Results 1 to 10 of about 4,257 (183)

It Takes Two to Tango: Current Understanding of the Role of M16 Family of Proteases and Their Structural Properties [PDF]

open access: yesBiomolecules
The M16 protease family comprises metalloendopeptidases, characterized by a unique molecular architecture. The active enzyme molecule is composed of two halves, which together form a structure resembling a clam shell.
Miroslaw Jarzab, Joanna Skorko-Glonek
doaj   +2 more sources

Production and application of peptidyl-lys metalloendopeptidase: advances, challenges, and future perspectives [PDF]

open access: yesApplied Microbiology and Biotechnology
Peptidyl-lys metalloendopeptidases (PKMs) are enzymes that selectively cleave peptide bonds at the N-terminus of lysine residues present in the P1′ position, making them valuable tools in proteomics.
Uzair Ahmed   +2 more
doaj   +2 more sources

The astacin family of metalloendopeptidases [PDF]

open access: yesProtein Science, 1995
AbstractThe astacin family of metalloendopeptidases was recognized as a novel family of proteases in the 1990s. The crayfish enzyme astacin was the first characterized and is one of the smallest members of the family. More than 20 members of the family have now been identified.
Robert J. Beynon
exaly   +3 more sources

Families of metalloendopeptidases and their relationships [PDF]

open access: yesFEBS Letters, 1992
Crystal structures available for four metalloendopeptidases have revealed zinc ligands for these enzymes. New sequence information has made it possible to compare the primary structures of the zinc‐binding site in metalloendopeptidases. A scheme based on the zinc‐binding site is proposed to classify metalloendopeptidases into five distinct families ...
Jiang, Weiping, Bond, Judith S.
exaly   +3 more sources

The ADAMTS family: from extracellular matrix proteases to orchestrators of fibrosis [PDF]

open access: yesCell Communication and Signaling
Fibrosis, a pathological process defined by excessive extracellular matrix (ECM) accumulation, contributes significantly to chronic organ failure worldwide.
Yang Yuan   +4 more
doaj   +2 more sources

Soluble Metalloendopeptidases and Neuroendocrine Signaling [PDF]

open access: yesEndocrine Reviews, 2002
Peptidases play a vital and often highly specific role in the physiological and pathological generation and termination of peptide hormone signals. The thermolysin-like family of metalloendopeptidases involved in the extracellular processing of neuroendocrine and cardiovascular peptides are of particular significance, reflecting both their specificity ...
Corie N, Shrimpton   +2 more
exaly   +3 more sources

Homologues of insulinase, a new superfamily of metalloendopeptidases [PDF]

open access: yesBiochemical Journal, 1991
On the basis of a statistical analysis of an alignment of the amino acid sequences, a new superfamily of metalloendopeptidases is proposed, consisting of human insulinase, Escherichia coli protease III and mitochondrial processing endopeptidases from Saccharomyces and Neurospora.
Neil David Rawlings, Alan J. Barrett
exaly   +3 more sources

Extracellular matrix turnover in salivary gland disorders and regenerative therapies: Obstacles and opportunities

open access: yesJournal of Oral Biology and Craniofacial Research, 2023
Salivary gland (SG) extracellular matrix (ECM) has a major influence on tissue development, homeostasis, and tissue regeneration after injury. During aging, disease, and physical insult, normal remodeling of the SG microenvironment (i.e.
Milos Marinkovic   +6 more
doaj   +1 more source

gone early, a novel germline factor, ensures the proper size of the stem cell precursor pool in the Drosophila ovary. [PDF]

open access: yesPLoS ONE, 2014
In order to sustain lifelong production of gametes, many animals have evolved a stem cell-based gametogenic program. In the Drosophila ovary, germline stem cells (GSCs) arise from a pool of primordial germ cells (PGCs) that remain undifferentiated even ...
Shinya Matsuoka   +4 more
doaj   +1 more source

Specific fluorogenic substrates for neprilysin (neutral endopeptidase, EC 3.4.24.11) which are highly resistant to serine- and metalloproteases [PDF]

open access: yes, 1997
Two intramolecularly quenched fluorogenic peptides containing o-aminobenzoyl (Abz) and ethylenediamine 2,4-dinitrophenyl (EDDnp) groups at amino- and carboxyl-terminal amino acid residues, Abz-DArg-Arg-Leu-EDDnp (Abz-DRRL-EDDnp) and Abz-DArg-Arg-Phe ...
Boileau, G.   +4 more
core   +4 more sources

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