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Forced detachment of the CD2-CD58 complex
scientific article
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instance of
scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
title
Forced detachment of the CD2-CD58 complex
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
author name string
M V Bayas
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
K Schulten
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
D Leckband
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
language of work or name
English
0 references
publication date
1 April 2003
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
published in
Biophysical Journal
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
volume
84
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
page(s)
2223-2233
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
issue
4
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
cites work
All-atom empirical potential for molecular modeling and dynamics studies of proteins
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PubMed Central
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5 July 2018
Direct measurements of heterotypic adhesion between the cell surface proteins CD2 and CD48
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5 July 2018
Steered molecular dynamics and mechanical functions of proteins
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PubMed Central
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5 July 2018
Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule.
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PubMed Central
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5 July 2018
Single molecular force spectroscopy of modular proteins in the nervous system
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PubMed Central
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5 July 2018
Mechanical unfolding intermediates in titin modules.
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5 July 2018
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors
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PubMed Central
reference URL
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5 July 2018
Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution
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PubMed Central
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5 July 2018
Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch
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PubMed Central
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5 July 2018
CD2 and the nature of protein interactions mediating cell-cell recognition.
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PubMed Central
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5 July 2018
Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
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5 July 2018
The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2
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5 July 2018
The molecular structure of cell adhesion molecules
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PubMed Central
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5 July 2018
Molecular dynamics study of unbinding of the avidin-biotin complex
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5 July 2018
Dynamic strength of molecular adhesion bonds
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5 July 2018
VMD: visual molecular dynamics
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5 July 2018
The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy
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5 July 2018
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution
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5 July 2018
The immunoglobulin fold. Structural classification, sequence patterns and common core
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5 July 2018
Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1302789
retrieved
5 July 2018
The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC'C" face of the human CD2 adhesion domain
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1302789
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5 July 2018
Role of interaction of CD2 molecules with lymphocyte function-associated antigen 3 in T-cell recognition of nominal antigen
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1302789
retrieved
5 July 2018
Molecular dissection of the CD2-CD58 counter-receptor interface identifies CD2 Tyr86 and CD58 Lys34 residues as the functional "hot spot".
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1302789
retrieved
28 October 2018
CD2-mediated adhesion facilitates T lymphocyte antigen recognition function
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1302789
retrieved
28 October 2018
Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy
1 reference
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Crossref
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https://api.crossref.org/works/10.1016%2FS0006-3495%2803%2975028-0
retrieved
7 January 2021
The Immunoglobulin Fold
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/12668431
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/S0006-3495(03)75028-0
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
PMCID
1302789
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
PubMed ID
12668431
1 reference
stated in
Europe PubMed Central
PubMed ID
12668431
retrieved
31 July 2017
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