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	Pfam 20.0 : Serpin (Site not responding. Last check: 2007-10-22)
		Serpins (SERine Proteinase INhibitors) PUBMED:14705960, PUBMED:2690952, PUBMED:8417965 belong to MEROPS inhibitor family I4, clan ID. Serpins are proteins that are primarily known as irreversible serine protease inhibitors active against S1 (), S8 () and C14 () peptidases.
		Serpins and their homologues are a group of high molecular weight (40 to 50 kDa) structurally related proteins involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation, tumour suppression and hormone transport.
		In contrast to "rigid" proteinase inhibitors, such as those of the Kunitz or Kazal families, the serpins are metastable proteins (active-state proteins) which interact with their substrate and irreversibly trap the acyl intermediate as a result of a major conformational change PUBMED:11116079; they are best described as suicide substrate inhibitors.
	pfam.wustl.edu /cgi-bin/getdesc?name=Serpin (382 words)

	Keeping the Serpin Machine Running Smoothly -- Gettins 10 (12): 1833 -- Genome Research
		PI as the serpin and trypsin as the proteinase.
		Serpin and proteinase bind to form an initial noncovalent Michaelis-like complex (EI) in which the proteinase docks with the exposed reactive center loop (red) with no distortion of the proteinase or the body of the serpin (Peterson et al.
		The phylogenetic analysis of serpin sequences by Irving and colleagues (Irving et al.
	www.genome.org /cgi/content/full/10/12/1833 (2131 words)

	CIMR Serpin Abstracts
		Tryptase cleavage of several large proteins argues against size exclusion of SERPINs from the tetrameric core of tryptase as the sole explanation for resistance to inhibition and suggests that the resistance of tryptase to SERPINs may be related to the lack of specificity displayed by tryptase.
		Serpins form stable complexes of 1:1 stoichiometry with their target proteinases by reaction of their P1-P1' peptide bond with the proteinase active site, resulting in formation of an ester bond between the active site serine of the proteinase and the P1 residue of the serpin [1].
		We are studying the folding and stability of maspin in an effort to understand the relationship between its structure and function, to investigate the possibility of alternative conformations in maspin and their role in function, and as background for the possible design of improved maspin molecules for therapeutic purposes.
	www-structmed.cimr.cam.ac.uk /Serpins/abstracts.html (20687 words)

	Anti-Serpin antibodies from RDI Divison of Fitzgerald Industries Intl
		Description: Members of the human serpin family regulate a diverse array of serine and cysteine proteinases associated with essential biological processes such as fibrinolysis, coagulation, inflammation, cell mobility, cellular differentiation, and apoptosis.
		Differential display was used to identify a novel serpin (headpin or SERPINB13) that is underexpressed in squamous cell cancers of the oral cavity.
		A novel serpin gene, SERPINB10, is highly expressed in human bone marrow cells and plays a role in the regulation of protease activities during hematopoiesis.
	www.researchd.com /miscabs/serpin.htm (524 words)

	Purification, cDNA Cloning, and Characterization of a New Serpin with Megakaryocyte Maturation Activity -- Tsujimoto et ...
		consensus sequence of the serpin superfamily is underlined.
		The primary function of members of the serpin family is considered to neutralize overexpressed serine protease activity (26).
		was shown to be a serpin with neurotropic activity (29).
	www.jbc.org /cgi/content/full/272/24/15373 (4879 words)

	Distribution of the Human Intracellular Serpin Protease Inhibitor 8 in Human Tissues -- Strik et al. 50 (11): 1443 -- ...
		Potempa J, Korzus E, Travis J (1994) The serpin superfamily of proteinase inhibitors: structure, function, and regulation.
		Riewald M, Schleef RR (1995) Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow.
		Scott FL, Hirst CE, Sun J, Bird CH, Bottomley SP, Bird PI (1999) The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. Blood 93:2089-2097
	www.jhc.org /cgi/content/full/50/11/1443 (4685 words)

	The ovalbumin serpins revisited: Perspective from the chicken genome of clade B serpin evolution in vertebrates -- ...
		The ovalbumin serpins revisited: Perspective from the chicken genome of clade B serpin evolution in vertebrates -- Benarafa and Remold-O'Donnell 102 (32): 11367 -- Proceedings of the National Academy of Sciences
		The serpin cluster is flanked downstream by the Werner helicase-interacting protein (WHIP) and upstream by the vacuolar sorting protein 4b (VPS4B), follicular lymphoma variant translocation 1 (FVT1), and B cell leukemia/lymphoma 2 (BCL2).
		Serpin genes and their orientation are represented by blue (seven-exon genes) or orange (eight-exon genes) block arrows.
	www.pnas.org /cgi/content/full/102/32/11367 (4234 words)

	Serpin 2a Is Induced in Activated Macrophages and Conjugates to a Ubiquitin Homolog -- Hamerman et al. 168 (5): 2415 -- ...
		Serpin 2a Is Induced in Activated Macrophages and Conjugates to a Ubiquitin Homolog -- Hamerman et al.
		Serpin 2a Is Induced in Activated Macrophages and Conjugates to a Ubiquitin Homolog
		The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. Blood 93:2089.
	www.jimmunol.org /cgi/content/full/168/5/2415 (6887 words)

	DAYBREAK - Role of a 'Serpin' in Alzheimer's Revealed
		Researchers have discovered that a protein -- known as a serpin -- can double the accumulation of Alzheimer’s disease-associated amyloid plaque in the brains of mice, suggesting a possible new target for therapy in humans.
		The study led by investigators at the Gladstone Institute of Neurological Disease and UCSF is reported in the December issue of The American Journal of Pathology.
		Alpha1-antichymotrypsin (ACT) is a serin protease inhibitor, or serpin, that normally prevents enzymes known as proteases from digesting proteins.
	www.ucsf.edu /daybreak/2000/12/07_serpin.htm (481 words)

	Manduca sexta Serpin-6 Regulates Immune Serine Proteinases PAP-3 and HP8: cDNA CLONING, PROTEIN EXPRESSION, INHIBITION ...
		by serine proteinase cascades and regulated by serpins in hemolymph.
		30 and 15 serpin genes in the Drosophila melanogaster and Anopheles
		inhibitors of the serpin superfamily (15, 40, 41).
	www.jbc.org /cgi/content/full/280/14/14341 (4352 words)

	Modeling the three-dimensional structure of serpin/molecular chaperone HSP47
		There are at least 30 serpin proteins, including HSP47, which have been identified on the basis of their primary amino acid sequences (12, 13) and where X-ray crystal structure information is to hand the three dimensional structures are surprisingly consistent (13, 14).
		However, the amino acid sequence identity of mrmHSP47 was found to be 30 % (Figure 1) with the serpin human protein C inhibitor (hPCI), therefore the structure of mouse HSP47 was modeled using the X-ray crystal structure coordinates of hPCI in preference.
		As a result, the conformation of the serpin loop (red strand, Figure 2c) in the model is very similar to the conformation displayed in the X-ray crystal structure of latent PAI-1 (18).
	www.ch.ic.ac.uk /ectoc/papers/miller (3509 words)

	Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function -- ...
		Inhibitory serpins can generally be recognized by a consensus pattern in their sequences in the hinge (Hopkins et al.
		The tree is a combination of the majority consensus maximum parsimony trees seen in Figure 4, with groups of serpins of similar type (e.g., antithrombin) represented by a single identifier, where possible.
		With the exception of the viral serpins, all known serpins appear in organisms of the eukaryote crown group taxon.
	www.genome.org /cgi/content/full/GR-1478Rv1 (6086 words)

	Nucleocytoplasmic Distribution of the Ovalbumin Serpin PI-9 Requires a Nonconventional Nuclear Import Pathway and the ...
		Proteinase inhibitor 9 (PI-9) is a human serpin present in the cytoplasm of cytotoxic lymphocytes and epithelial cells.
		A mesangium-predominant gene, megsin, is a new serpin upregulated in IgA nephropathy.
		Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase.
	mcb.asm.org /cgi/content/full/21/16/5396 (7901 words)

	Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and ...
		A of the serpin occurs and that the proteinase consequently moves
		of the serpin moiety in the noncovalent complex.
		The ovalbumin serpins revisited: Perspective from the chicken genome of clade B serpin evolution in vertebrates
	www.pnas.org /cgi/content/full/96/9/4808 (5009 words)

	Georgia Plant Conservation Alliance \| SERPIN (Site not responding. Last check: 2007-10-22)
		Created by a partnership of institutions in the region, SERPIN aims to make large and small museum and library collections more easily available to researchers, teachers, students, land managers, and the public in the Southeast and worldwide.
		SERPIN is meant to be more than a roadmap to existing Internet resources.
		Initial funding for SERPIN was provided by the Institute of Museum and Library Services and the University of Georgia.
	www.uga.edu /~gpca/serpin.html (274 words)

	Serpins 2005 - fun between the {beta}-sheets: Meeting report based upon presentations made at the 4th International ... (Site not responding. Last check: 2007-10-22)
		Serpins 2005 - fun between the {beta}-sheets: Meeting report based upon presentations made at the 4th International Symposium on Serpin Structure, Function and Biology (Cairns, Australia) -- Whisstock et al.
		The RCL is highlighted in magenta at the top of the molecule, the body of the serpin is in green and the protease is in cyan.
		Zhou A, Stein PE, Huntington JA and Carrell RW (2003) Serpin polymerization is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycerol.
	content.febsjournal.org /cgi/content/full/272/19/4868 (2780 words)

	The necrotic Gene in Drosophila Corresponds to One of a Cluster of Three Serpin Transcripts Mapping at 43A1.2 -- Green ...
		The necrotic Gene in Drosophila Corresponds to One of a Cluster of Three Serpin Transcripts Mapping at 43A1.2 -- Green et al.
		melanogaster serpins SP1, 2, and 6 (EMBL AJ251744, 251745, and 251749).
		serpins in imaginal discs are hard to interpret given that the
	www.genetics.org /cgi/content/full/156/3/1117 (4699 words)

	Formation of a large, complex domain of histone hyperacetylation at human 14q32.1 requires the serpin locus control ...
		DHSs in the proximal serpin subcluster was formed (19).
		Histone hyperacetylation in the proximal serpin subcluster was
		The identification of the proximal serpin subcluster as a discrete
	nar.oxfordjournals.org /cgi/content/full/33/10/3313 (5227 words)

	Suppressors of a Host Range Mutation in the Rabbitpox Virus Serpin SPI-1 Map to Proteins Essential for Viral DNA ... (Site not responding. Last check: 2007-10-22)
		SPI-1 T309R serpin is inactive as a protease inhibitor in vitro.
		CrmA, a poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis.
		The cowpox virus serpin SPI-3 complexes with and inhibits urokinase-type and tissue-type plasminogen activators and plasmin.
	jvi.asm.org /cgi/content/full/79/14/9168 (8336 words)

	A Mesangium-predominant Gene, Megsin, Is a New Serpin Upregulated in IgA Nephropathy -- Miyata et al. 102 (4): 828 -- ...
		A Mesangium-predominant Gene, Megsin, Is a New Serpin Upregulated in IgA Nephropathy -- Miyata et al.
		In conclusion, megsin is a new serpin protein expressed predominantly in mesangial cells.
		Cataltepe, N.M. Schechter, P.A. Pemberton, and G.A. Silverman (1997) Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chyotrypsin-like proteases cathepsin G and mast cell chymase.
	www.jci.org /cgi/content/full/102/4/828 (4292 words)

	Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast cells and forms complexes with ...
		The serpins are an expanding superfamily of structurally similar but functionally diverse proteins: evolution, mechanism of inhibition, novel functions, and a revised nomenclature.
		Circulating serpin tumor markers SCCA1 and SCCA2 are not actively secreted but reside in the cytosol of squamous carcinoma cells.
		The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. Blood.
	www.bloodjournal.org /cgi/content/full/103/7/2710 (4656 words)

	Serpin Alignments
		A new family of ten murine ovalbumin serpins includes two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor (proteinase inhibitor 9).
		A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II.
		Molecular cloning and expression of an intracellular serpin: an elastase inhibitor from horse leucocytes.
	www-structmed.cimr.cam.ac.uk /Serpins/serp_seq.html (4563 words)

	Role of the P6-P3' Region of the Serpin Reactive Loop in the Formation and Breakdown of the Inhibitory Complex
		Serpins have a large external peptide loop known as the reactive loop.
		A series of ACT-PI chimeras were constructed in which segments of increasing length taken from the P6-P3' region of PI replaced the corresponding residues of ACT.
		These results indicate that residues in the reactive loop region predicted to contact a specific target protease cannot fully transfer inhibitory activity from one serpin to another, suggesting that specific reactive loop-serpin body and serpin body-protease body interactions play a significant role in determining serpin inhibitory activity against target proteases.
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/1997/36/i47/abs/bi971530j.html (448 words)

	Identification and characterization of nuclear matrix-attachment regions in the human serpin gene cluster at 14q32.1 -- ...
		Identification and characterization of nuclear matrix-attachment regions in the human serpin gene cluster at 14q32.1 -- Rollini et al.
		Identification and characterization of nuclear matrix-attachment regions in the human serpin gene cluster at 14q32.1
		serpin locus were integrated randomly into the rat genome.
	nar.oxfordjournals.org /cgi/content/full/27/19/3779 (7402 words)

	A Novel Serpin Expressed by Blood-Borne Microfilariae of the Parasitic Nematode Brugia malayi Inhibits Human Neutrophil ...
		Most serpin family members so-far characterized are from mammals, insects, and viruses.
		The serpin signature of FRANHPFLYAI (aa 377-387, Fig 1A) corresponds well to that, for example, of chicken gene Y, FRADHPFLFFI.
		The serpin superfamily has been constructed on the basis of sequence similarities at the protein level.
	www.bloodjournal.org /cgi/content/full/94/4/1418 (6463 words)

	Inhibition of apoptosis in human tumour cells by the tumour-associated serpin, SCC antigen-1 (Site not responding. Last check: 2007-10-22)
		The squamous cell carcinoma antigen (SCC Ag) is a tumour-associated protein and a member of theserineproteaseinhibitor (serpin) family.
		The SCC Ag has been used as a serologic tumour marker for SCC progression, and its elevated serum levels are a risk factor for disease relapse.
		Thus, overexpression of the SCC Ag-1, a member of the serpin family, in human cancer cells contributed to their survival by mediating protection from drug-, cytokine- or effector cell-induced apoptosis.
	www.nature.com /bjc/journal/v82/n4/abs/6691028a.html (278 words)

	Hormone binding globulins undergo serpin conformational change in inflammation (Site not responding. Last check: 2007-10-22)
		Apparently evol-ution has completely adapted the serpin structure for its new role in these proteins as a transport agent, as there is no evidence of any retained protease inhibitory activity.
		To function as inhibitors the serpins have a native stressed (S) conformation that makes them vulnerable to proteolytic cleavage, the cleavage being accompanied by an irreversible transition to a stable relaxed (R) form
		We demon-strate here that TBG and CBG have retained the stressed native structure typical of the inhibitor members of the family and we provide evidence that the S−R transition has been adapted to allow altered hormone delivery at inflammatory sites.
	www.nature.com /nature/journal/v336/n6196/abs/336257a0.html;jsessionid=06F8E51699DFD15ABF65CEFE24EE153D (297 words)

	Maspin Is an Intracellular Serpin That Partitions into Secretory Vesicles and Is Present at the Cell Surface -- ...
		Maspin Is an Intracellular Serpin That Partitions into Secretory Vesicles and Is Present at the Cell Surface -- Pemberton et al.
		Pemberton PA (1997) The role of serpin superfamily members in cancer.
		Evidence that maspin is not a protease inhibitory serpin.
	www.jhc.org /cgi/content/full/45/12/1697 (4794 words)

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