שרה טייכמן (Hebrew Wikipedia)

Analysis of information sources in references of the Wikipedia article "שרה טייכמן" in Hebrew language version.

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A. B. Makar, K. E. McMartin, M. Palese, T. R. Tephly, Formate assay in body fluids: application in methanol poisoning, Biochemical Medicine 13, 1975-06, עמ' 117–126 doi: 10.1016/0006-2944(75)90147-7
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
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
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
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
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
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
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

nih.gov

pubmed.ncbi.nlm.nih.gov

A. B. Makar, K. E. McMartin, M. Palese, T. R. Tephly, Formate assay in body fluids: application in methanol poisoning, Biochemical Medicine 13, 1975-06, עמ' 117–126 doi: 10.1016/0006-2944(75)90147-7
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
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
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
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
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
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

sciencemag.org

sciencecareers.sciencemag.org

Elisabeth Pain, Harnessing computer power to understand biology, Science, 2015-07-07 doi: 10.1126/science.caredit.a1500172

worldcat.org

Sarah A. Teichmann, Teenage detectives, Berlin, ISBN 3-464-05336-9