Amino Acid Sequence Requirements of Laminin β1 Chain Peptide B133 (DISTKYFQMSLE) for Amyloid-like Fibril Formation, Syndecan Binding, and Neurite Outgrowth Promotion

Biochemistry ◽  
2010 ◽  
Vol 49 (28) ◽  
pp. 5909-5918 ◽  
Author(s):  
Fumihiko Katagiri ◽  
Kazuki Takeyama ◽  
Yukiko Ohga ◽  
Kentaro Hozumi ◽  
Yamato Kikkawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurite Outgrowth ◽  
Fibril Formation ◽  
Sequence Requirements

Fibril Formation of hsp10 Homologue Proteins and Determination of Fibril Core Regions: Differences in Fibril Core Regions Dependent on Subtle Differences in Amino Acid Sequence

2008 ◽  
Vol 377 (5) ◽  
pp. 1593-1606 ◽  
Author(s):  
Hisashi Yagi ◽  
Ai Sato ◽  
Akihiro Yoshida ◽  
Yoshiki Hattori ◽  
Masahiro Hara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fibril Formation

scholarly journals Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

2010 ◽  
Vol 285 (23) ◽  
pp. 17465-17470 ◽  
Author(s):  
Saori Kunii ◽  
Koichi Morimoto ◽  
Kouhei Nagai ◽  
Takuya Saito ◽  
Kenji Sato ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals Amino Acid Sequence Requirements of the Transmembrane and Cytoplasmic Domains of Influenza Virus Hemagglutinin for Viable Membrane Fusion

1999 ◽  
Vol 10 (6) ◽  
pp. 1821-1836 ◽  
Author(s):  
Grigory B. Melikyan ◽  
Sasa Lin ◽  
Michael G. Roth ◽  
Fredric S. Cohen
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Membrane Fusion ◽  
Integral Membrane Protein ◽  
Wild Type ◽  
Influenza Virus Hemagglutinin ◽  
Tm Domain ◽  
Fusion Pores ◽  
Sequence Requirements

The amino acid sequence requirements of the transmembrane (TM) domain and cytoplasmic tail (CT) of the hemagglutinin (HA) of influenza virus in membrane fusion have been investigated. Fusion properties of wild-type HA were compared with those of chimeras consisting of the ectodomain of HA and the TM domain and/or CT of polyimmunoglobulin receptor, a nonviral integral membrane protein. The presence of a CT was not required for fusion. But when a TM domain and CT were present, fusion activity was greater when they were derived from the same protein than derived from different proteins. In fact, the chimera with a TM domain of HA and truncated CT of polyimmunoglobulin receptor did not support full fusion, indicating that the two regions are not functionally independent. Despite the fact that there is wide latitude in the sequence of the TM domain that supports fusion, a point mutation of a semiconserved residue within the TM domain of HA inhibited fusion. The ability of a foreign TM domain to support fusion contradicts the hypothesis that a pore is composed solely of fusion proteins and supports the theory that the TM domain creates fusion pores after a stage of hemifusion has been achieved.

Amino acid sequence requirements for the epitope recognized by a monoclonal antibody reacting with the secreted antigen GP28.5 of Toxoplasma gondii

1992 ◽  
Vol 29 (11) ◽  
pp. 1375-1382 ◽  
Author(s):  
M.F. Cesbron-Delauw ◽  
C. Boutillon ◽  
C. Mercier ◽  
M.P. Fourmaux ◽  
A. Murray ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Toxoplasma Gondii ◽  
Amino Acid Sequence ◽  
Sequence Requirements

Amino acid sequence requirements in the human IgAl hinge for cleavage by streptococcal IgAl proteases

2002 ◽  
Vol 30 (3) ◽  
pp. A68-A68
Author(s):  
B. W. Senior ◽  
M. R. Batten ◽  
M. Kilian ◽  
J. M. Woof
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Requirements

SEARCH FOR FOLDING INITIATION SITES FROM AMINO ACID SEQUENCE

2008 ◽  
Vol 06 (04) ◽  
pp. 681-691 ◽  
Author(s):  
OXANA V. GALZITSKAYA
Keyword(s):  
Protein Folding ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Transition State ◽  
Initiation Site ◽  
Ribonuclease A ◽  
Fibril Formation ◽  
Protein Chain ◽  
Folding Nucleus ◽  
Key Residues

A crucial event in protein folding is the formation of a folding nucleus, which is a structured part of the protein chain in the transition state. We demonstrate a correlation between locations of residues involved in the folding nuclei and locations of predicted amyloidogenic regions. The average Φ-values are significantly greater inside amyloidogenic regions than outside them. We have found that fibril formation and normal folding involve many of the same key residues, giving an opportunity to outline the folding initiation site in protein chains. The search for folding initiation sites for apomyoglobin and ribonuclease. A coincides with the predictions made by other approaches.

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