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biochemistry & molecular biology (35) 35
escherichia-coli (33) 33
fkpa (33) 33
peptidylprolyl cis,trans-isomerase fkpa (29) 29
protein folding (27) 27
index medicus (26) 26
chaperone (18) 18
escherichia coli (17) 17
escherichia coli - metabolism (17) 17
escherichia coli proteins - metabolism (17) 17
escherichia coli - genetics (16) 16
membrane proteins - metabolism (16) 16
peptidylprolyl isomerase - metabolism (16) 16
molecular chaperones - metabolism (15) 15
membrane proteins - genetics (14) 14
microbiology (14) 14
escherichia coli proteins - genetics (13) 13
humans (13) 13
proteins (13) 13
peptidylprolyl isomerase - genetics (12) 12
animals (11) 11
biotechnology & applied microbiology (10) 10
models, molecular (10) 10
molecular chaperones (10) 10
outer-membrane proteins (10) 10
escherichia coli - enzymology (9) 9
peptidylprolyl isomerase - chemistry (9) 9
prolyl isomerase (9) 9
trigger factor (9) 9
amino acid sequence (8) 8
bacteria (8) 8
molecular chaperones - chemistry (8) 8
phage display (8) 8
recombinant proteins - genetics (8) 8
chaperone activity (7) 7
crystal-structure (7) 7
functional expression (7) 7
immunology (7) 7
in-vitro (7) 7
molecular chaperone (7) 7
molecular chaperones - genetics (7) 7
molecular sequence data (7) 7
periplasm - metabolism (7) 7
protein binding (7) 7
protein conformation (7) 7
recombinant proteins (7) 7
research (7) 7
cis,trans-isomerase fkpa (6) 6
dsbc (6) 6
gene expression (6) 6
immunophilins - chemistry (6) 6
immunophilins - genetics (6) 6
immunophilins - metabolism (6) 6
membrane proteins - chemistry (6) 6
periplasm - enzymology (6) 6
protein disulfide-isomerases - genetics (6) 6
protein structure, secondary (6) 6
protein structure, tertiary (6) 6
recombinant proteins - biosynthesis (6) 6
substrate specificity (6) 6
antibodies (5) 5
antibody (5) 5
antibody fragments (5) 5
biotechnology (5) 5
catalysis (5) 5
colicins - metabolism (5) 5
degp (5) 5
disulfide bond formation (5) 5
escherichia coli - drug effects (5) 5
escherichia coli proteins (5) 5
escherichia coli proteins - chemistry (5) 5
in-vivo (5) 5
kinetics (5) 5
mice (5) 5
mip (5) 5
mutation (5) 5
peptide library (5) 5
physiological aspects (5) 5
protein disulfide-isomerases - metabolism (5) 5
solubility (5) 5
sura (5) 5
viral antibodies (5) 5
amino-acid-sequence (4) 4
analysis (4) 4
antibodies - genetics (4) 4
catalytic domain (4) 4
chaperones (4) 4
colicins - chemistry (4) 4
colicins - pharmacology (4) 4
dimerization (4) 4
electrophoresis, polyacrylamide gel (4) 4
enzymes (4) 4
female (4) 4
fkbp (4) 4
fkpa protein (4) 4
high-level expression (4) 4
lipids (4) 4
maltose-binding protein (4) 4
membrane proteins - physiology (4) 4
peptidyl-prolyl cis/trans isomerase (4) 4
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1. Full Text Expression of recombinant antibodies
by Frenzel, André and Hust, Michael and Schirrmann, Thomas
Frontiers in Immunology, ISSN 1664-3224, 2013, Volume 4, p. 217
Recombinant antibodies are highly specific detection probes in research, diagnostics, and have emerged over the last two decades as the fastest growing class... 
Fungi | Yeast | Mammalian cell | Insect cells | Recombinant antibody | Procaryotes | Transgenic organisms | procaryotes | mammalian cell | FV-FC FUSIONS | SINGLE-CHAIN ANTIBODY | HUMAN MONOCLONAL-ANTIBODY | transgenic organisms | IMMUNOLOGY | yeast | HIGH-LEVEL EXPRESSION | fungi | VARIABLE-FRAGMENT SCFV | FED-BATCH CULTURE | TRANSIENT GENE-EXPRESSION | NON-HODGKINS-LYMPHOMA | LINKED IMMUNOSORBENT ASSAYS | recombinant antibody | insect cells | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | transgenic plants | Transgenic Animals | Escherichia coli | Filamentous fungi
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2. Full Text Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein
by Ruiz-Perez, Fernando and Henderson, Ian R and Nataro, James P
Gut Microbes, ISSN 1949-0976, 09/2010, Volume 1, Issue 5
Chaperone | SurA | FkpA | Skp | DegP | YaeT | Autotranspoter | EspP
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3. Full Text Prolyl lsomerization and Its Catalysis in Protein Folding and Protein Function
by Schmidpeter, PAM and Schmid, FX
JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, 04/2015, Volume 427, Issue 7, pp. 1609 - 1631
Prolyl isomerizations are intrinsically slow processes. They determine the rates of many protein folding reactions and control regulatory events in folded... 
CYTOSOLIC BINDING-PROTEIN | FILAMENTOUS PHAGE INFECTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIV-1 CAPSID PROTEIN | protein regulation | ESCHERICHIA-COLI PROTEIN | prolyl isonnerases | folding enzymes | MITOCHONDRIAL PERMEABILITY TRANSITION | CIS-TRANS-ISOMERASE | protein folding | CONSERVED PROLINE SWITCH | C-TERMINAL DOMAIN | chaperones | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | SRC HOMOLOGY-3 DOMAIN
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4. Full Text Control of protein function by prolyl isomerization
by Schmidpeter, Philipp A.M and Koch, Johanna R and Schmid, Franz X
BBA - General Subjects, ISSN 0304-4165, 10/2015, Volume 1850, Issue 10, pp. 1973 - 1982
Background: Prolyl isomerizations have long been known as critical and rate-limiting steps in protein folding. Results: Now it is clear that they are also used... 
Protein regulation | Signaling | Allostery | Protein folding | Prolyl isomerase | CYTOSOLIC BINDING-PROTEIN | N-TERMINAL DOMAINS | PEPTIDE-BONDS | FILAMENTOUS PHAGE INFECTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CIS-TRANS-ISOMERIZATION | ITK SH2 DOMAIN | AMINO-ACID-SEQUENCE | BIOPHYSICS | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | SRC HOMOLOGY-3 DOMAIN | Proline | Isomerization | Proteins
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5. Full Text Engineering toward a bacterial " endoplasmic reticulum" for the rapid expression of immunoglobulin proteins
by Groff, D and Armstrong, S and Rivers, PJ and Zhang, J and Yang, JH and Green, E and Rozzelle, J and Liang, SW and Kittle, JD and Steiner, AR and Baliga, R and Thanos, CD and Hallam, TJ and Sato, AK and Yam, AY
MABS, ISSN 1942-0862, 05/2014, Volume 6, Issue 3, pp. 671 - 678
Antibodies are well-established as therapeutics, and the preclinical and clinical pipeline of these important biologics is growing rapidly. Consequently, there... 
SYSTEM | MEDICINE, RESEARCH & EXPERIMENTAL | CELLS | antibody | strain engineering | OCFS | cell free | ESCHERICHIA-COLI | IgG | rapid | ANTIBODY FRAGMENTS | DsbC | IN-VITRO | COEXPRESSION | chaperone | FkpA | CYTOPLASM | high titer | SECRETION | PEPTIDYL-PROLYL-ISOMERASE
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6. Full Text Engineering toward a bacterial “endoplasmic reticulum” for the rapid expression of immunoglobulin proteins
by Groff, Dan and Armstrong, Stephanie and Rivers, Patrick J and Zhang, Juan and Yang, Junhao and Green, Evan and Rozzelle, James and Liang, Shengwen and Kittle, Joseph D and Steiner, Alexander R and Baliga, Ramesh and Thanos, Christopher D and Hallam, Trevor J and Sato, Aaron K and Yam, Alice Y
mAbs, ISSN 1942-0870, 05/2014, Volume 6, Issue 3, pp. 671 - 678
Antibodies are well-established as therapeutics, and the preclinical and clinical pipeline of these important biologics is growing rapidly. Consequently, there... 
DsbC | antibody | strain engineering | chaperone | Report | OCFS | cell free | FkpA | IgG | rapid | high titer
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7. Full Text Role for Skp in LptD Assembly in Escherichia coli
by Jaclyn Schwalm and Tara F. Mahoney and Garner R. Soltes and Thomas J. Silhavy
Journal of Bacteriology, ISSN 0021-9193, 08/2013, Volume 195, Issue 16, pp. 3734 - 3742
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
OUTER-MEMBRANE PROTEINS | COMPLEX | DOMAIN | BIOGENESIS | FKPA | LIPOPOLYSACCHARIDE | MICROBIOLOGY | PERIPLASMIC CHAPERONE SKP | ENVELOPE STRESS | IDENTIFICATION | DIFFERENTIAL PROTEOMICS | Molecular Chaperones - metabolism | Molecular Chaperones - genetics | Escherichia coli Proteins - metabolism | Cell Membrane - genetics | DNA-Binding Proteins - genetics | Gene Expression Regulation, Bacterial - physiology | DNA-Binding Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Gene Deletion | Alleles | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Cell Membrane - metabolism | Bacterial Outer Membrane Proteins - genetics | Physiological aspects | Research | Molecular chaperones | Escherichia coli | Analysis | Membrane proteins
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8. Full Text Chaperone Domains Convert Prolyl Isomerases into Generic Catalysts of Protein Folding
by Roman P. Jakob and Gabriel Zoldák and Tobias Aumüller and Franz X. Schmid
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2009, Volume 106, Issue 48, pp. 20282 - 20287
The cis/trans isomerization of peptide bonds before proline (prolylbonds) is a rate-limiting step in many protein folding reactions, and it is used to switch... 
Proteins | Enzymes | Protein folding | Protein refolding | Isomerization | Substrate specificity | Escherichia coli | Libraries | Catalysis | Kinetics | Folding catalysis | Folding helpers | Trigger factor | SlyD | Folding mechanism | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | FK506-BINDING PROTEIN | CIS-TRANS-ISOMERIZATION | CIS/TRANS ISOMERIZATION | folding mechanism | trigger factor | BOND ISOMERIZATION | folding helpers | folding catalysis | MOLECULAR CHAPERONE | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | PROLINE ISOMERIZATION | NATIVE-STATE | Humans | Tacrolimus Binding Protein 1A - chemistry | Models, Molecular | Spectrometry, Fluorescence | Substrate Specificity | Protein Structure, Tertiary - genetics | Molecular Chaperones - chemistry | Protein Folding | Peptidylprolyl Isomerase - chemistry | Escherichia coli Proteins - chemistry | Isomerases | Research | Molecular chaperones | Properties | Biological Sciences
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9. Full Text Integrating protein homeostasis strategies in prokaryotes
by Mogk, Axel and Huber, Damon and Bukau, Bernd
Cold Spring Harbor Perspectives in Biology, ISSN 1943-0264, 2011, Volume 3, Issue 4, pp. 1 - 19
Bacterial cells are frequently exposed to dramatic fluctuations in their environment, which cause perturbation in protein homeostasis and lead to protein... 
ESCHERICHIA-COLI PROTEINS | DISULFIDE BOND FORMATION | OUTER-MEMBRANE PROTEINS | TRIGGER FACTOR | IN-VIVO | REDOX-REGULATED CHAPERONE | NEWLY SYNTHESIZED PROTEINS | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | TRANSCRIPTION FACTOR SIGMA | HEAT-SHOCK-PROTEIN | CELL BIOLOGY | Proteins - genetics | Gene Expression Regulation - physiology | Bacteria - metabolism | Proteins - metabolism | Homeostasis - physiology | Protein Folding | 047
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10. Full Text Enhancement of antibody fragment secretion into the Escherichia coli periplasm by co-expression with the peptidyl prolyl isomerase, FkpA, in the cytoplasm
by Levy, Raphael and Ahluwalia, Kiran and Bohmann, David J and Giang, Hoa M and Schwimmer, Lauren J and Issafras, Hassan and Reddy, Nithin B and Chan, Chung and Horwitz, Arnold H and Takeuchi, Toshihiko
Journal of Immunological Methods, ISSN 0022-1759, 08/2013, Volume 394, Issue 1-2, pp. 10 - 21
Improper protein folding or aggregation can frequently be responsible for low expression and poor functional activity of antibody fragments secreted into the... 
Bacteria | Phage display | Chaperones | Cytoplasm | LOCALIZATION | TRIGGER FACTOR | MOLECULAR CHAPERONES | BIOCHEMICAL RESEARCH METHODS | LEVEL | IMMUNOLOGY | FOLDING MODULATORS | MALTOSE-BINDING PROTEIN | CIS,TRANS-ISOMERASE FKPA | FUNCTIONAL EXPRESSION | SKP | Enzyme-Linked Immunosorbent Assay | Immunoglobulin Fab Fragments - metabolism | Membrane Proteins - physiology | Periplasm - metabolism | Peptidylprolyl Isomerase - physiology | Escherichia coli - immunology | Escherichia coli Proteins - physiology | Peptide Library | Protein Folding | Viral antibodies | Antibodies | Escherichia coli
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11. Full Text Folding LacZ in the periplasm of Escherichia coli
by Dwyer, Robert S and Malinverni, Juliana C and Boyd, Dana and Beckwith, Jon and Silhavy, Thomas J
Journal of Bacteriology, ISSN 0021-9193, 2014, Volume 196, Issue 18, pp. 3343 - 3350
Targeted, translational LacZ fusions provided the initial support for the signal sequence hypothesis in prokaryotes and allowed for selection of the mutations... 
OUTER-MEMBRANE-PROTEIN | LOCALIZATION | PROLYL ISOMERASE | GENE | BACTERIOPHAGE-LAMBDA | FKPA | BETA-GALACTOSIDASE | MICROBIOLOGY | MUTATIONS | CHAPERONE | SIGNAL-TRANSDUCTION PATHWAY | Translocation, Genetic | Signal Transduction | Membrane Proteins - genetics | Escherichia coli Proteins - metabolism | Genotype | Recombinant Proteins | Lac Operon - physiology | Gene Expression Regulation, Bacterial - physiology | Protein Folding | Escherichia coli - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Peptidylprolyl Isomerase - metabolism | Membrane Proteins - metabolism | Peptidylprolyl Isomerase - genetics | Physiological aspects | Periplasm | Research | Escherichia coli | Index Medicus
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12. Full Text Engineering toward a bacterial "endoplasmic reticulum" for the rapid expression of immunoglobulin proteins
by Groff, Dan and Armstrong, Stephanie and Rivers, Patrick J and Zhang, Juan and Yang, Junhao and Green, Evan and Rozzelle, James and Liang, Shengwen and Kittle, Joseph D and Steiner, Alexander R and Baliga, Ramesh and Thanos, Christopher D and Hallam, Trevor J and Sato, Aaron K and Yam, Alice Y
mAbs, ISSN 1942-0862, 05/2014, Volume 6, Issue 3, pp. 671 - 678
Antibodies are well-established as therapeutics, and the preclinical and clinical pipeline of these important biologics is growing rapidly. Consequently, there... 
DsbC | antibody | strain engineering | chaperone | OCFS | cell free | FkpA | IgG | rapid | high titer | Antibody | Cell free | Chaperone | Strain engineering | High titer | Rapid | Biotechnology | Molecular Chaperones - metabolism | Protein Disulfide-Isomerases - metabolism | Humans | Endoplasmic Reticulum - metabolism | Immunoglobulins - genetics | Recombinant Proteins - biosynthesis | Antibodies, Monoclonal, Humanized - genetics | Immunoglobulin G - biosynthesis | Antibodies, Monoclonal, Humanized - biosynthesis | Protein Engineering | Immunoglobulins - biosynthesis | Bacteria - metabolism | Endoplasmic Reticulum - genetics | Immunoglobulin G - chemistry | Molecular Chaperones - genetics | Escherichia coli Proteins - metabolism | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Bacteria - genetics | Protein Folding | Immunoglobulins - chemistry | Protein Disulfide-Isomerases - genetics | Immunoglobulin G - genetics | Cell-Free System | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | Trastuzumab | Antibodies, Monoclonal, Humanized - chemistry
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13. Full Text Influence of FkpA variants on survival and replication of Cronobacter spp. in human macrophages
by Eshwar, Athmanya Konegadde and Tasara, Taurai and Stephan, Roger and Lehner, Angelika
Research in Microbiology, ISSN 0923-2508, 04/2015, Volume 166, Issue 3, pp. 186 - 195
Members of the genus are responsible for cases of meningitis and bacteremia with high fatality rates in neonates. Macrophage uptake of invading microbes is an... 
Cronobacter spp | THP-1 | CLSM | Macrophage survival | Virulence factor | FkpA | ENTEROBACTER-SAKAZAKII | GEN. NOV | PROTEIN | ESCHERICHIA-COLI | MICROBIOLOGY | VIRULENCE | INTENSIVE-CARE-UNIT | TURICENSIS | SEQUENCE | RESISTANCE | COMB. NOV | Genes, Bacterial | Macrophages - ultrastructure | Sequence Deletion | Virulence Factors - genetics | Cronobacter - genetics | Humans | Genetic Complementation Test | Sequence Analysis, DNA | Cronobacter - growth & development | Sequence Alignment | Cronobacter - metabolism | Real-Time Polymerase Chain Reaction | Cell Line, Transformed | Macrophages - microbiology | Proteins | Aminoglycosides | Virulence (Microbiology) | Macrophages | Analysis
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14. Full Text Prokaryotic expression of antibodies
by Arbabi-Ghahroudi, Mehdi and Tanha, Jamshid and MacKenzie, Roger
Cancer and Metastasis Reviews, ISSN 0167-7659, 12/2005, Volume 24, Issue 4, pp. 501 - 519
Maximizing the expression yields of recombinant whole antibodies and antibody fragments such as Fabs, single-chain Fvs and single-domain antibodies is highly... 
Medicine & Public Health | Cancer Research | Oncology | bacterial expression of antibodies | recombinant antibodies | tumor-specific antibodies | single domain antibodies | Bacterial expression of antibodies | Single domain antibodies | Tumor-specific antibodies | Recombinant antibodies | HUMAN VH DOMAINS | PHAGE DISPLAY | ESCHERICHIA-COLI EXPRESSION | HEAT-SHOCK PROTEINS | IN-VITRO | MALTOSE-BINDING PROTEIN | ONCOLOGY | SINGLE-CHAIN FV | SMALL RECOGNITION UNITS | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | Immunohistochemistry | Antigen-Antibody Complex | Antibodies - metabolism | Humans | Escherichia coli - immunology | Immunoglobulin Fragments - biosynthesis | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | Recombinant Proteins - isolation & purification | Animals | Escherichia coli - genetics | Escherichia coli - metabolism | Antibodies - genetics | Immunoglobulin Fragments - genetics | Viral antibodies | Antibodies | Escherichia coli
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15. Production systems for recombinant antibodies
by Schirrmann, Thomas and Al-Halabi, Laila and Dübel, Stefan and Hust, Michael
Frontiers in Bioscience, ISSN 1093-9946, 2008, Volume 13, Issue 12, pp. 4576 - 4594
Recombinant antibodies are the fastest growing class of therapeutic proteins. Furthermore, antibodies are key detection reagents in research and diagnostics.... 
Production systems | Yeasts | Gram positive bacteria | Transgenic animals | Escherichia coli | Filamentous fungi | Insect cells | Recombinant antibody | Review | Transgenic plants | Mammalian cells | transgenic plants | filamentous fungi | production systems | FV-FC FUSIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SINGLE-CHAIN ANTIBODY | HUMAN MONOCLONAL-ANTIBODY | FULL-SIZE ANTIBODY | YEAST PICHIA-PASTORIS | CELL BIOLOGY | transgenic animals | INFECTED INSECT CELLS | HIGH-LEVEL EXPRESSION | review | TRANSIENT GENE-EXPRESSION | mammalian cells | recombinant antibody | insect cells | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | Genetic Engineering - methods | Recombinant Fusion Proteins - biosynthesis | Protein Engineering - methods | Animals, Genetically Modified | Cell Physiological Phenomena | Recombinant Proteins - biosynthesis | Fungi - genetics | Gram-Positive Bacteria - genetics | Animals | Plants, Genetically Modified | Cloning, Molecular | Antibody Formation | Antibodies - genetics | Gram-Negative Bacteria - genetics
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16. Full Text Chaperone-assisted thermostability engineering of a soluble T cell receptor using phage display
by Gunnarsen, Kristin S and Gunnarsen, Kristin S and Kristinsson, Solveig G and Kristinsson, Solveig G and Justesen, Sune and Justesen, Sune and Frigstad, Terje and Frigstad, Terje and Buus, Søren and Buus, Søren and Bogen, Bjarne and Bogen, Bjarne and Sandlie, Inger and Sandlie, Inger and Løset, Geir Åge and Løset, Geir Åge
Scientific reports, ISSN 2045-2322, 2013, Volume 3, Issue 1, p. 1162
We here report a novel phage display selection strategy enabling fast and easy selection of thermostabilized proteins. The approach is illustrated with... 
RANDOM MUTAGENESIS | B-CELLS | IN-VITRO | PROTEIN STABILITY | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ANTIBODY LIBRARIES | SELECTION | PEPTIDYLPROLYL CIS,TRANS-ISOMERASE FKPA | DIRECTED EVOLUTION | CELIAC-DISEASE | Cell Line | Receptors, Antigen, T-Cell - chemistry | Molecular Chaperones | Protein Engineering - methods | Receptors, Antigen, T-Cell - metabolism | Membrane Proteins - genetics | Escherichia coli Proteins - metabolism | Peptide Library | Multiple Myeloma - metabolism | Animals | Cell Line, Tumor | Escherichia coli Proteins - genetics | Peptidylprolyl Isomerase - metabolism | Membrane Proteins - metabolism | Mice | Receptors, Antigen, T-Cell - genetics | Peptidylprolyl Isomerase - genetics | Multiple Myeloma - genetics | T-cell receptor | Phage display | Overexpression | T cell receptors | Surface plasmon resonance | Myeloma | Monomers | Thermal stability
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17. Full Text Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa
by Barreteau, Hélène and Tiouajni, Mounira and Graille, Marc and Josseaume, Nathalie and Bouhss, Ahmed and Patin, Delphine and Blanot, Didier and Fourgeaud, Martine and Mainardi, Jean-Luc and Arthur, Michel and Van Tilbeurgh, Herman and Mengin-Lecreulx, Dominique and Touzé, Thierry
Journal of Biological Chemistry, ISSN 0021-9258, 10/2012, Volume 287, Issue 44, pp. 37395 - 37405
Colicin M (ColM) is the only enzymatic colicin reported to date that inhibits cell wall peptidoglycan biosynthesis. It catalyzes the specific degradation of... 
OUTS | EVOLUTION | CRYSTAL-STRUCTURE | BIOSYNTHESIS | FKPA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PEPTIDOGLYCAN PRECURSORS | CATALYTIC DOMAIN | M IMMUNITY PROTEIN | TOXICITY | Bacteriocins - chemistry | Escherichia coli - drug effects | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Pseudomonas aeruginosa - metabolism | Anti-Bacterial Agents - chemistry | Colicins - chemistry | Conserved Sequence | Bacteriocins - metabolism | Amino Acid Sequence | Catalytic Domain | Mutagenesis, Site-Directed | Phosphoric Diester Hydrolases - metabolism | Protein Structure, Secondary | Models, Molecular | Anti-Bacterial Agents - metabolism | Colicins - pharmacology | Phosphoric Diester Hydrolases - chemistry | Peptide Fragments - chemistry | Colicins - metabolism | Bacteriocins - pharmacology | Anti-Bacterial Agents - pharmacology | Phosphoric Diester Hydrolases - pharmacology | Structural Homology, Protein | Amino Acid Substitution | Peptidoglycan | Colicin M | Microbiology | Bacterial Toxins | X-ray Crystallography | Bacteriocin | Pseudomonas aeruginosa | Lipid II | Protein Structure | Phosphodiesterases
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