Basic carboxypeptidases: regulators of peptide hormone activity.
about
Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidaseCarboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiationSequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domainsEnzymic characterization of a novel member of the regulatory B-like carboxypeptidase with transcriptional repression function: stimulation of enzymic activity by its target DNAIdentification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulationPlasma carboxypeptidases as regulators of the plasminogen systemThree-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivityHigh concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cellsActivated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone proteinExtracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase MRecent developments in inhibiting cysteine and serine proteases.Rational design of matrix metalloproteinase-13 activatable probes for enhanced specificity.Analytical Prediction of the Spatiotemporal Distribution of Chemoattractants around Their Source: Theory and Application to Complement-Mediated Chemotaxis.Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues.Prologue: kinins and related systems. New life for old discoveries.Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis.Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.Bradykinin metabolism and hypotensive transfusion reactions.gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family.Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D.Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase).Carboxypeptidase B and other kininases of the rat coronary and mesenteric arterial bed perfusates.Kinin-stimulated B1 receptor signaling depends on receptor endocytosis whereas B2 receptor signaling does not.Characterization of dual agonists for kinin B1 and B2 receptors and their biased activation of B2 receptorsA structural and functional analysis of Nna1 in Purkinje cell degeneration (pcd) mice.Kinin- and angiotensin-converting enzyme (ACE) inhibitor-mediated nitric oxide production in endothelial cells.New aspects of melanocortin signaling: a role for PRCP in α-MSH degradationDyslipidemia in obesity: mechanisms and potential targetsStructure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivatorCarboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor.Probing of C-terminal lysine variation in a recombinant monoclonal antibody production using Chinese hamster ovary cells with chemically defined media.Interaction of angiotensin-converting enzyme (ACE) with membrane-bound carboxypeptidase M (CPM) - a new function of ACE.Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient b1 signaling from B2 agonists.1993 Mack Forster Award Lecture. Review. The endothelium as a target and mediator of cardiovascular disease.Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process.The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing.Carboxypeptidase M as a marker of macrophage maturation.Cellular carboxypeptidases.Plasmin alters the activity and quaternary structure of human plasma carboxypeptidase N.Carboxypeptidases: new regulators of plasminogen activation in vivo?
P2860
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P2860
Basic carboxypeptidases: regulators of peptide hormone activity.
description
1988 nî lūn-bûn
@nan
1988 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Basic carboxypeptidases: regulators of peptide hormone activity.
@ast
Basic carboxypeptidases: regulators of peptide hormone activity.
@en
Basic carboxypeptidases: regulators of peptide hormone activity.
@nl
type
label
Basic carboxypeptidases: regulators of peptide hormone activity.
@ast
Basic carboxypeptidases: regulators of peptide hormone activity.
@en
Basic carboxypeptidases: regulators of peptide hormone activity.
@nl
prefLabel
Basic carboxypeptidases: regulators of peptide hormone activity.
@ast
Basic carboxypeptidases: regulators of peptide hormone activity.
@en
Basic carboxypeptidases: regulators of peptide hormone activity.
@nl
P1476
Basic carboxypeptidases: regulators of peptide hormone activity.
@en
P2093
Skidgel RA
P304
P356
10.1016/0165-6147(88)90015-6
P577
1988-08-01T00:00:00Z