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THE AMINO ACID SEQUENCE OF HYPERTENSIN II [PDF]

open access: yesJournal of Experimental Medicine, 1956
The amino acid sequence of horse hypertensin II has been determined by the use of chymotrypsin, the fluorodinitrobenzene method, and stepwise phenylisothiocyanate degradation. The results indicate that the amino acids of hypertensin II are arranged in the following order: asp-arg-val-tyr-iso-hist-pro-phe.
L T Skeggs   +2 more
exaly   +3 more sources

The amino acid sequence of Scenedesmus ferredoxin

open access: yesBiochemical and Biophysical Research Communications, 1968
The complete amino acid sequence of ferredoxin isolated from a green alga, Scenedesmus species, was determined by analyses of tryptic and chymotryptic digests, and cyanogen bromide cleavage of the S-carboxymethylcysteinylferredoxin. The total number of amino acid residues is 96, one less than for the higher plant ferredoxins.
K, Sugeno, H, Matsubara
openaire   +3 more sources

The amino acid sequence of human glucagon [PDF]

open access: yesFEBS Letters, 1972
The amino acid sequence of bovine glucagon has been found to be the same as that reported for porcine glucagon [ 1,2] . Human glucagon has been isolated and crystallized [3] . The crystal form and the amino acid composition of human glucagon proved to be identical with those of porcine and bovine glucagon.
Thomsen, J.   +3 more
openaire   +2 more sources

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

open access: yesFEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes   +4 more
wiley   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

open access: yesFEBS Letters, EarlyView.
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy   +4 more
wiley   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

Phosphoinositides and inositol phosphates as molecular glues

open access: yesFEBS Letters, EarlyView.
Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry   +9 more
wiley   +1 more source

Structural insights and therapeutic targets in Acinetobacter baumannii capsule biosynthesis

open access: yesFEBS Letters, EarlyView.
Hypervirulent KL49 A. baumannii's capsular polysaccharide contains the nonulosonic acid 8‐epi‐Leg5,7Ac2, synthesized by epimerization via ElaA, ElaB, and ElaC. Crystal structures of ElaA, ElaB, and ElaC reveal their role in CMP‐Leg5,7Ac2 synthesis and regioselective C8 epimerization.
Woo Cheol Lee   +7 more
wiley   +1 more source

The amino acid sequence of peanut agglutinin [PDF]

open access: yesEuropean Journal of Biochemistry, 1991
The amino acid sequence of peanut (Arachis hypogaea) agglutinin was determined from three major fragments obtained by mild acid cleavage at Asp‐Pro peptide bonds. The sequence of 236 amino acids has residues identical to those that form the metal‐binding site and the hydrophobic pocket in concanavlin A and other lectins, although the overall similarity
Young, N., Johnston, R., Watson, David
openaire   +3 more sources

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

open access: yesFEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

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