4.5 Article

Improving the alkaline stability of pepsin through rational protein design using renin, an alkaline-stable aspartic protease, as a structural and functional reference

Related references

Note: Only part of the references are listed.
Article Biotechnology & Applied Microbiology

Comparative bioinformatic and structural analyses of pepsin and renin

Douglas S. A. Grahame et al.

ENZYME AND MICROBIAL TECHNOLOGY (2020)

Article Biochemical Research Methods

STRUM: structure-based prediction of protein stability changes upon single-point mutation

Lijun Quan et al.

BIOINFORMATICS (2016)

Article Biochemical Research Methods

CAPITO-a web server-based analysis and plotting tool for circular dichroism data

Christoph Wiedemann et al.

BIOINFORMATICS (2013)

Article Biochemical Research Methods

SDM-Assist software to design site-directed mutagenesis primers introducing silent restriction sites

Abhijit Karnik et al.

BMC BIOINFORMATICS (2013)

Article Biochemistry & Molecular Biology

H++3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations

Ramu Anandakrishnan et al.

NUCLEIC ACIDS RESEARCH (2012)

Article Biochemistry & Molecular Biology

The Prosegment Catalyzes Pepsin Folding to a Kinetically Trapped Native State

Derek R. Dee et al.

BIOCHEMISTRY (2010)

Article Biotechnology & Applied Microbiology

Pepsin homologues in bacteria

Neil D. Rawlings et al.

BMC GENOMICS (2009)

Article Multidisciplinary Sciences

Rational stabilization of enzymes by computational redesign of surface charge-charge interactions

Alexey V. Gribenko et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)

Article Biochemistry & Molecular Biology

Effect of mutations on the dimer stability and the pH optimum of the human foamy virus protease

Tamas Sperka et al.

PROTEIN ENGINEERING DESIGN & SELECTION (2006)

Article Biochemistry & Molecular Biology

Prediction of protein stability changes for single-site mutations using support vector machines

JL Cheng et al.

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2006)

Article Biochemistry & Molecular Biology

SRide:: a server for identifying stabilizing residues in proteins

C Magyar et al.

NUCLEIC ACIDS RESEARCH (2005)

Article Biochemical Research Methods

Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis

G Candiano et al.

ELECTROPHORESIS (2004)

Article Biochemistry & Molecular Biology

DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data

L Whitmore et al.

NUCLEIC ACIDS RESEARCH (2004)

Article Chemistry, Multidisciplinary

UCSF chimera - A visualization system for exploratory research and analysis

EF Pettersen et al.

JOURNAL OF COMPUTATIONAL CHEMISTRY (2004)

Article Biochemistry & Molecular Biology

Kinetics of the dimerization of retroviral proteases:: The fireman's grip and dimerization

M Ingr et al.

PROTEIN SCIENCE (2003)

Article Biochemistry & Molecular Biology

N-terminal modifications increase the neutral-pH stability of pepsin

BC Bryksa et al.

BIOCHEMISTRY (2003)

Article Biochemistry & Molecular Biology

Structural dissection of alkaline-denatured pepsin

YO Kamatari et al.

PROTEIN SCIENCE (2003)

Review Chemistry, Multidisciplinary

Structure and mechanism of the pepsin-like family of aspartic peptidases

BM Dunn

CHEMICAL REVIEWS (2002)

Review Biochemistry & Molecular Biology

Natively unfolded proteins: A point where biology waits for physics

VN Uversky

PROTEIN SCIENCE (2002)

Review Biochemistry & Molecular Biology

What does it mean to be natively unfolded?

VN Uversky

EUROPEAN JOURNAL OF BIOCHEMISTRY (2002)

Article Biochemistry & Molecular Biology

N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH

T Tanaka et al.

PROTEIN ENGINEERING (2001)