scholarly journals GLUE That Sticks to HIV: A Helix-Grafted GLUE Protein That Selectively Binds the HIV gp41 N-Terminal Helical Region

ChemBioChem ◽  
2014 ◽  
Vol 16 (2) ◽  
pp. 219-222 ◽  
Author(s):  
Susanne N. Walker ◽  
Rachel L. Tennyson ◽  
Alex M. Chapman ◽  
Alan J. Kennan ◽  
Brian R. McNaughton
Keyword(s):  
Glue Protein ◽  
Helical Region ◽  
Hiv Gp41

Adhesive Property and Mechanism of Silkworm Egg Glue Protein

2021 ◽  
Author(s):  
Yutian Lei ◽  
Kaiyu Guo ◽  
Yan Zhang ◽  
Xiaolu Zhang ◽  
Lixia Qin ◽  
...  
Keyword(s):  
Adhesive Property ◽  
Glue Protein

Mussel glue protein has an open conformation

1989 ◽  
Vol 269 (2) ◽  
pp. 415-422 ◽  
Author(s):  
Taffy Williams ◽  
Keishi Marumo ◽  
J.Herbert Waite ◽  
Robert W. Henkens
Keyword(s):  
Open Conformation ◽  
Glue Protein

scholarly journals Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1

Open Biology ◽  
2014 ◽  
Vol 4 (3) ◽  
pp. 130172 ◽  
Author(s):  
Barbara Franke ◽  
Alexander Gasch ◽  
Dayté Rodriguez ◽  
Mohamed Chami ◽  
Muzamil M. Khan ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Quaternary Structure ◽  
E3 Ubiquitin Ligase ◽  
Coiled Coil ◽  
Trim Protein ◽  
Muscle Catabolism ◽  
And Function ◽  
Helical Region ◽  
Structural Significance

MuRF1 is an E3 ubiquitin ligase central to muscle catabolism. It belongs to the TRIM protein family characterized by a tripartite fold of RING, B-box and coiled-coil (CC) motifs, followed by variable C-terminal domains. The CC motif is hypothesized to be responsible for domain organization in the fold as well as for high-order assembly into functional entities. But data on CC from this family that can clarify the structural significance of this motif are scarce. We have characterized the helical region from MuRF1 and show that, contrary to expectations, its CC domain assembles unproductively, being the B2- and COS-boxes in the fold (respectively flanking the CC) that promote a native quaternary structure. In particular, the C-terminal COS-box seemingly forms an α-hairpin that packs against the CC, influencing its dimerization. This shows that a C-terminal variable domain can be tightly integrated within the conserved TRIM fold to modulate its structure and function. Furthermore, data from transfected muscle show that in MuRF1 the COS-box mediates the in vivo targeting of sarcoskeletal structures and points to the pharmacological relevance of the COS domain for treating MuRF1-mediated muscle atrophy.

scholarly journals Leucine-58 in the putative 5th helical region of human interleukin (IL)-6 is important for activation of the IL-6 signal transducer, gp130

FEBS Letters ◽  
1995 ◽  
Vol 369 (2-3) ◽  
pp. 187-191 ◽  
Author(s):  
Floris D. de Hon ◽  
Hanny Klaasse Bos ◽  
Saskia B. Ebeling ◽  
Joachim Grötzinger ◽  
Günther Kurapkat ◽  
...  
Keyword(s):  
Signal Transducer ◽  
Helical Region

Development of a FRET Assay for Monitoring of HIV gp41 Core Disruption

2007 ◽  
Vol 72 (18) ◽  
pp. 6700-6707 ◽  
Author(s):  
Yang Xu ◽  
Mark S. Hixon ◽  
Philip E. Dawson ◽  
Kim D. Janda
Keyword(s):  
Hiv Gp41

scholarly journals Autoimmunity to type II collagen an experimental model of arthritis.

1977 ◽  
Vol 146 (3) ◽  
pp. 857-868 ◽  
Author(s):  
D E Trentham ◽  
A S Townes ◽  
A H Kang
Keyword(s):  
Type Ii Collagen ◽  
Intradermal Injection ◽  
Type I ◽  
Type Ii ◽  
Incomplete Freund’S Adjuvant ◽  
Freund’S Adjuvant ◽  
Freund's Adjuvant ◽  
Cartilage Proteoglycans ◽  
Bacterial Preparations ◽  
Helical Region

We have found that intradermal injection of native type II collagen extracted from human, chick or rat cartilage induces an inflammatory arthritis in approximately 40% of rats of several strains whether complete Freund's adjuvant or incomplete Freund's adjuvant is used. Type I or III collagen extracted from skin, cartilage proteoglycans and alpha1(II) chains were incapable of eliciting arthritis, as was type II collagen injected without adjuvant. The disease is a chronic proliferative synovitis, resembling adjuvant arthritis in rats and rheumatoid arthritis in humans. Native type II co-lagen modified by limited pepsin digestion still produces arthritis, suggesting that type-specific determinants residing in the helical region of the molecule are responsible for the induction of disease. Since homologous type II collagen emulsified in oil without bacterial preparations regularly causes the disease, this new animal model of arthritis represents a unique example of experimentally-inducible autoimmunity to a tissue component.

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