2014
DOI: 10.1016/j.jsb.2014.03.010
|View full text |Cite
|
Sign up to set email alerts
|

Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

11
116
0

Year Published

2015
2015
2022
2022

Publication Types

Select...
9

Relationship

6
3

Authors

Journals

citations
Cited by 68 publications
(127 citation statements)
references
References 51 publications
11
116
0
Order By: Relevance
“…TEM as well as AFM revealed fibrillar structures (Figure A,B), exhibiting a length of around 200–500 nm, average diameters of 15 nm (Figure A), and heights in the range of 1.0–1.3 nm (Figure B). Length and diameter of eMaSp1s fibrils is consistent with values reported earlier for recombinant spider silk fibrils …”
Section: Resultssupporting
confidence: 90%
“…TEM as well as AFM revealed fibrillar structures (Figure A,B), exhibiting a length of around 200–500 nm, average diameters of 15 nm (Figure A), and heights in the range of 1.0–1.3 nm (Figure B). Length and diameter of eMaSp1s fibrils is consistent with values reported earlier for recombinant spider silk fibrils …”
Section: Resultssupporting
confidence: 90%
“…19,[22][23][24]49,55,[58][59][60][61][62] Here, the protein was modified with different tags for stimulating internalization of respective protein particles by HeLa cells (Fig. 19,[22][23][24]49,55,[58][59][60][61][62] Here, the protein was modified with different tags for stimulating internalization of respective protein particles by HeLa cells (Fig.…”
Section: Spider Silk Protein Modificationmentioning
confidence: 99%
“…The nano‐ and micro‐scale self‐assemblies are constructed mainly of nanoparticles, nanofibrils, microspheres, and vesicles, whereas macro‐scale self‐assembly focuses on developing macroscopic materials, such as hydrogels and fibers. Most of these self‐assembly processes were conducted in aqueous solutions . However, some RSSPs, such as spidroin variants from the C‐terminal domain of the major ampullate and cylindriform silk, as well as major ampullate spidroin‐like RSSP with a high ratio of hydrophobic polyalanine regions, have limited water‐solubility.…”
Section: Multiscale Self‐assembly Of the Rsspsmentioning
confidence: 99%