相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。Introducing Lasso Peptides as Molecular Scaffolds for Drug Design: Engineering of an Integrin Antagonist
Thomas A. Knappe et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2011)
The Antibacterial Threaded-lasso Peptide Capistruin Inhibits Bacterial RNA Polymerase
Konstantin Kuznedelov et al.
JOURNAL OF MOLECULAR BIOLOGY (2011)
Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides
Severine Zirah et al.
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY (2011)
Computational design of the lasso peptide antibiotic microcin J25
Si Jia Pan et al.
PROTEIN ENGINEERING DESIGN & SELECTION (2011)
The Engineering of an Orally Active Conotoxin for the Treatment of Neuropathic Pain
Richard J. Clark et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2010)
An Experimental and Computational Investigation of Spontaneous Lasso Formation in Microcin J25
Andrew L. Ferguson et al.
BIOPHYSICAL JOURNAL (2010)
High-Resolution Crystal Structure of a Lasso Peptide
Herbert Nar et al.
CHEMMEDCHEM (2010)
The glucagon receptor antagonist BI-32169 constitutes a new class of lasso peptides
Thomas A. Knappe et al.
FEBS LETTERS (2010)
Much of the Microcin J25 Leader Peptide is Dispensable
Wai Ling Cheung et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2010)
Lys17 in the 'lasso' peptide lariatin A is responsible for anti-mycobacterial activity
Masato Iwatsuki et al.
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS (2009)
How Bugs Make Lassos
K. Johan Rosengren et al.
CHEMISTRY & BIOLOGY (2009)
Insights into the Biosynthesis and Stability of the Lasso Peptide Capistruin
Thomas A. Knappe et al.
CHEMISTRY & BIOLOGY (2009)
The Ile13 residue of microcin J25 is essential for recognition by the receptor FhuA, but not by the inner membrane transporter SbmA
Sergio B. Socias et al.
FEMS MICROBIOLOGY LETTERS (2009)
Systematic structure-activity analysis of microcin J25
Olga Pavlova et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Isolation and structural characterization of capistruin, a lasso peptide predicted from the genome sequence of Burkholderia thailandensis E264
Thomas A. Knappe et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2008)
Two enzymes catalyze the maturation of a lasso peptide in Escherichia coli
Sophie Duquesne et al.
CHEMISTRY & BIOLOGY (2007)
Lariatins, novel anti-mycobacterial peptides with a lasso structure, produced by Rhodococcus jostii K01-B0171
Masato Iwatsuki et al.
JOURNAL OF ANTIBIOTICS (2007)
Low-molecular-weight post-translationally modified microcins
Konstantin Severinov et al.
MOLECULAR MICROBIOLOGY (2007)
Maturation of McjA precursor peptide into active microcin MccJ25
David J. Clarke et al.
ORGANIC & BIOMOLECULAR CHEMISTRY (2007)
NMR as a tool for elucidating the structures of circular and knotted proteins
David J. Craik et al.
MOLECULAR BIOSYSTEMS (2007)
The synthesis, structural characterization, and receptor specificity of the α-conotoxin Vc1.1
Richard J. Clark et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Lariatins, antimycobacterial peptides produced by Rhodococcus sp K01-B0171, have a lasso structure
Masato Iwatsuki et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2006)
MccJ25 C-terminal is involved in RNA-polymerase inhibition but not in respiration inhibition
PA Vincent et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2005)
An asymmetric ion channel derived from gramicidin A - Synthesis, function and NMR structure
XL Xie et al.
FEBS JOURNAL (2005)
Structure of thermolysin cleaved microcin J25: Extreme stability of a two-chain antimicrobial peptide devoid of covalent links
KJ Rosengren et al.
BIOCHEMISTRY (2004)
BI-32169, a bicyclic 19-peptide with strong glucagon receptor antagonist activity from Streptomyces sp.
O Potterat et al.
JOURNAL OF NATURAL PRODUCTS (2004)
Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel
J Mukhopadhyay et al.
MOLECULAR CELL (2004)
Microcin J25, from the macrocyclic to the lasso structure:: Implications for biosynthetic, evolutionary and biotechnological perspectives
S Rebuffat et al.
CURRENT PROTEIN & PEPTIDE SCIENCE (2004)
Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail
KA Wilson et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)
Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone
KJ Rosengren et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)
Structure of antibacterial peptide microcin J25: A 21-residue lariat protoknot
MJ Bayro et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2003)
NMR Spectroscopy techniques for screening and identifying ligand binding to protein receptors
B Meyer et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2003)
Mutations of bacterial RNA polymerase leading to resistance to microcin J25
J Yuzenkova et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity
A Blond et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2002)
Propeptin, a new inhibitor of prolyl endopeptidase produced by Microbispora - II. Determination of chemical structure
Y Esumi et al.
JOURNAL OF ANTIBIOTICS (2002)
Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
MA Delgado et al.
JOURNAL OF BACTERIOLOGY (2001)
Solution structure of microcin J25, the single macrocyclic antimicrobial peppide from Escherichia coli
A Blond et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2001)
Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization
LZ Yan et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2001)