Multifunctional aspartic peptidase prosegments.

[1]  R. Yada,et al.  The prosegment catalyzes pepsin folding to a kinetically trapped native state. , 2010, Biochemistry.

[2]  A. Wlodawer,et al.  Crystal structures of the histo-aspartic protease (HAP) from Plasmodium falciparum. , 2009, Journal of molecular biology.

[3]  F. Ahmad,et al.  The denaturation of covalently inhibited swine pepsin. , 2009, International journal of peptide and protein research.

[4]  Martin Fusek,et al.  Cathepsin D--many functions of one aspartic protease. , 2008, Critical reviews in oncology/hematology.

[5]  Y. Kiso,et al.  Design of Potent Aspartic Protease Inhibitors to Treat Various Diseases , 2008, Archiv der Pharmazie.

[6]  H. Kalbacher,et al.  Cathepsin E: a mini review. , 2008, Biochemical and biophysical research communications.

[7]  M. Ogawa,et al.  Expression and enzymatic characterization of the soluble recombinant plasmepsin I from Plasmodium falciparum. , 2007, Protein engineering, design & selection : PEDS.

[8]  B. Winblad,et al.  The Alzheimer's disease-associated γ-secretase complex: Functional domains in the presenilin 1 protein , 2007, Physiology & Behavior.

[9]  S. Krueger,et al.  Comparison of solution structures and stabilities of native, partially unfolded and partially refolded pepsin. , 2006, Biochemistry.

[10]  Peng Liu,et al.  Inhibitor binding to the plasmepsin IV aspartic protease from Plasmodium falciparum. , 2006, Biochemistry.

[11]  M. Ogawa,et al.  Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum. , 2006, Protein expression and purification.

[12]  J. Kelly,et al.  Structural biology: Proteins downhill all the way , 2006, Nature.

[13]  B. B. Scott,et al.  Development of inhibitors of the aspartyl protease renin for the treatment of hypertension. , 2006, Current protein & peptide science.

[14]  Tooru Kimura,et al.  Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor. , 2006, Acta crystallographica. Section D, Biological crystallography.

[15]  A. J. Padilla-Zúñiga,et al.  Loosely packed papain prosegment displays inhibitory activity. , 2006, Archives of biochemistry and biophysics.

[16]  Sungga Lee,et al.  Prodomain processing of recombinant plasmepsin II and IV, the aspartic proteases of Plasmodium falciparum, is auto- and trans-catalytic. , 2006, Journal of biochemistry.

[17]  E. Sakai,et al.  Characterization of rat cathepsin E and mutants with changed active‐site residues and lacking propeptides and N‐glycosylation, expressed in human embryonic kidney 293T cells , 2006, The FEBS journal.

[18]  Kenji Yamamoto,et al.  The role of the cathepsin E propeptide in correct folding, maturation and sorting to the endosome. , 2005, Journal of biochemistry.

[19]  D. Goldberg,et al.  Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum. , 2005, Molecular and biochemical parasitology.

[20]  L. Prade,et al.  X-ray Structure of Plasmepsin II Complexed with a Potent Achiral Inhibitor* , 2005, Journal of Biological Chemistry.

[21]  K. Dill,et al.  Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases. , 2005, Journal of molecular biology.

[22]  J. Clemente,et al.  Crystallization and preliminary X-ray analysis of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae. , 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

[23]  K. Marsh,et al.  Clinical features and pathogenesis of severe malaria. , 2004, Trends in parasitology.

[24]  B. de Strooper,et al.  BACE1 and Presenilin: Two Unusual Aspartyl Proteases Involved in Alzheimer’s Disease , 2004, Neurodegenerative Diseases.

[25]  I. Simões,et al.  Structure and function of plant aspartic proteinases. , 2004, European journal of biochemistry.

[26]  D. Agard,et al.  The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability , 2004, Protein science : a publication of the Protein Society.

[27]  J. Dame,et al.  Structural insights into the activation of P. vivax plasmepsin. , 2003, Journal of molecular biology.

[28]  D. Kitts,et al.  Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. , 2003, Current pharmaceutical design.

[29]  P. Loll.  Membrane protein structural biology: the high throughput challenge. , 2003, Journal of structural biology.

[30]  R. Vassar,et al.  β-Secretase (BACE) as a drug target for alzheimer’s disease , 2002 .

[31]  Djamel Medjahed,et al.  Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 A in complex with the inhibitors rs367 and rs370. , 2002, Acta crystallographica. Section D, Biological crystallography.

[32]  B. Dunn.  Structure and mechanism of the pepsin-like family of aspartic peptidases. , 2002, Chemical reviews.

[33]  M. Laloi,et al.  Molecular and biochemical characterisation of two aspartic proteinases TcAP1 and TcAP2 from Theobroma cacao seeds , 2002, Planta.

[34]  J. Cooper,et al.  Aspartic proteinases in disease: a structural perspective. , 2002, Current drug targets.

[35]  Robert G. Ridley,et al.  Medical need, scientific opportunity and the drive for antimalarial drugs , 2002, Nature.

[36]  D. Goldberg,et al.  Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets. , 2001, Trends in parasitology.

[37]  J. Falgueyret,et al.  Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. , 2000, European journal of biochemistry.

[38]  C. Dobson,et al.  A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein. , 2000, Biochemistry.

[39]  A Wlodawer,et al.  Structural and biochemical studies of retroviral proteases. , 2000, Biochimica et biophysica acta.

[40]  M. Inouye,et al.  Intramolecular chaperones: polypeptide extensions that modulate protein folding. , 2000, Seminars in cell & developmental biology.

[41]  T. Tanaka,et al.  Contribution of a prosegment lysine residue to the function and structure of porcine pepsinogen A and its active form pepsin A. , 1999, European journal of biochemistry.

[42]  U. Certa,et al.  A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum , 1999, FEBS letters.

[43]  S. Gal,et al.  Plant aspartic proteinases: enzymes on the way to a function , 1999 .

[44]  T. Tanaka,et al.  Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin. , 1998, The Biochemical journal.

[45]  M. Crabbe,et al.  Chymosin and aspartic proteinases , 1998 .

[46]  R E Cachau,et al.  Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[47]  D. Goldberg,et al.  The plasmodium digestive vacuole: metabolic headquarters and choice drug target. , 1995, Parasitology today.

[48]  E. Schiffrin,et al.  Molecular Analysis of Human Prorenin Prosegment Variants in Vitro and in Vivo(*) , 1995, The Journal of Biological Chemistry.

[49]  J. Chirgwin,et al.  The Propeptide Is Nonessential for the Expression of Human Cathepsin D (*) , 1995, The Journal of Biological Chemistry.

[50]  B. Dunn,et al.  High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum , 1994, FEBS letters.

[51]  D A Agard,et al.  Kinetics versus thermodynamics in protein folding. , 1994, Biochemistry.

[52]  G. Koelsch,et al.  Multiple functions of pro‐parts of aspartic proteinase zymogens , 1994, FEBS letters.

[53]  D A Agard,et al.  The role of pro regions in protein folding. , 1993, Current opinion in cell biology.

[54]  F. Sussman,et al.  Conformational instability of the N‐ and C‐terminal lobes of porcine pepsin in neutral and alkaline solutions , 1993, Protein science : a publication of the Protein Society.

[55]  J. Winther,et al.  The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region. , 1993, The Journal of biological chemistry.

[56]  T. Blundell,et al.  Catching a common fold , 1993, Protein science : a publication of the Protein Society.

[57]  G. Conner.  The role of the cathepsin D propeptide in sorting to the lysosome. , 1992, The Journal of biological chemistry.

[58]  S J Remington,et al.  The high‐resolution crystal structure of porcine pepsinogen , 1992, Proteins.

[59]  D. Baker,et al.  A protein-folding reaction under kinetic control , 1992, Nature.

[60]  J. Winther,et al.  Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[61]  Z. Voburka,et al.  Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen , 1991, FEBS letters.

[62]  M. Inouye,et al.  Pro‐peptide as an intermolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro‐peptide , 1991 .

[63]  A. Fedorov,et al.  Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution. , 1990, Journal of molecular biology.

[64]  S. Kent,et al.  Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 protease , 1988, Cell.

[65]  B. Foltmann.  Structure and function of proparts in zymogens for aspartic proteinases. , 1988, Biological chemistry Hoppe-Seyler.

[66]  M. James,et al.  Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution , 1986, Nature.

[67]  J. Ménard,et al.  Inhibition of human renin by synthetic peptides derived from its prosegment. , 1985, The Journal of biological chemistry.

[68]  P. Privalov,et al.  Comparative thermodynamic study of pepsinogen and pepsin structure. , 1981, Journal of molecular biology.

[69]  C. Anfinsen.  Principles that govern the folding of protein chains. , 1973, Science.

[70]  Jun Kong,et al.  MEROPS: the peptidase database. , 2004, Nucleic acids research.

[71]  A. Fersht,et al.  Is there a unifying mechanism for protein folding? , 2003, Trends in biochemical sciences.

[72]  K. Yamauchi,et al.  Bovine lactoferrin and lactoferricin derived from milk: production and applications. , 2002, Biochemistry and cell biology = Biochimie et biologie cellulaire.

[73]  D. Agard,et al.  Two energetically disparate folding pathways of alpha-lytic protease share a single transition state. , 2000, Nature structural biology.

[74]  Robert G. Ridley,et al.  Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum , 1999, Nature Structural Biology.

[75]  D A Agard,et al.  Unfolded conformations of alpha-lytic protease are more stable than its native state. , 1998, Nature.

[76]  R. Kumar,et al.  Stable expression, secretion, and characterization of active human renin in mammalian cells. , 1992, Molecular pharmacology.

[77]  D. Barbano,et al.  Cheese Yield Performance of Fermentation-Produced Chymosin and Other Milk Coagulants , 1992 .

[78]  D. Davies,et al.  The structure and function of the aspartic proteinases. , 1990 .

[79]  J. Ménard,et al.  Synthesis of peptides related to the prosegment of mouse submaxillary gland renin precursor: an approach to renin inhibitors. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[80]  B. Foltmann,et al.  Comparison of the primary structures of acidic proteinases and of their zymogens. , 1977, Advances in experimental medicine and biology.