pH-induced Conformational Transitions of the Propeptide of Human Cathepsin L (Q60214210)

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Proteolytic processing and physiological regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Potent slow-binding inhibition of cathepsin B by its propeptide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

A covalently trapped folding intermediate of subtilisin E: spontaneous dimerization of a prosubtilisin E Ser49Cys mutant in vivo and its autoprocessing in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Protease pro region required for folding is a potent inhibitor of the mature enzyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Principles that govern the folding of protein chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

A protein-folding reaction under kinetic control

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Energetics of folding subtilisin BPN'

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Abnormal glycosylation of procathepsin L due to N-terminal point mutations correlates with failure to sort to lysosomes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Intracellular targeting of lysosomal cathepsin D in COS cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Secretion and processing mechanisms of procathepsin L in bone resorption

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The proregion of cathepsin L is required for proper folding, stability, and ER exit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Expression of full-length human procathepsin L cDNA in Escherichia coli and refolding of the expression product.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Surface activation of pro-cathepsin L

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Multi-step processing of procathepsin L in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

DNA replication in Physarum polycephalum: characterization of DNA replication products made in vivo in the presence of cycloheximide in strains sensitive and resistant to cycloheximide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Molten globule intermediates and protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Recombinant pro-regions from papain and papaya proteinase IV-are selective high affinity inhibitors of the mature papaya enzymes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Folding of subtilisin BPN': role of the pro-sequence.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Intramolecular chaperones and protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Novel structures CTLA-2 alpha and CTLA-2 beta expressed in mouse activated T cells and mast cells and homologous to cysteine proteinase proregions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Gene structure and 5'-upstream sequence of rat cathepsin L.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

A novel family of cathepsin L-like (CTSLL) sequences on human chromosome 10q and related transcripts.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Role of proteolytic enzymes in biological regulation (a review)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Fluorescence quenching studies of matrix metalloproteinases (MMPs): evidence for structural rearrangement of the proMMP-2/TIMP-2 complex upon mercurial activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Highly ordered molten globule-like state of ovalbumin at acidic pH: native-like fragmentation by protease and selective modification of Cys367 with dithiodipyridine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

A partly Folded State of Acidic Fibroblast Growth Factor at Low Ph

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Characterization of the equilibrium intermediates in acid denaturation of human stefin B

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Structure of the acid state of Escherichia coli ribonuclease HI.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Acid-induced molten globule state of a fully active mutant of human interleukin-6

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Role of electrostatic repulsion in the acidic molten globule of cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded alpha-lactalbumin bound to model membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The 'molten globule' state is involved in the translocation of proteins across membranes?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Tumour necrosis factor is in equilibrium with a trimeric molten globule at low pH

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

The inhibition of cathepsin S by its propeptide--specificity and mechanism of action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498

Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.19.11498