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Streptavidin
Known as:
Strepavidin
, Streptavidin [Chemical/Ingredient]
A bacterial protein that has high affinity for biotin. The non-covalent streptavidin-biotin complex is resistant to organic solvents, denaturants…
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National Institutes of Health
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Related topics
Related topics
15 relations
Bacteria
Binding Proteins
Biotin
In Blood
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Broader (2)
Bacterial Proteins
Indicators and Reagents
Narrower (1)
traptavidin
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2011
Review
2011
Tailoring nanocarriers for intracellular protein delivery.
Zhen Gu
,
A. Biswas
,
Muxun Zhao
,
Yi Tang
Chemical Society Reviews
2011
Corpus ID: 5321048
Proteins play a crucial role in life, taking part in all vital processes in the body. In the past decade, there was increasing…
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Highly Cited
2006
Highly Cited
2006
A monovalent streptavidin with a single femtomolar biotin binding site
M. Howarth
,
D. Chinnapen
,
+5 authors
A. Ting
Nature Methods
2006
Corpus ID: 11254521
Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers…
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Highly Cited
2003
Highly Cited
2003
Characterization of DNA immobilization and subsequent hybridization on a 2D arrangement of streptavidin on a biotin-modified lipid bilayer supported on SiO2.
C. Larsson
,
M. Rodahl
,
F. Höök
Analytical Chemistry
2003
Corpus ID: 43739463
We show how the water content (and effective density) of thin adsorbed films composed of biomolecules can be determined using…
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Highly Cited
2001
Highly Cited
2001
One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag.
Anthony D. Keefe
,
David S. Wilson
,
B. Seelig
,
J. Szostak
Protein Expression and Purification
2001
Corpus ID: 6318975
We describe the use of the SBP-tag, a new streptavidin-binding peptide, for both the one-step purification and the detection of…
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Highly Cited
1995
Highly Cited
1995
Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
D. Görlich
,
S. Kostka
,
+4 authors
S. Prehn
Current Biology
1995
Corpus ID: 6055941
Highly Cited
1991
Highly Cited
1991
Activity of amphipathic poly(ethylene glycol) 5000 to prolong the circulation time of liposomes depends on the liposome size and is unfavorable for immunoliposome binding to target.
A. Klibanov
,
Kazuo Maruyama
,
Anne Marie Beckerleg
,
Vladimir P. Torchilin
,
Leaf Huang
Biochimica et Biophysica Acta
1991
Corpus ID: 27584683
Highly Cited
1990
Highly Cited
1990
Random peptide libraries: a source of specific protein binding molecules.
James J. Devlin
,
L. C. Panganiban
,
P. Devlin
Science
1990
Corpus ID: 1437430
Libraries of random peptide sequences were constructed and screened to identify peptides that specifically bind to proteins. In…
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Highly Cited
1989
Highly Cited
1989
Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.
Wayne A. HENDRICKSONt
,
Arno PAHLERt
,
Janet L. SMITHtt
,
Yoshinori Satow
,
Ethan A. MERRITTIItt
,
'. R.PAULPHIZACKERLEY
Proceedings of the National Academy of Sciences…
1989
Corpus ID: 19291464
A three-dimensional crystal structure of the biotin-binding core of streptavidin has been determined at 3.1-A resolution. The…
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Highly Cited
1989
Highly Cited
1989
A two-site monoclonal antibody ELISA for the quantification of the major Dermatophagoides spp. allergens, Der p I and Der f I.
C. Luczynska
,
L. Arruda
,
ThomasA. E. Platts-Mills
,
Jeffrey D. Miller
,
Manuel Lopez
,
M. Chapman
JIM - Journal of Immunological Methods
1989
Corpus ID: 8860076
Highly Cited
1983
Highly Cited
1983
Rapid and sensitive colorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots.
J. Leary
,
D. Brigati
,
D. Ward
Proceedings of the National Academy of Sciences…
1983
Corpus ID: 23945694
Biotin-labelled DNA probes, prepared by nick-translation in the presence of biotinylated analogs of TTP, are hybridized to DNA or…
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