Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the…

By W. Bode, F. Gomis‐Rüth, Walter Stöckler. 1993

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Citations in the corpus

A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “Currently, 37 ADAMs have been identified in rats, 34 ADAMs have been discovered in mice, and 22 ADAMs have been found in the human genome, among which 13 proteins are proteolytically active [13].”
Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold (2006, background): “…2004), with a flat ellipsoidal shape having a central core made up of five stranded b-sheets and five a-helices and a conserved methionine (Met-turn) below the active site histidine residues, which bears the typical structural feature of metzincin family of metallopro- teinases (Bode et al, 1993).”
Progress in matrix metalloproteinase research. (2008, background): “Thus, they are typical metzincin members (Bode et al., 1993), but what distinguishes MMPs from other metzincins are the primary structures of the catalytic domains.”
Structure and function of matrix metalloproteinases and TIMPs. (2006, unknown): “A (pappalysins, PAPP-A), and they are collectively called ‘‘metzincins’’ [21].”
Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease. (2018, unknown): “1) (Bode et al., 1993; Bode et al., 1999; Visse and Nagase, 2003).”
Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases (2001, background): “The members of the ADAM family belong to the metzincin superfamily (19, 20).”
A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions (2016, background): “Those mammalian ADAMs that are catalytically active use a cysteine-switch mechanism to maintain enzyme latency [11].”
Control of matrix metalloproteinase catalytic activity. (2007, background): “The metzincin subfamily of metalloproteases are characterized by 3-histidine zinc-binding motif and a conserved methionine turn following the active site (Bode et al., 1993).”
The ADAM metalloproteinases (2008, background): “…human ADAMs, 13 encode proteins that possess the characteristic reprolysin-type active site (HEXGHXXGXXHD) in the metalloproteinase domain followed downstream by the ‘‘Met turn” that is the signature of the Metzincin enzymes (Bode et al., 1993), indicating functional proteolytic capability.”
Physiology and pathophysiology of matrix metalloproteases (2010, background): “…by three histidine residues in the zinc-binding consensus sequence HExxHxxGxxH that is present in all proteolytically active metzincins, and a characteristic, strictly conserved methionine-containing tight 1,4 beta turn forming a hydrophobic cleft for the catalytic zinc ion (Bode et al. 1993).”