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Aggregation-resistant domain antibodies selected on phage by heat denaturation
scientific article published on 08 August 2004
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instance of
scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
title
Aggregation-resistant domain antibodies selected on phage by heat denaturation
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
author name string
Laurent Jespers
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
Oliver Schon
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
Kristoffer Famm
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
Greg Winter
series ordinal
4
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
publication date
8 August 2004
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
published in
Nature Biotechnology
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
volume
22
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
page(s)
1161-1165
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
issue
9
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
exact match
https://scigraph.springernature.com/pub.10.1038/nbt1000
0 references
cites work
Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
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Biophysical Properties of Camelid VHHDomains Compared to Those of Human VH3 Domains†
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Single-domain antibody fragments with high conformational stability
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7 January 2021
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Thermal Unfolding of a Llama Antibody Fragment: A Two-State Reversible Process†
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Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies
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7 January 2021
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Crystal structure of HEL4, a soluble, refoldable human V(H) single domain with a germ-line scaffold.
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Phage antibodies: filamentous phage displaying antibody variable domains
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7 January 2021
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Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability
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7 January 2021
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Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
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7 January 2021
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Biophysical properties of human antibody variable domains
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7 January 2021
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Binders Based on Dimerised Immunoglobulin VH Domains
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7 January 2021
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Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
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7 January 2021
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Proteolytic selection for protein folding using filamentous bacteriophages
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7 January 2021
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Selecting proteins with improved stability by a phage-based method
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7 January 2021
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In-vitro selection of highly stabilized protein variants with optimized surface
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Directed evolution of a stable scaffold for T-cell receptor engineering.
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Selection for improved protein stability by phage display.
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The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops
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Stability engineering of antibody single-chain Fv fragments
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Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
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Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
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7 January 2021
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Structural repertoire of the human VH segments
1 reference
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Crossref
reference URL
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7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/NBT1000
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
PubMed ID
15300256
1 reference
stated in
Europe PubMed Central
PubMed ID
15300256
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15300256%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 December 2019
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