/CD23)

1 reference

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Recognition of errors in three-dimensional structures of proteins

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CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD11b-CD18 and CD11c-CD18

1 reference

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CD23 interacts with a new functional extracytoplasmic domain involving N-linked oligosaccharides on CD21

1 reference

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Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes

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P- and E-selectin use common sites for carbohydrate ligand recognition and cell adhesion

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Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

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7 April 2017

Receptors for IgE.

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28 September 2017

Modelling the carbohydrate recognition domain of human E-selectin

1 reference

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Structure of antibody hypervariable loops reproduced by a conformational search algorithm

1 reference

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Two distinct classes of carbohydrate-recognition domains in animal lectins

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Biology and chemistry of low affinity IgE receptor (Fc epsilon RII/CD23)

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Immunohistochemical demonstration of CD23 expression on lymphocytes in rheumatoid synovitis

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The low-affinity receptor for IgE

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28 September 2017

Alpha-helical coiled-coil stalks in the low-affinity receptor for IgE (Fc epsilon RII/CD23) and related C-type lectins

1 reference

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28 September 2017

A B cell-specific differentiation antigen, CD23, is a receptor for IgE (Fc epsilon R) on lymphocytes

1 reference

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30 May 2018

Identification of an E-selectin region critical for carbohydrate recognition and cell adhesion

1 reference

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30 May 2018

Molecular model of the extracellular lectin-like domain in CD69

1 reference

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Immunoglobulin E-binding site in Fc epsilon receptor (Fc epsilon RII/CD23) identified by homolog-scanning mutagenesis

1 reference

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Comparison of a protein model with its X-ray structure: the ligand binding domain of E-selectin

1 reference

https://pubmed.ncbi.nlm.nih.gov/8745401

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Marked amelioration of established collagen-induced arthritis by treatment with antibodies to CD23 in vivo

1 reference

https://pubmed.ncbi.nlm.nih.gov/8745401

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Interaction of P-selectin (CD62) and its cellular ligand: analysis of critical residues

1 reference

https://pubmed.ncbi.nlm.nih.gov/8745401

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Knowledge-based model building of proteins: concepts and examples

1 reference

https://api.crossref.org/works/10.1002%2FPRO.5560050207

7 January 2021

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Molecular structure of human lymphocyte receptor for immunoglobulin E

1 reference

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inferred from DOI database lookup

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

1 reference

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based on heuristic

inferred from DOI database lookup

Identifiers

10.1002/PRO.5560050207

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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