שרה טייכמן
הערות שוליים

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1 2  M. M. Ris, R. A. Deitrich, J. P. Von Wartburg, Inhibition of aldehyde reductase isoenzymes in human and rat brain, Biochemical Pharmacology 24, 1975-10-15, עמ' 1865–1869 doi: 10.1016/0006-2952(75)90405-0
1 2  A. E. Halaris, K. T. Belendiuk, D. X. Freedman, Antidepressant drugs affect dopamine uptake, Biochemical Pharmacology 24, 1975-10-15, עמ' 1896–1897 doi: 10.1016/0006-2952(75)90412-8
1 2  J. M. Stein, The effect of adrenaline and of alpha- and beta-adrenergic blocking agents on ATP concentration and on incorporation of 32Pi into ATP in rat fat cells, Biochemical Pharmacology 24, 1975-09-15, עמ' 1659–1662 doi: 10.1016/0006-2952(75)90002-7
↑  O. Isaac, K. Thiemer, [Biochemical studies on camomile components/III. In vitro studies about the antipeptic activity of (--)-alpha-bisabolol (author's transl)], Arzneimittel-Forschung 25, 1975-09, עמ' 1352–1354
↑  M. Ardenne, P. G. Reitnauer, [Demonstration of tumor inhibiting properties of a strongly immunostimulating low-molecular weight substance. Comparative studies with ifosfamide on the immuno-labile DS carcinosarcoma. Stimulation of the autoimmune activity for approx. 20 days by BA 1, a N-(2-cyanoethylene)-urea. Novel prophylactic possibilities], Arzneimittel-Forschung 25, 1975-09, עמ' 1369–1379
↑  H. Flohr, W. Breull, Effect of etafenone on total and regional myocardial blood flow, Arzneimittel-Forschung 25, 1975-09, עמ' 1400–1403
1 2 3 4  H. Kröger, I. Donner, G. Skiello, Influence of a new virostatic compound on the induction of enzymes in rat liver, Arzneimittel-Forschung 25, 1975-09, עמ' 1426–1429
↑  R. R. Scherberger, H. Kaess, S. Brückner, [Studies on the action of an anticholinergic agent in combination with a tranquilizer on gastric juice secretion in man], Arzneimittel-Forschung 25, 1975-09, עמ' 1460–1463
↑  S. Maneksha, T. V. Harry, Lorazepam in sexual disorders, The British Journal of Clinical Practice 29, 1975-07, עמ' 175–176
↑  P. D. Mier, J. J. van den Hurk, Lysosomal hydrolases of the epidermis. I. Glycosidases, The British Journal of Dermatology 93, 1975-07, עמ' 1–10 doi: 10.1111/j.1365-2133.1975.tb06468.x
↑  P. D. Mier, J. J. van den Hurk, Lysosomal hydrolases of the epidermis. 2. Ester hydrolases, The British Journal of Dermatology 93, 1975-10, עמ' 391–398 doi: 10.1111/j.1365-2133.1975.tb06512.x
↑  M. L. Beck, B. Freihaut, R. Henry, S. Pierce, A serum haemagglutinating property dependent upon polycarboxyl groups, British Journal of Haematology 29, 1975-01, עמ' 149–156 doi: 10.1111/j.1365-2141.1975.tb01808.x
↑  C. W. Garner, F. J. Behal, Effect of pH on substrate and inhibitor kinetic constants of human liver alanine aminopeptidase. Evidence for two ionizable active center groups, Biochemistry 14, 1975-11-18, עמ' 5084–5088 doi: 10.1021/bi00694a009
↑  T. Sanner, Formation of transient complexes in the glutamate dehydrogenase catalyzed reaction, Biochemistry 14, 1975-11-18, עמ' 5094–5098 doi: 10.1021/bi00694a011
↑  R. Roskoski, C. T. Lim, L. M. Roskoski, Human brain and placental choline acetyltransferase: purification and properties, Biochemistry 14, 1975-11-18, עמ' 5105–5110 doi: 10.1021/bi00694a013
↑  V. M. Bhagwat, B. V. Ramachandran, Malathion A and B esterases of mouse liver-I, Biochemical Pharmacology 24, 1975-09-15, עמ' 1713–1717 doi: 10.1016/0006-2952(75)90011-8
↑  E. Stellwagen, J. Babul, Stabilization of the globular structure of ferricytochrome c by chloride in acidic solvents, Biochemistry 14, 1975-11-18, עמ' 5135–5140 doi: 10.1021/bi00694a018
↑  R. G. Duggleby, H. Kaplan, A competitive labeling method for the determination of the chemical properties of solitary functional groups in proteins, Biochemistry 14, 1975-11-18, עמ' 5168–5175 doi: 10.1021/bi00694a023
↑  H. F. Gilbert, M. H. O'Leary, Modification of arginine and lysine in proteins with 2,4-pentanedione, Biochemistry 14, 1975-11-18, עמ' 5194–5199 doi: 10.1021/bi00694a027
↑  D. L. Peterson, J. M. Gleisner, R. L. Blakley, Bovine liver dihydrofolate reductase: purification and properties of the enzyme, Biochemistry 14, 1975-12-02, עמ' 5261–5267 doi: 10.1021/bi00695a005
↑  P. McPhie, The origin of the alkaline inactivation of pepsinogen, Biochemistry 14, 1975-12-02, עמ' 5253–5256 doi: 10.1021/bi00695a003
↑  D. Baccanari, A. Phillips, S. Smith, D. Sinski, Purification and properties of Escherichia coli dihydrofolate reductase, Biochemistry 14, 1975-12-02, עמ' 5267–5273 doi: 10.1021/bi00695a006
↑  F. C. Hartman, G. M. LaMuraglia, Y. Tomozawa, R. Wolfenden, The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group, Biochemistry 14, 1975-12-02, עמ' 5274–5279 doi: 10.1021/bi00695a007
1 2  J. C. Jaton, H. Huser, D. G. Braun, D. Givol, Conformational changes induced in a homogeneous anti-type III pneumococcal antibody by oligosaccharides of increasing size, Biochemistry 14, 1975-12-02, עמ' 5312–5315 doi: 10.1021/bi00695a014
↑  S. R. Fahnestock, Evidence of the involvement of a 50S ribosomal protein in several active sites, Biochemistry 14, 1975-12-02, עמ' 5321–5327 doi: 10.1021/bi00695a016
↑  T. R. Anderson, T. A. Slotkin, Maturation of the adrenal medulla--IV. Effects of morphine, Biochemical Pharmacology 24, 1975-08-15, עמ' 1469–1474 doi: 10.1016/0006-2952(75)90020-9
↑  Y. W. Chow, R. Pietranico, A. Mukerji, Studies of oxygen binding energy to hemoglobin molecule, Biochemical and Biophysical Research Communications 66, 1975-10-27, עמ' 1424–1431 doi: 10.1016/0006-291x(75)90518-5
↑  M. C. van Dam-Mieras, A. J. Slotboom, W. A. Pieterson, G. H. de Haas, The interaction of phospholipase A2 with micellar interfaces. The role of the N-terminal region, Biochemistry 14, 1975-12-16, עמ' 5387–5394 doi: 10.1021/bi00696a001
↑  B. Renaud, M. Buda, B. D. Lewis, J. F. Pujol, Effects of 5,6-dihydroxytryptamine on tyrosine-hydroxylase activity in central catecholaminergic neurons of the rat, Biochemical Pharmacology 24, 1975-09-15, עמ' 1739–1742 doi: 10.1016/0006-2952(75)90018-0
↑  A. Schmoldt, H. F. Benthe, G. Haberland, Digitoxin metabolism by rat liver microsomes, Biochemical Pharmacology 24, 1975-09-01, עמ' 1639–1641
↑  J. K. Martin, M. G. Luthra, M. A. Wells, R. P. Watts, Phospholipase A2 as a probe of phospholipid distribution in erythrocyte membranes. Factors influencing the apparent specificity of the reaction, Biochemistry 14, 1975-12-16, עמ' 5400–5408 doi: 10.1021/bi00696a003
↑  K. S. Bose, R. H. Sarma, Delineation of the intimate details of the backbone conformation of pyridine nucleotide coenzymes in aqueous solution, Biochemical and Biophysical Research Communications 66, 1975-10-27, עמ' 1173–1179 doi: 10.1016/0006-291x(75)90482-9
↑  Elisabeth Pain, Harnessing computer power to understand biology, Science, 2015-07-07 doi: 10.1126/science.caredit.a1500172
↑  Sarah A. Teichmann, Teenage detectives, Berlin, ISBN 3-464-05336-9
↑  J. C. Cassatt, C. P. Marini, J. W. Bender, The reversible reduction of horse metmyoglobin by the iron(II) complex of trans-1,2-diaminocyclohexane-N,N,N,n-tetraacetate, Biochemistry 14, 1975-12-16, עמ' 5470–5475 doi: 10.1021/bi00696a014
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בקרת זהויות :  NLI: 987007297440705171  PLWABN: 9810589247505606  ACM DL: 81100561207  dblp: 90/4458  GND: 1209177935  ISNI: 0000 0001 1646 3358  LCCN: n2019180430  MGP: 254860  ORCID: 0000-0002-6294-6366  S2AuthorId: 3334474  VIAF: 54870541   WorldCat (עם VIAF): 54870541