Joachim Stahl

Max Delbrück Center

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H Bielka

Max Delbrück Center

Gudrun Lutsch

Max Delbrück Center

Rainer Benndorf

Temple University

Ulrich‐Axel Bommer

University of Wollongong

D. M. Graifer

Siberian Branch of the Russian Academy of Sciences

Heinz Welfle

Max Delbrück Center

ГГ

Г. Г. Карпова

Siberian Branch of the Russian Academy of Sciences

Matthias Gaestel

Medizinische Hochschule Hannover

Peter Westermann

University of Virginia

K. N. Bulygin

Institute of Chemical Biology and Fundamental Medicine

Cooperative Institutions

Institute of Molecular Biology

Max Delbrück Center

Charité - Universitätsmedizin Berlin

Russian Academy of Sciences

Humboldt-Universität zu Berlin

Siberian Branch of the Russian Academy of Sciences

Institute of Chemical Biology and Fundamental Medicine

Harvard University

Dana-Farber Cancer Institute

Institute of Bioorganic Chemistry

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[A METHOD FOR OBTAINING LONG-CHAIN POLYNUCLEOTIDES WITH POLYNUCLEOTIDE PHOSPHORYLASE FROM MICROCOCCUS LYSODEIKTICUS].

Acta biologica et medica Germanica (1965)

Joachim Stahl W. Heumann

Polynucleotide

Polynucleotide phosphorylase

Micrococcus

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Citations (1)

40 S subunits from rat liver ribosomes contain two codon‐dependent sites for transfer RNA

FEBS Letters (1985)

Yu.P. Semenkov S.V. Kirillov Joachim Stahl

40 S subunits from rat liver ribosomes are able to bind, after heat activation, two molecules of either Phe-tRNAPhe, Ac-Phe-tRNAPhe or deacylated tRNAPhe. Addition of 60 S subunits to the quaternary complex 40 S.poly(U).(Phe-tRNAPhe)2 results in quantitative formation of (Phe)2-tRNAPhe. This indicates that the two binding sites for tRNA on 40 S subunits should be considered as the constituent of P and A sites of 80 S ribosomes.

Protein quaternary structure

10.1016/0014-5793(85)80088-0

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Identification and characterization of heat shock protein 27 protein species in human myocardial two‐dimensional electrophoresis patterns

Electrophoresis (1997)

Christian Scheler Eva‐Christina Müller Joachim Stahl Ursula Müller‐Werdan Johann Salnikow

Abstract Immunostaining of heat shock protein 27 (Hsp27) protein species on two‐dimensional electrophoresis (2‐DE) gels with enhanced sensitivity yields 59 spots reacting with anti‐Hsp27 antibodies. Recombinant Hsp27 exists in 2‐DE as two major protein species which comigrate in the human myocardial pattern with Hsp27 spots C754 and D899 as defined in the heart high‐performance 2‐DE database ( http://www.mdc‐berlin.de/∼emu/heart/ ). Preparative electrophoresis of human myocardial proteins and analysis of the enriched mass range 20–30 kDa by 2‐DE revealed eight protein spots (C438, C582, C658, C697, C754, C595, C750) from the human myocardial database and a new spot not previously detected on silver‐stained gels. These spots were identified as Hsp27 protein species by enzymatic in‐gel‐digestion and analysis by matrix assisted laser desorption‐ionization (MALDI) peptide mass fingerprinting and, in part, MALDI‐post source decay sequencing of single fragments. Possible post‐translational modifications were investigated: immunostaining tests with anti‐phospho‐serine/‐threonine/‐tyrosine antibodies, although positive for other myocardial proteins, were negative for presumed Hsp27 protein species; likewise, periodate‐glycostaining assays and biotinylation screening did not detect modifications in the investigated Hsp27 protein species.

Peptide mass fingerprinting

Hsp27

Immunostaining

Proteome

10.1002/elps.1150181518

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Citations (63)

Ribosomes of rat liver catalyze ‘minimal’ donor reaction

FEBS Letters (1979)

Marina K. Kukhanova Alexander A. Krayevsky B. P. Gottikh Joachim Stahl

Molecular cell biology

10.1016/0014-5793(79)81013-3

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Citations (10)

Studies on the structure of aminal ribosomes. 3. Electron microscopic investigations of isolated rat liver ribosomes and their subunits.

PubMed (1972)

Gudrun Lutsch H Bielka K. Wahn Joachim Stahl

Aminal

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[On the biochemical causes of the cytostatic effect of glyceraldehyde].

PubMed (1967)

P. Langen H. Bielka Joachim Stahl

Glyceraldehyde

Glyceraldehyde 3-phosphate dehydrogenase

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Studies on proteins of animal ribosomes. Affinity labeling of rat liver ribosomes by N‐bromoacetylpuromycin

FEBS Letters (1974)

Joachim Stahl Klaus Dressler H Bielka

10.1016/0014-5793(74)80451-5

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Citations (33)

Human ribosomal protein S3a: cloning of the cDNA and primary structure of the protein

Gene (1992)

Andres Metspalu Ana Rebane Stefan Hoth Margus Pooga Joachim Stahl

Ribosomal protein

Cloning (programming)

Protein primary structure

Human proteins

10.1016/0378-1119(92)90289-2

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Citations (22)

Ribosomal Proteins in Eukaryotes

Encyclopedia of Life Sciences (2001)

Joachim Stahl

Abstract About 80 different ribosomal proteins are imperative for processing and functioning of eukaryotic ribosomes. Most have remained conserved through evolution but several are specific for eukaryotes; some are able to perform extraribosomal functions.

Ribosomal protein

Eukaryotic Ribosome

10.1038/npg.els.0000536

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Citations (0)

CCA paper: A new two-dimensional cyanuric chloride-activated matrix for universal application in molecular biology

Analytical Biochemistry (1986)

Hans-Dieter Hunger Ch. Coutelle G. Behrendt Chr. Flachmeier André Rosenthal

Cyanuric chloride

Electroblotting

10.1016/0003-2697(86)90255-1

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Citations (15)