Question: Protein phosphorylation is a post-translational modification of proteins, was first reported in 1906 by which American biochemist who studied the structure and function of nucleic acids, at the Rockefeller Institute for Medical Research?

full_context: Document 1: Ephraim Levin: Ephraim Y. Levin, born Feb.22, 1933, Baltimore, Maryland. 1957 BA and MA, 1953, MD, 1957, all at Johns Hopkins University. Internship and residencies at Johns Hopkins Hospital and Sinai Hospital of Baltimore. Married Ruth Lee Shefferman June 17, 1956; Four children: Joshua, Rebecca, Daniel, and Michael. Served in USPHS 1953-1998, on active duty 1958-1960 and 1974-1998. With Seymour Kaufman discovered the role of ascorbic acid in the enzymatic hydroxylation of dopamine to form norepinephrine, the first evidence for a specific metabolic function for this vitamin. Fellowship with Konrad Bloch at Harvard University 1961-1963, under auspices of Sinai Hospital. On Faculty of Pediatrics at Johns Hopkins School of Medicine 1963-1974. Along with Vagn Flyger, demonstrated the partial deficiency of uroporphyrinogen cosynthetase in congenital erythropoietic porphyria of cattle and human beings, its occurrence in asymptomatic carriers of the disease, in fibroblasts as well as in bone marrow, and its probable cause of red bones in fox squirrels.
Document 2: Phoebus Levene: Phoebus Aaron Theodore Levene, M.D. (25 February 1869 – 6 September 1940) was an American biochemist who studied the structure and function of nucleic acids. He characterized the different forms of nucleic acid, DNA from RNA, and found that DNA contained adenine, guanine, thymine, cytosine, deoxyribose, and a phosphate group.
Document 3: Protein tyrosine phosphatase: Protein tyrosine phosphatases are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48 ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation, transformation, and synaptic plasticity.
Document 4: Ubiquitin-activating enzyme: Ubiquitin-activating enzymes, also known as E1 enzymes, catalyze the first step in the ubiquitination reaction, which (among other things) can target a protein for degradation via a proteasome. This covalent attachment of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic organisms. Many processes such as cell division, immune responses and embryonic development are also regulated by post-translational modification by ubiquitin and ubiquitin-like proteins.
Document 5: Max Delbrück: Max Ludwig Henning Delbrück, ForMemRS (September 4, 1906 – March 9, 1981), a German–American biophysicist, helped launch the molecular biology research program in the late 1930s. He stimulated physical scientists' interest into biology, especially as to basic research to physically explain genes, mysterious at the time. Formed in 1945 and led by Delbrück along with Salvador Luria and Alfred Hershey, the Phage Group made substantial headway unraveling important aspects of genetics. The three shared the 1969 Nobel Prize in Physiology or Medicine "for their discoveries concerning the replication mechanism and the genetic structure of viruses". He was the first physicist to predict what is now called Delbrück scattering.
Document 6: Phosphorylation: Phosphorylation allows coupling and addition of a phosphoryl group. This particular biochemistry probably represents the origins of catecholamine overload (PO) to a molecule. In biology, phosphorylation and its counterpart, dephosphorylation, are critical for many cellular processes. A large fraction of proteins (between 1/3 to 2/3 of the proteome in eukaryotes ) are temporarily phosphorylated, as are many sugars, lipids, and other molecules. Phosphorylation is especially important for protein function as this modification activates (or deactivates) almost half of the enzymes, thereby regulating their function. Protein phosphorylation is considered the most abundant post-translational modification in eukaryotes.
Document 7: Phosphoproteomics: Phosphoproteomics is a branch of proteomics that identifies, catalogs, and characterizes proteins containing a phosphate group as a post-translational modification. Phosphorylation is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins and therefore cell signalling networks. With all of these modification results, it is estimated that between 30% - 65% of all proteins may be phosphorylated, some multiple times. Based on statistical estimates from many datasets, 230,000 156,000 and 40,000 phosphorylation sites should exist in human, mouse, and yeast, respectively.
Document 8: Francis Crick: Francis Harry Compton Crick (8 June 1916 – 28 July 2004) was a British molecular biologist, biophysicist, and neuroscientist, most noted for being a co-discoverer of the structure of the DNA molecule in 1953 with James Watson, work which was based partly on fundamental studies done by Rosalind Franklin, Raymond Gosling and Maurice Wilkins. Together with Watson and Maurice Wilkins, he was jointly awarded the 1962 Nobel Prize in Physiology or Medicine "for their discoveries concerning the molecular structure of nucleic acids and its significance for information transfer in living material".
Document 9: Protein phosphorylation: Protein phosphorylation is a post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, and tyrosine in eukaryotes, and histidine in prokaryotes, which play important and well-characterized roles in signaling pathways and metabolism. However, many other amino acids can also be phosphorylated, including arginine, lysine, and cysteine. Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered.
Document 10: Protein phosphatase: A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg- or Mn-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. The protein pseudophosphatases form part of the larger phosphatase family, and in most cases are thought to be catalytically inert, instead functioning as phosphate-binding proteins, integrators of signalling or subcellular traps. Examples of membrane-spanning protein phosphatases containing both active (phosphatase) and inactive (pseudophosphatase) domains linked in tandem are known, conceptually similar to the kinase and pseudokinase domain polypeptide structure of the JAK pseudokinases. A complete comparative analysis of human phosphatases and pseudophosphatases has been completed by Manning and colleagues, forming a companion piece to the ground-breaking analysis of the human kinome, which encodes the complete set of ~536 human protein kinases.
Document 11: Karst Hoogsteen: Karst Hoogsteen (October 1, 1923 – August 10, 2015) was a Dutch-born American biochemist famous for noting a new base pairing form in DNA, now called Hoogsteen base pairs. These base pairing intercede in the Watson-Crick base pairing, forging a base pair 'triplex'. The Base Pairs use the N7 nitrogen atom as the accepter rather than the N1 as observed in Watson-Crick base pairing. This leads to a twisted, non-linear arrangement.
Document 12: Avery–MacLeod–McCarty experiment: The Avery–MacLeod–McCarty experiment was an experimental demonstration, reported in 1944 by Oswald Avery, Colin MacLeod, and Maclyn McCarty, that DNA is the substance that causes bacterial transformation, in an era when it had been widely believed that it was proteins that served the function of carrying genetic information (with the very word "protein" itself coined to indicate a belief that its function was "primary"). It was the culmination of research in the 1930s and early 20th Century at the Rockefeller Institute for Medical Research to purify and characterize the "transforming principle" responsible for the transformation phenomenon first described in Griffith's experiment of 1928: killed "Streptococcus pneumoniae" of the virulent strain type III-S, when injected along with living but non-virulent type II-R pneumococci, resulted in a deadly infection of type III-S pneumococci. In their paper ""Studies on the Chemical Nature of the Substance Inducing Transformation of Pneumococcal Types: Induction of Transformation by a Desoxyribonucleic Acid Fraction Isolated from Pneumococcus Type III"", published in the February 1944 issue of the "Journal of Experimental Medicine", Avery and his colleagues suggest that DNA, rather than protein as widely believed at the time, may be the hereditary material of bacteria, and could be analogous to genes and/or viruses in higher organisms.
Document 13: Phenylalanine racemase (ATP-hydrolysing): The enzyme phenylalanine racemase (EC 5.1.1.11 , "phenylalanine racemase", "phenylalanine racemase (adenosine triphosphate-hydrolysing)", "gramicidin S synthetase I") is the enzyme that acts on amino acids and derivatives. It activates both the L & D stereo isomers of phenylalanine to form L-phenylalanyl adenylate and D-phenylalanyl adenylate, which are bound to the enzyme. These bound compounds are then transferred to the thiol group of the enzyme followed by conversion of its configuration, the D-isomer being the more favorable configuration of the two, with a 7 to 3 ratio between the two isomers. The racemisation reaction of phenylalanine is coupled with the highly favorable hydrolysis of adenosine triphosphate (ATP) to adenosine monophosphate (AMP) and pyrophosphate (PP), thermodynamically allowing it to proceed. This reaction is then drawn forward by further hydrolyzing PP to inorganic phosphate (P), via Le Chatelier's principle.
Document 14: Palmitoylation: Palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine and less frequently to serine and threonine residues of proteins, which are typically membrane proteins. The precise function of palmitoylation depends on the particular protein being considered. Palmitoylation enhances the hydrophobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments, as well as in modulating protein–protein interactions. In contrast to prenylation and myristoylation, palmitoylation is usually reversible (because the bond between palmitic acid and protein is often a thioester bond). The reverse reaction is catalysed by palmitoyl protein thioesterases. Because palmitoylation is a dynamic, post-translational process, it is believed to be employed by the cell to alter the subcellular localization, protein–protein interactions, or binding capacities of a protein.
Document 15: James Watson: James Dewey Watson (born April 6, 1928) is an American molecular biologist, geneticist and zoologist, best known as one of the co-discoverers of the structure of DNA in 1953 with Francis Crick and Rosalind Franklin. Watson, Crick, and Maurice Wilkins were awarded the 1962 Nobel Prize in Physiology or Medicine "for their discoveries concerning the molecular structure of nucleic acids and its significance for information transfer in living material".
ground_truth: Phoebus Aaron Theodore Levene