WorldCat Identities

Kornberg, Roger D.

Overview
Works: 27 works in 50 publications in 1 language and 674 library holdings
Genres: Periodicals 
Roles: Speaker, Editor, Author, Thesis advisor
Publication Timeline
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Most widely held works about Roger D Kornberg
 
Most widely held works by Roger D Kornberg
Nucleosomes by Paul M Wassarman( Book )

11 editions published in 1989 in English and held by 548 WorldCat member libraries worldwide

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences
Chromatin and transcription by Roger D Kornberg( Visual )

2 editions published in 2007 in English and held by 50 WorldCat member libraries worldwide

Annual review of biochemistry( Book )

1 edition published in 2006 in English and held by 15 WorldCat member libraries worldwide

Annual review of biochemistry( Book )

1 edition published in 2010 in English and held by 9 WorldCat member libraries worldwide

Annual review of biochemistry by Roger D Kornberg( Book )

2 editions published in 2007 in English and held by 8 WorldCat member libraries worldwide

Annual review of biochemistry( Book )

1 edition published in 2005 in English and held by 7 WorldCat member libraries worldwide

Methods in enzymology( Book )

6 editions published between 1989 and 2005 in English and Undetermined and held by 5 WorldCat member libraries worldwide

Annual review of biochemistry by Charles C Richardson( Book )

3 editions published between 1932 and 2009 in English and held by 4 WorldCat member libraries worldwide

Annual review of biochemistry by Roger D Kornberg( Book )

2 editions published in 2012 in English and held by 4 WorldCat member libraries worldwide

The diffusion of phospholipids in membranes by Roger D Kornberg( )

3 editions published in 1972 in English and held by 3 WorldCat member libraries worldwide

Single-molecule measurements of transcript elongation and termination by RNA polymerase by Matthew Herbert Larson( )

1 edition published in 2011 in English and held by 2 WorldCat member libraries worldwide

Transcription by RNAP is highly regulated in both prokaryotic and eukaryotic cells, and the ability of the cell to differentiate and respond to its environment is largely due to this regulation. During elongation, for example, RNAP is known to momentarily halt in response to certain cellular signals, and this pause state has been implicated in the regulation of gene expression in both prokaryotic and eukaryotic organisms. In addition, once RNAP reaches the end of a gene, it must reliably terminate and release the newly-transcribed RNA, providing another potential point of regulation within different cell types. Both of these steps are crucial to ensure proper gene expression. In this dissertation, I focus on transcription elongation by both prokaryotic and eukaryotic RNA polymerases, as well as their regulation through pausing and termination. To probe the role of RNA hairpins in transcriptional pausing, a novel single-molecule "RNA-pulling" assay was used to block the formation of secondary structure in the nascent transcript. Force along the RNA did not significantly affect transcription elongation rates, pause frequencies, or pause lifetimes, indicating that short "ubiquitous" pauses are not a consequence of RNA hairpins. Force-based single-molecule techniques were also used to study the mechanism and energetics of transcription termination in bacteria. The data suggest two separate mechanisms for termination: one that involves hypertranslocation of RNAP along the DNA, and one that involves shearing of the RNA:DNA hybrid within the enzyme. In addition, a quantitative energetic model is presented that successfully predicts the termination efficiency of both wild-type and mutant terminators. Finally, the implementation of a novel optical-trapping assay capable of directly observing transcription by eukaryotic RNA polymerase II (RNAPII) molecules is described. This approach was used to probe the RNAPII nucleotide-addition cycle, as well as the role of the trigger loop (a conserved subdomain) in elongation. The results are consistent with a Brownian ratchet model of elongation which incorporates a secondary NTP binding site, and the trigger loop was found to modulate translocation, NTP binding, and catalysis, as well as substrate selection and mismatch recognition by RNAPII
The molecular basis of eukaryotic transcription by Roger D Kornberg( Visual )

2 editions published between 2008 and 2011 in English and held by 2 WorldCat member libraries worldwide

(CIT): A complete RNA polymerase II transcription system has been derived by the fractionation of yeast and mammalian cell extracts. The required polypeptides comprise the 12-subunit RNA polymerase II, multiple "general transcription factors", and a 20-subunit "Mediator". The general transcription factors are responsible for promoter recognition and for melting the DNA template for the initiation of transcription. Mediator makes the key connection between enhancers and promoters. It transduces regulatory information from activator and repressor proteins to RNA polymerase II. Structural studies of the RNA polymerase II transcription machinery began with electron microscope analysis of two-dimensional protein crystals formed on lipid layers. This led to the derivation of a 10-subunit form of RNA polymerase II especially conducive to crystallization, and to the use of two-dimensional crystals as seeds for the growth of large single crystals for X-ray analysis. The large size of the polymerase, over half a million Daltons, presented unusual technical difficulties, eventually overcome, and the structure was determined at 2.8 Angstroms resolution. RNA polymerase II was also crystallized in the form of an actively transcribing complex, containing template DNA and product RNA. The structure of this complex was solved by molecular replacement, revealing the DNA entering and unwinding in the active center cleft. Nine base pairs of DNA-RNA hybrid could be seen extending from the active center at nearly right angles to the entering DNA. Protein-nucleic acid contacts help explain DNA and RNA strand separation, the specificity of RNA synthesis, and RNA and DNA translocation during transcription elongation. RNA polymerase II crystallography has been extended to general transcription factors. The results have been assembled in a preliminary picture of a complete transcription initiation complex. From this picture, principles of both the initiation of transcription. The NIH Director's Wednesday Afternoon Lecture Series includes weekly scientific talks by some of the top researchers in the biomedical sciences worldwide
Yeast RNA polymerase II transcription : structure, mechanism and regulation( Visual )

1 edition published in 1995 in English and held by 2 WorldCat member libraries worldwide

Purification of a promoter-specific and activator-dependent nucleosome disassembly factor by Andreas Ehrensberger( )

1 edition published in 2010 in English and held by 2 WorldCat member libraries worldwide

The disassembly of promoter nucleosomes is a requirement for the activation of eukaryotic genes. It renders the DNA accessible to the transcriptional machinery and primes it for the synthesis of messenger RNA by RNA Polymerase II. Promoter selection is achieved by the activator, a sequence-specific DNA binding protein that recognizes the promoter and recruits the nucleosome disassembly factor. The goals of this project were: 1. To establish an assay that recapitulates promoter-specific and activator-dependent nucleosome disassembly in vitro as it has been observed in vivo. 2. To identify the nucleosome disassembly factor responsible for this activity by purifying it from fractionated crude yeast extract and testing individual fractions using the aforementioned assay. As a model system, I chose the PHO5 promoter from yeast. Its activator, Pho4, is shuttled into the nucleus in response to phosphate starvation, where it binds to the promoter and triggers the disassembly of three nucleosomes. This process has been postulated to require an ATP-dependent nucleosome disassembly factor that is recruited via the activation domain of Pho4. Previous genetic and biochemical experiments have failed at revealing the identity of such a factor. I discovered that an activator-dependent nucleosome disassembly activity can be detected in vitro, that it depends on the activation domain of Pho4, and that it exhibits strong preference for the PHO5 promoter over its open-reading frame. As expected, the activity requires ATP. I developed a chromatographic fractionation protocol through which the activity was purified to a high degree of homogeneity. Mass spectrometry revealed the chromatin-remodeling complex Chd1 and the transcription elongation factor Sub1 to coelute with the activity. Purified Chd1 exhibited nucleosome disassembly activity and a chd1 deletion strain constitutively activated at PHO5 lacked expression of PHO5. These results pave the way for a further characterization of Chd1 in promoter-specific nucleosome disassembly and for the quest for additional stimulatory factors involved in this fundamental biochemical process
Single-molecule studies on transcriptional elongation in prokaryotes and eukaryotes by Jing Zhou( )

1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

Transcription, the process of copying genetic information stored in DNA into RNA, is fundamental to life. It is carried out by an extraordinary nano-machine called RNA polymerase (RNAP). Transcriptional elongation, during which RNAP moves along the DNA, adding one nucleotide at a time to the RNA transcript, is highly dynamic and regulated. The motion of RNAP is discontinuous and interrupted by pauses that play an essential role in gene regulation. Fundamental questions regarding the mechanisms of elongation and its modulation by transcription factors, however, remain unclear. In this dissertation, I focus on using high-resolution, optical trapping techniques to study the mechanisms of transcriptional elongation by both prokaryotic and eukaryotic RNA polymerases at the single-molecule level. First, I describe the studies on how the motion of single E.coli RNAP molecules is modulated by two universally conserved, essential transcription factors (NusA and NusG). From individual transcriptional elongation records, the rates of entering pause states, the pause state lifetimes, and the pause-free elongation speeds can all be extracted. By studying the effects of NusA (and NusG) on these kinetic rates as a function of the applied load, we were able to develop a quantitative kinetic scheme for elongation and pausing. This model not only explains the functions of NusA/NusG, but also provides insight into the mechanism of transcriptional pausing, which had previously been controversial. Second, a novel optical-trapping assay capable of directly probing elongation by individual eukaryotic RNA polymerase II (RNAPII) molecules will be described. We find that the RNAPII trigger loop, an evolutionarily conserved protein subdomain, not only affects each of the three main phases of elongation, namely: substrate binding, translocation, and catalysis; but also plays a critical role in controlling the fidelity of transcription. Our data also support a Brownian ratchet model for elongation which incorporates a secondary nucleotide binding site
Laureate lectures for the Sloan, Kettering, and Mott Prizes for cancer research( Visual )

1 edition published in 2005 in English and held by 1 WorldCat member library worldwide

Annual review of biochemistry by Charles C Richardson( Book )

1 edition published in 2003 in English and held by 1 WorldCat member library worldwide

Basic science, the hope of progress by Roger D Kornberg( Book )

1 edition published in 2010 in English and held by 1 WorldCat member library worldwide

Single-molecule studies of eukaryotic and prokaryotic transcription by Furqan Muhammad Fazal( )

1 edition published in 2015 in English and held by 1 WorldCat member library worldwide

Chromatin and transcription by Roger D Kornberg( )

1 edition published in 2007 in English and held by 1 WorldCat member library worldwide

Audio-visual presentation: Chromatin remodeling for transcription -- The RNA polymerase II transcription machinery -- Mediator of transcriptional regulation -- Atomic structure of RNA polymerase II and of a transcribing complex -- Structural basis of ribonucleotide addition and transcript elongation -- Structure of a complete pre-initiation complex
 
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Annual review of biochemistry
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Annual review of biochemistry
Alternative Names
Kornberg, Roger 1947-...

Kornberg, Roger David 1947-

Rodjer Dévïd Kornberg

Rodžer D. Kornberg

Roger D. Kornberg chimist american

Roger D. Kornberg químic estatunidenc

Roger D. Kornberg químico estadounidense

Roger D. Kornberg US-amerikanischer Biochemiker und Nobelpreisträger für Chemie

Roger D. Kornberg Usana kemiisto

Roger D. Kornberg usona kemiisto

Roger David Kornberg americký chemik

Roger David Kornberg chimico statunitense

Roger Kornberg

Roger Kornberg Amerikaans biochemicus

Roger Kornberg chemik amerykański, noblista

Roger Kornberg chimiste américain

Корнберг, Роджер

Роджер Девід Корнберг

Роджер Дэвид Корнберг

Роџер Д. Корнберг

רוג'ר דויד קורנברג

רוג'ר דויד קורנברג כימאי אמריקאי

راجر ڈی کورنبرگ

راجر کورنبرق

راجر کورنبرگ

روجر كورنبيرغ

روجر كورنبيرغ كيميائي أمريكي

رودجەر دەۆىيد كورنبەرگ

رۆگەر د. کۆرنبەرگ

रोजर डी कोर्नबर्ग

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റോജർ ഡി. കോൺബർഗ്

റോജർ ഡി. കോൺബർഗ് രസതന്ത്രത്തിനുള്ള നോബൽ പുരസ്കാരം നേടിയ അമേരിക്കൻ ശാസ്ത്രജ്ഞന്‍

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English (44)