Hydrophobic Cluster Formation Is Necessary for Dibenzofuran-Based Amino Acids to Function as .beta.-Sheet Nucleators

1994 ◽  
Vol 116 (9) ◽  
pp. 3988-4005 ◽  
Author(s):  
Kwok Yin Tsang ◽  
Humberto Diaz ◽  
Nilsa Graciani ◽  
Jeffery W. Kelly
Keyword(s):  
Amino Acids ◽  
Cluster Formation ◽  
Beta Sheet ◽  
Hydrophobic Cluster

Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane

2002 ◽  
Vol 115 (8) ◽  
pp. 1583-1590 ◽  
Author(s):  
Angela I. M. Barth ◽  
Kathleen A. Siemers ◽  
W. James Nelson
Keyword(s):  
Amino Acids ◽  
Cluster Formation ◽  
Adenomatous Polyposis ◽  
Polyposis Coli ◽  
Binding Domains ◽  
C Terminus ◽  
Endogenous Proteins ◽  
Apc Protein ◽  
Necessary And Sufficient ◽  
Armadillo Repeats

End-binding protein (EB) 1 binds to the C-terminus of adenomatous polyposis coli (APC) protein and to the plus ends of microtubules (MT) and has been implicated in the regulation of APC accumulation in cortical clusters at the tip of extending membranes. We investigated which APC domains are involved in cluster localization and whether binding to EB1 or MTs is essential for APC cluster localization. Armadillo repeats of APC that lack EB1- and MT-binding domains are necessary and sufficient for APC localization in cortical clusters; an APC fragment lacking the armadillo repeats, but containing MT-and EB1-binding domains, does not localize to the cortical clusters but instead co-aligns with MTs throughout the cell. Significantly, analysis of endogenous proteins reveals that EB1 does not accumulate in the APC clusters. However, overexpressed EB1 does accumulate in APC clusters; the APC-binding domain in EB1 is located in the C-terminal region of EB1 between amino acids 134 and 268. Overexpressed APC- or MT-binding domains of EB1 localize to APC cortical clusters and MT, respectively, without affecting APC cluster formation itself. These results show that localization of APC in cortical clusters is different from that of EB1 at MT plus ends and appears to be independent of EB1.

Conformational studies on cyclic tetrapeptides: Hydrophobic cluster formation

Peptides 1994 ◽  
1995 ◽  
pp. 521-522
Author(s):  
R. K. Konat ◽  
S. Golic Grdadolnik ◽  
W. Schmitt ◽  
H. Kessler
Keyword(s):  
Cluster Formation ◽  
Conformational Studies ◽  
Hydrophobic Cluster ◽  
Cyclic Tetrapeptides

Bismuth(iii) complexes derived from α-amino acids: the impact of hydrolysis and oxido-cluster formation on their activity against Helicobacter pylori

2014 ◽  
Vol 43 (48) ◽  
pp. 17980-17990 ◽  
Author(s):  
Madleen Busse ◽  
Emily Border ◽  
Peter C. Junk ◽  
Richard L. Ferrero ◽  
Philip C. Andrews
Keyword(s):  
Amino Acids ◽  
Helicobacter Pylori ◽  
Cluster Formation ◽  
H Pylori ◽  
The Impact

Bi(iii) complexes, [BiL3] and [Bi2L3], derived from α-amino acids (LH) have been synthesised and characterised. Hydrolysis and oxido-cluster formation in water impacts significantly on their activity towardsH. pylori.

Amino acids stimulate phosphorylation of p70 S6k and organization of rat adipocytes into multicellular clusters

1998 ◽  
Vol 274 (1) ◽  
pp. C206-C213 ◽  
Author(s):  
Heather L. Fox ◽  
Scot R. Kimball ◽  
Leonard S. Jefferson ◽  
Christopher J. Lynch
Keyword(s):  
Amino Acids ◽  
Primary Culture ◽  
Signaling Pathway ◽  
Culture Medium ◽  
Cluster Formation ◽  
S6 Kinase ◽  
Rat Adipocytes ◽  
Ribosomal Protein S6 ◽  
P70 S6k ◽  
Fasted Rats

In previous studies we have shown that rat adipocytes suspended in Matrigel and placed in primary culture migrate through the gel to form multicellular clusters over a 5- to 6-day period. In the present study, phosphorylation of the insulin-regulated 70-kDa ribosomal protein S6 kinase (p70 S6k ) was observed within 30 min of establishment of adipocytes in primary culture. Two inhibitors of the p70 S6k signaling pathway, rapamycin and LY-294002, greatly reduced phosphorylation of p70 S6k and organization of adipocytes into multicellular clusters. Of all the components of the cell culture medium, amino acids, and in particular a subset of neutral amino acids, were found to promote both phosphorylation of p70 S6k and cluster formation. Lowering the concentrations of amino acids in the medium to levels approximating those in plasma of fasted rats decreased both phosphorylation of p70 S6k and cluster formation. Furthermore, stimulation of p70 S6k phosphorylation by amino acids was prevented by either rapamycin or LY-294002. These findings demonstrate that amino acids stimulate the p70 S6k signaling pathway in adipocytes and imply a role for this pathway in multicellular clustering.

scholarly journals A Method to Predict Amino Acids at Proximity of Beta-Sheet Axes from Protein Sequences

2014 ◽  
Vol 05 (01) ◽  
pp. 79-89 ◽  
Author(s):  
Antonin Guilloux ◽  
Bernard Caudron ◽  
Jean-Luc Jestin
Keyword(s):  
Amino Acids ◽  
Protein Sequences ◽  
Beta Sheet

Quantum-Chemical Analysis of Thermodynamics of Two-Dimensional Cluster Formation of α-Amino Acids at the Air/Water Interface

2009 ◽  
Vol 113 (52) ◽  
pp. 16557-16567 ◽  
Author(s):  
Yu. B. Vysotsky ◽  
E. S. Fomina ◽  
E. A. Belyaeva ◽  
E. V. Aksenenko ◽  
D. Vollhardt ◽  
...  
Keyword(s):  
Amino Acids ◽  
Chemical Analysis ◽  
Quantum Chemical ◽  
Cluster Formation ◽  
Water Interface ◽  
Two Dimensional ◽  
Quantum Chemical Analysis ◽  
Air Water Interface

A Thermodynamic Scale for the .beta.-Sheet Forming Tendencies of the Amino Acids

Biochemistry ◽  
1994 ◽  
Vol 33 (18) ◽  
pp. 5510-5517 ◽  
Author(s):  
Catherine K. Smith ◽  
Jane M. Withka ◽  
Lynne Regan
Keyword(s):  
Amino Acids ◽  
Sheet Forming ◽  
Beta Sheet ◽  
Thermodynamic Scale
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