The role of pro regions in protein folding

Current Opinion in Cell Biology

Volumn 5, Issue 6, 1993, Pages 966-970

  Baker, David ^a   Shiau, Andrew K ^a   Agard, David A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME PRECURSOR; PROTEINASE; PROTEINASE INHIBITOR;

AMINO TERMINAL SEQUENCE; EVOLUTION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN TRANSPORT; REVIEW;

BACTERIAL PROTEINS; ENDOPEPTIDASES; ENZYME PRECURSORS; EVOLUTION; KINETICS; PROTEASE INHIBITORS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0027485469     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/0955-0674(93)90078-5     Document Type: Article

References (33)

1. Molecular Analysis of the Gene Encoding α-Lytic Protease: Evidence for a Preproenzyme
2. Requirement of Pro-Sequence for the Production of Active Subtilisin E in Escherichia coli
3. Analysis of Prepro-α-Lyric Protease Expression in Escherichia coli Reveals that the Pro Region is Required for Activity
4. The α-Lytic Protease Pro-Region Does not Require a Physical Linkage to Activate the Protease Domain in Vivo
5. Protcase Pro Region Required for Folding is a Potent Inhibitor of the Mature Enzyme
6. Pro-Sequence of Subtilisin Can Guide the Refolding of Denatured Subtilisin in an Intermolecular Process
7. Propeptide of Carboxypeptidase Y Provides a Chaperone-Like Function as Well as inhibition of the Enzymatic Activity
8. A non-covalent NH2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence inEscherichia coli
9. Role of the Proregion in the Production and Secretion of the Yarrowia lipolytica Alkaline Extracellular Protease
10. Processing of the Papain Precursor. Purification of the Zymogen and Characterization of Its Mechanism of Processing
11. Production of Crystallizable Cruzain, the Major Cysteine Protease from Trypanosoma cruzi
12. Activity and Deletion Analysis of Recombinant Human Cathepsin L Expressed in Escherichia coli
13. Yeast Carboxypeptidase Y Vacuolar Targeting Signal is Defined by Four Propeptide Amino Acids
14. Intracellular Transit of a Yeast Protease is Rescued by rans-Complementation with its Prodomain
15. Correct Folding of α-Lytic Protease is Required for Its Extracellular Secretion from Escherichia coli
16. Pro-Peptide as an Intramolecular Chaperone: Renaturation of Denatured Subtilisin E with a Synthetic ProPeptide
17. Inhibition of Aspartic Proteinases by Propart Peptides of Human Procathepsin D and Chicken Pepsinogen
18. The Severed Activation Segment of Porcine Pancreatic Procarboxypeptidase A is a Powerful Inhibitor of the Active Enzyme. Isolation and Characterisation of the Activation Peptide
19. Potent Slow-Binding Inhibition of Cathepsin B by Its Propeptide
20. Mechanisms of Zymogen Activation
21. Introduction of a Cysteine Protease Active Site into Trypsin
22. Chaperorons: Helpers Along the Pathways to Protein Folding
23. To Fold or Not to Fold
24. A Protein-Folding Reaction under Kinetic Control
25. Folding of Subtilisin BPN′: Characterization of a Folding Intermediate
26. Catalysis of a Protein Folding Reaction: Thermodynamic and Kinetic Analysis of Subtilisin BPN Interactions with Its Propeptide Fragment
27. Energetics of Folding Subtilisin BPN′
28. Functional Analysis of the Intramolecular Chaperone. Mutational Hot Spots in the Subtilisin Pro-Peptide and a Second-Site Suppressor Mutation within the Subtilisin Molecule
29. 1 Pro-Regions in Homodimer Assembly
30. Identification and Analysis of Discrete Functional Domains in the Pro Region of Pre-Pro-Transforming Growth Factor β1
31. The pro domain of pre-pro-transforming growth factor .beta.1 when independently expressed is a functional binding protein for the mature growth factor
32. The Pro Region of BPTI Facilitates Folding
33. Principles that Govern the Folding of Protein Chains