1977 - Fellow of the American Association for the Advancement of Science (AAAS)
1975 - Member of the National Academy of Sciences
Robert L. Hill mainly focuses on Biochemistry, Peptide sequence, Enzyme, Agarose and Sialyltransferase. As part of his studies on Biochemistry, Robert L. Hill often connects relevant areas like Thrombin. His Peptide sequence research incorporates themes from Lysozyme, Lactalbumin, Alanine, Sequence analysis and Acyl carrier protein.
His research investigates the link between Sequence analysis and topics such as Hydrolysis that cross with problems in Amino acid. His Agarose research is multidisciplinary, incorporating perspectives in Affinity chromatography and Gel electrophoresis. Robert L. Hill combines subjects such as Fucosyltransferases, Fucose, Glycosylation and Galactoside with his study of Sialyltransferase.
His primary areas of investigation include Biochemistry, Stereochemistry, Enzyme, Amino acid and Peptide sequence. Biochemistry and Molecular biology are commonly linked in his work. His Stereochemistry research is multidisciplinary, incorporating elements of Reactivity, Alpha-lactalbumin, Fumarase and Substrate.
The study incorporates disciplines such as Structural similarity and Guanidine in addition to Enzyme. His Amino acid study incorporates themes from Residue, Peptide and Lysozyme. His work in Peptide sequence tackles topics such as Lactalbumin which are related to areas like Egg white and Lactose.
Robert L. Hill mostly deals with Biochemistry, Mucin, Molecular biology, Threonine and Amino acid. His study brings together the fields of Stereochemistry and Biochemistry. His work deals with themes such as Dimer and EGF-like domain, which intersect with Stereochemistry.
His Mucin study combines topics from a wide range of disciplines, such as Mutant, Transfection and Golgi apparatus, Endoplasmic reticulum, Brefeldin A. His research in Molecular biology intersects with topics in Nucleic acid sequence, Coding region, Complementary DNA, Gene and Exon. His work carried out in the field of Threonine brings together such families of science as Peptide and Glycoprotein.
His primary areas of investigation include Biochemistry, Mucin, Molecular biology, Complementary DNA and Nucleic acid sequence. His Glycoprotein and Peptide sequence study in the realm of Biochemistry connects with subjects such as Tandem repeat and Insulin-like growth factor 2 receptor. His biological study spans a wide range of topics, including Threonine, Serine and Protease.
His studies in Peptide sequence integrate themes in fields like Restriction enzyme and Recognition sequence. His Insulin-like growth factor 2 receptor research spans across into subjects like Receptor, Kupffer cell, Free fatty acid receptor, Edman degradation and Protein primary structure.
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The Structure and Assembly of Secreted Mucins
Juan Perez-Vilar;Robert L. Hill.
Journal of Biological Chemistry (1999)
A possible three-dimensional structure of bovine alpha-lactalbumin based on that of hen's egg-white lysozyme.
W.J. Browne;A.C.T. North;D.C. Phillips;Keith Brew.
Journal of Molecular Biology (1969)
Human Factor XIII from Plasma and Platelets MOLECULAR WEIGHTS, SUBUNIT STRUCTURES, PROTEOLYTIC ACTIVATION, AND CROSS-LINKING OF FIBRINOGEN AND FIBRIN
Martin L. Schwartz;Salvatore V. Pizzo;Robert L. Hill;Patrick A. McKee.
Journal of Biological Chemistry (1973)
Hydrolysis of Proteins
Robert L. Hill.
Advances in Protein Chemistry (1965)
The Effect of Plasmin on the Subunit Structure of Human Fibrin
Salvatore V. Pizzo;Martin L. Schwartz;Robert L. Hill;Patrick A. McKee.
Journal of Biological Chemistry (1972)
The Complete Amino Acid Sequence of Bovine α-Lactalbumin
Keith Brew;Francis J. Castellino;Thomas C. Vanaman;Robert L. Hill.
Journal of Biological Chemistry (1970)
Comparison of the Amino Acid Sequence of Bovine α-Lactalbumin and Hens Egg White Lysozyme
Keith Brew;Thomas C. Vanaman;Robert L. Hill.
Journal of Biological Chemistry (1967)
Sialyl- and fucosyltransferases in the biosynthesis of asparaginyl-linked oligosaccharides in glycoproteins. Mutually exclusive glycosylation by beta-galactoside alpha2 goes to 6 sialyltransferase and N-acetylglucosaminide alpha1 goes to 3 fucosyltransferase.
Paulson Jc;Prieels Jp;Glasgow Lr;Hill Rl.
Journal of Biological Chemistry (1978)
Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae.
L R Glasgow;J C Paulson;R L Hill.
Journal of Biological Chemistry (1977)
Agarose Derivatives of Uridine Diphosphate and N-Acetylglucosamine for the Purification of a Galactosyltransferase
Robert Barker;Kenneth W. Olsen;Joel H. Shaper;Robert L. Hill.
Journal of Biological Chemistry (1972)
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