Results 191 to 200 of about 4,824 (245)

Myeloid transglutaminase 2 regulates Treg-Th17 balance in a female model of angiotensin II-induced hypertension and vascular stiffening. [PDF]

Am J Physiol Heart Circ Physiol
Naz H, Teixeiro E, Manrique-Acevedo C, Lastra G.   +3 more
europepmc   +1 more source

Factor XIII: driving (cross-)links in hemostasis, thrombosis, and disease.

Blood
Luyendyk JP, Flick MJ, Wolberg AS.
europepmc   +1 more source

Plant Transglutaminases

Phytochemistry, 1995
The identification procedures, the characteristics and the potential function of the recently detected plant transglutaminases, are discussed in the light of the knowledge of animal transglutaminases. The enzyme has been studied occasionally in lower organisms (bacteria, fungi and green algae) and more extensively in Angiosperms.
Simone Beninati, Stefano Del Duca, D Serafini-Fracassini   +2 more
exaly   +5 more sources

Transglutaminases and Receptor Tyrosine Kinases [PDF]

Amino Acids, 2013
Transglutaminases are confounding enzymes which are known to play key roles in various cellular processes. In this paper, we aim to bring together several pieces of evidence from published research and literature that suggest a potentially vital role for
Tristan I. Croll, Zee Upton, Manaswini Sivaramakrishnan   +2 more
exaly   +2 more sources

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Transglutaminases in Disease

Neurochemistry International, 2002
Transglutaminases (TGases) are enzymes that are widely used in many biological systems for generic tissue stabilization purposes. Mutations resulting in lost activity underlie several serious disorders. In addition, new evidence documents that they may also be aberrantly activated in tissues and cells and contribute to a variety of diseases, including ...
Soo-Youl Kim, Thomas M Jeitner, Peter M Steinert   +2 more
exaly   +3 more sources

Transglutaminases

Annual Review of Biochemistry, 1980
J E Folk
exaly   +3 more sources

Dark-Induced Senescence of Barley Leaves Involves Activation of Plastid Transglutaminases [PDF]

Amino Acids, 2015
Transglutaminases (E.C. 2.3.2.13) catalyze the post-translational modification of proteins by establishing ε-(γ-glutamyl) lysine isopeptide bonds and by the covalent conjugation of polyamines to endo-glutamyl residues of proteins.
Małgorzata Pietrowska-Borek, Magdalena Luczak, Stefano Del Duca   +2 more
exaly   +2 more sources

Plant and Animal Transglutaminases: Do Similar Functions Imply Similar Structures?

Amino Acids, 2009
In plants the post-translational modification of proteins by polyamines catalysed by transglutaminases has been studied since ’87: it was identified by the production of glutamyl-polyamine derivatives, biochemical features, recognition by animal ...
Stefano Del Duca, Rita Casadio, Donatella Serafini-Fracassini   +2 more
exaly   +2 more sources

Transglutaminases

Molecular and Cellular Biochemistry, 1984
This paper is intended as a background to the topic of transglutaminases, while focusing on current ideas regarding the biological roles of these enzymes. Specifically, the following topics are discussed: geometry of forming gamma-glutamyl-epsilon-lysine cross-linked structures; energetic considerations; the gamma-glutamyl-epsilon-lysine cross-link ...
L, Lorand, S M, Conrad
openaire   +2 more sources

Chromogranins as substrate for transglutaminase

Biochemical Pharmacology, 1971
Abstract The possible attachment of amines to proteins obtained from adrenal medulla was investigated using transglutaminase as the enzyme. Transglutaminase catalyzes a replacement of the amide group of certain protein-bound glutamine residues by primary amines.
I J, Wajda, I, Hanbauer, I, Manigault, A, Lajtha   +3 more
openaire   +2 more sources