Amanote Research
Register
Sign In
Discover open access scientific publications
Search, annotate, share and cite publications
Publications by M Kainz
Function of the C-Terminal Domain of the Alpha Subunit of Escherichia Coli RNA Polymerase in Basal Expression and Integration Host Factor-Mediated Activation of the Early Promoter of Bacteriophage Mu.
Journal of Bacteriology
Microbiology
Molecular Biology
Related publications
Escherichia Coli rpoC397 Encodes a Temperature-Sensitive C-Terminal Frameshift in the Beta' Subunit of RNA Polymerase That Blocks Growth of Bacteriophage P2.
Journal of Bacteriology
Microbiology
Molecular Biology
The C-Terminal Domain of the Largest Subunit of RNA Polymerase II and Transcription Initiation.
Molecular and Cellular Biology
Cell Biology
Molecular Biology
RNA Polymerase Alpha Subunit Binding Site in Positively Controlled Promoters: A New Model for RNA Polymerase-Promoter Interaction and Transcriptional Activation in the Escherichia Coli Ada and aidB Genes.
EMBO Journal
Immunology
Molecular Biology
Biochemistry
Microbiology
Neuroscience
Medicine
Genetics
Fine Structure of E. Coli RNA Polymerase-Promoter Interactions: Alpha Subunit Binding to the UP Element Minor Groove
Genes and Development
Genetics
Developmental Biology
The RNA Polymerase Subunit From Sinorhizobium Meliloti Can Assemble With RNA Polymerase Subunits From Escherichia Coli and Function in Basal and Activated Transcription Both in Vivo and in Vitro
Journal of Bacteriology
Microbiology
Molecular Biology
The Early Promoter of Bacteriophage Mu: Definition of the Site of Transcript Initiation
Nucleic Acids Research
Genetics
Structure and Function of the N-Terminal Domain of the Vesicular Stomatitis Virus RNA Polymerase
Journal of Virology
Insect Science
Immunology
Microbiology
Virology
The Regulatory C-Terminal Domain of Subunit of FoF1 ATP Synthase Is Dispensable for Growth and Survival of Escherichia Coli
Journal of Bacteriology
Microbiology
Molecular Biology
The Thioredoxin Binding Domain of Bacteriophage T7 DNA Polymerase Confers Processivity on Escherichia Coli DNA Polymerase I
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
