1987 - Member of the National Academy of Sciences
1958 - Fellow of the American Association for the Advancement of Science (AAAS)
His primary scientific interests are in Biochemistry, Fibrin, Tissue transglutaminase, Factor XIII and Enzyme. The concepts of his Biochemistry study are interwoven with issues in Calcium dependent, Calcium and Coagulation. His Fibrin research includes themes of Biophysics, Lysine, Pathology, Stereochemistry and Solubility.
His work deals with themes such as Molecular biology, Peripheral membrane protein and Hereditary Diseases, which intersect with Tissue transglutaminase. His study in Factor XIII is interdisciplinary in nature, drawing from both Covalent bond, Pregnancy, Endocrinology and Zymogen. His Enzyme research is multidisciplinary, incorporating elements of Cell biology, Cross-Linking Reagents and Amine gas treating.
Laszlo Lorand mostly deals with Biochemistry, Tissue transglutaminase, Fibrin, Enzyme and Factor XIII. His research investigates the link between Biochemistry and topics such as Molecular biology that cross with problems in Fibrinolysis and Antibody. Laszlo Lorand has researched Tissue transglutaminase in several fields, including Calcium, Putrescine, Tris and Intracellular, Cell biology.
His study in Fibrin is interdisciplinary in nature, drawing from both Immunoglobulin G, Biophysics, Coagulation, Polymer chemistry and Stereochemistry. In his research, Chromatography is intimately related to Amine gas treating, which falls under the overarching field of Enzyme. His work is dedicated to discovering how Factor XIII, Thrombin are connected with Gel electrophoresis and other disciplines.
Laszlo Lorand mainly focuses on Biochemistry, Tissue transglutaminase, Fibrin, Fibrinogen and Lysine. The study of Biochemistry is intertwined with the study of Alzheimer's disease in a number of ways. His Tissue transglutaminase study is concerned with the field of Enzyme as a whole.
The study incorporates disciplines such as Immunoglobulin G, Antibody and Gel electrophoresis in addition to Fibrin. His studies in Fibrinogen integrate themes in fields like Biophysics, Polymer chemistry, Molecular biology, Fibrinolysis and Thrombin. His Thrombin study incorporates themes from Factor XIII and Coagulation.
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Transglutaminases: crosslinking enzymes with pleiotropic functions
Laszlo Lorand;Robert M. Graham.
Nature Reviews Molecular Cell Biology (2003)
Structural origins of fibrin clot rheology.
Esther A. Ryan;Lyle F. Mockros;John W. Weisel;Laszlo Lorand.
Biophysical Journal (1999)
On the Solubility of Fibrin Clots.
K. Laki;L. Lóránd.
A filter paper assay for transamidating enzymes using radioactive amine substrates
L. Lorand;L.K. Campbell-Wilkes;L. Cooperstein.
Analytical Biochemistry (1972)
Transglutaminases and Disease: Lessons From Genetically Engineered Mouse Models and Inherited Disorders
Siiri E. Iismaa;Bryony M. Mearns;Laszlo Lorand;Robert M. Graham.
Physiological Reviews (2009)
Factor XIII: structure, activation, and interactions with fibrinogen and fibrin.
Annals of the New York Academy of Sciences (2006)
Role of the intrinsic transglutaminase in the Ca2+-mediated crosslinking of erythrocyte proteins
Laszlo Lorand;Lisa B. Weissmann;Debra L. Epel;Joyce Bruner-Lorand.
Proceedings of the National Academy of Sciences of the United States of America (1976)
FIBRINOLIGASE: THE FIBRIN‐STABILIZING FACTOR SYSTEM OF BLOOD PLASMA*
Annals of the New York Academy of Sciences (1972)
Human factor XIII: fibrin-stabilizing factor.
L Lorand;M S Losowsky;K J Miloszewski.
Progress in hemostasis and thrombosis (1980)
Calcium-dependent unmasking of active center cysteine during activation of fibrin stabilizing factor
C. G. Curtis;K. L. Brown;R. B. Credo;R. A. Domanik.
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