-
1
-
-
78651189765
-
On the nature of allosteric transition: A plausible model
-
Monod, J., J. Wyman, and J. P. Changeux. 1965. On the nature of allosteric transition: a plausible model. J. Mol. Biol. 12:88-118.
-
(1965)
J. Mol. Biol.
, vol.12
, pp. 88-118
-
-
Monod, J.1
Wyman, J.2
Changeux, J.P.3
-
2
-
-
0014958182
-
Stereochemistry of cooperative effects in haemoglobin
-
Perutz, M. F. 1970. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:726-739.
-
(1970)
Nature
, vol.228
, pp. 726-739
-
-
Perutz, M.F.1
-
3
-
-
0018654083
-
Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
-
Perutz, M. F. 1979. Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. Annu. Rev. Biochem. 48:327-386.
-
(1979)
Annu. Rev. Biochem.
, vol.48
, pp. 327-386
-
-
Perutz, M.F.1
-
4
-
-
33845282119
-
Stereochemistry of cooperative mechanisms in hemoglobin
-
Perutz, M. F., G. Fermi, B. Luisi, B. Shaanan, and R. C. Liddington. 1987. Stereochemistry of cooperative mechanisms in hemoglobin. Acc. Chem. Res. 20:309-321.
-
(1987)
Acc. Chem. Res.
, vol.20
, pp. 309-321
-
-
Perutz, M.F.1
Fermi, G.2
Luisi, B.3
Shaanan, B.4
Liddington, R.C.5
-
5
-
-
0025344693
-
Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide
-
Perutz, M. F. 1990. Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Annu. Rev. Physiol. 52:1-25.
-
(1990)
Annu. Rev. Physiol.
, vol.52
, pp. 1-25
-
-
Perutz, M.F.1
-
6
-
-
0016753485
-
Allosteric interpretation of haemoglobin properties
-
Shulman, R. G., J. J. Hopfield, and S. Ogawa. 1975. Allosteric interpretation of haemoglobin properties. Q. Rev. Biophys. 8:325-420.
-
(1975)
Q. Rev. Biophys.
, vol.8
, pp. 325-420
-
-
Shulman, R.G.1
Hopfield, J.J.2
Ogawa, S.3
-
7
-
-
0037072945
-
2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors
-
2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors. J. Biol. Chem. 277:34508-34520.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 34508-34520
-
-
Yonetani, T.1
Park, S.I.2
Tsuneshige, A.3
Imai, K.4
Kanaori, K.5
-
8
-
-
0038503269
-
Functional and spectroscopic characterization of half-liganded iron-Zinc hybrid hemoglobin: Evidence for conformational plasticity within the T state
-
Samuni, U., L. Juszczak, D. Dantsker, I. Khan, A. J. Friedman, J. Perez-Gonzalez-de-Apodaca, S. Bruno, H. L. Hui, J. E. Colby, E. Karasik, L. D. Kwiatkowski, A. Mozzarelli, R. Noble, and J. M. Friedman. 2003. Functional and spectroscopic characterization of half-liganded iron-Zinc hybrid hemoglobin: evidence for conformational plasticity within the T state. Biochemistry. 42:8272-8288.
-
(2003)
Biochemistry
, vol.42
, pp. 8272-8288
-
-
Samuni, U.1
Juszczak, L.2
Dantsker, D.3
Khan, I.4
Friedman, A.J.5
Perez-Gonzalez-De-Apodaca, J.6
Bruno, S.7
Hui, H.L.8
Colby, J.E.9
Karasik, E.10
Kwiatkowski, L.D.11
Mozzarelli, A.12
Noble, R.13
Friedman, J.M.14
-
9
-
-
1942502768
-
Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: Evidence for long-range communication pathways
-
Peterson, E. S., R. Shinder, I. Khan, L. Juczszak, J. Wang, B. Manjula, S. A. Acharya, C. Bonaventura, and J. M. Friedman. 2004. Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: Evidence for long-range communication pathways. Biochemistry. 43:4832-4843.
-
(2004)
Biochemistry
, vol.43
, pp. 4832-4843
-
-
Peterson, E.S.1
Shinder, R.2
Khan, I.3
Juczszak, L.4
Wang, J.5
Manjula, B.6
Acharya, S.A.7
Bonaventura, C.8
Friedman, J.M.9
-
10
-
-
0015515865
-
X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
-
Arnone, A. 1972. X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin. Nature. 237:146-149.
-
(1972)
Nature
, vol.237
, pp. 146-149
-
-
Arnone, A.1
-
11
-
-
0014214428
-
The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin
-
Benesch, R., and R. E. Benesch. 1967. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. Biophys. Res. Commun. 26:162-167.
-
(1967)
Biochem. Biophys. Res. Commun.
, vol.26
, pp. 162-167
-
-
Benesch, R.1
Benesch, R.E.2
-
12
-
-
0020959160
-
Bezafibrate lowers oxygen affinity of haemoglobin
-
Perutz, M. F., and C. Poyart. 1983. Bezafibrate lowers oxygen affinity of haemoglobin. Lancet. 2:881-882.
-
(1983)
Lancet
, vol.2
, pp. 881-882
-
-
Perutz, M.F.1
Poyart, C.2
-
13
-
-
0018361151
-
Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
-
Baldwin, J., and C. Chothia. 1979. Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129:175-220.
-
(1979)
J. Mol. Biol.
, vol.129
, pp. 175-220
-
-
Baldwin, J.1
Chothia, C.2
-
14
-
-
0016756387
-
Proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water
-
Fung, L. W.-M., and C. Ho. 1975. Proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water. Biochemistry. 14:2526-2535.
-
(1975)
Biochemistry
, vol.14
, pp. 2526-2535
-
-
Fung, L.W.-M.1
Ho, C.2
-
15
-
-
0026619765
-
Proton nuclear magnetic resonance studies on hemoglobin: Cooperative interactions and partially ligated intermediates
-
Ho, C. 1992. Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates. Adv. Protein Chem. 43:192-214.
-
(1992)
Adv. Protein Chem.
, vol.43
, pp. 192-214
-
-
Ho, C.1
-
16
-
-
0037064138
-
Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-Å resolution. A novel allosteric binding site in R-state hemoglobin
-
Shibayama, N., S. Miura, R. H. J. Tame, T. Yonetani, and S.-Y. Park. 2002. Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-Å resolution. A novel allosteric binding site in R-state hemoglobin. J. Biol. Chem. 277:38791-38796.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 38791-38796
-
-
Shibayama, N.1
Miura, S.2
Tame, R.H.J.3
Yonetani, T.4
Park, S.-Y.5
-
17
-
-
0002052550
-
Biological applications of raman spectroscopy
-
T. G. Spiro, editor. John Wiley & Sons, New York
-
Kitagawa, T. 1988. Biological applications of raman spectroscopy. In Biological Applications of Raman Spectroscopy, Vol. 3. T. G. Spiro, editor. John Wiley & Sons, New York. 97-131.
-
(1988)
Biological Applications of Raman Spectroscopy
, vol.3
, pp. 97-131
-
-
Kitagawa, T.1
-
18
-
-
0033596899
-
New light on allostery: Dynamic resonance Raman spectroscopy of hemoglobin Kempsey
-
Hu, X., K. R. Rodgers, I. Mukerji, and T. G. Spiro. 1999. New light on allostery: dynamic resonance Raman spectroscopy of hemoglobin Kempsey. Biochemistry. 38:3462-3467.
-
(1999)
Biochemistry
, vol.38
, pp. 3462-3467
-
-
Hu, X.1
Rodgers, K.R.2
Mukerji, I.3
Spiro, T.G.4
-
19
-
-
0027993426
-
Nanosecond dynamics of the R→T transition in hemoglobin: Ultraviolet Raman studies
-
Rodgers, K. R., and T. G. Spiro. 1994. Nanosecond dynamics of the R→T transition in hemoglobin: ultraviolet Raman studies. Science. 265:1697-1699.
-
(1994)
Science
, vol.265
, pp. 1697-1699
-
-
Rodgers, K.R.1
Spiro, T.G.2
-
20
-
-
0028936429
-
Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan β37 mutant
-
Nagai, M., S. Kaminaka, Y. Ohba, Y. Nagai, Y. Mizutani, and T. Kitagawa. 1995. Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan β37 mutant. J. Biol. Chem. 270:1636-1642.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 1636-1642
-
-
Nagai, M.1
Kaminaka, S.2
Ohba, Y.3
Nagai, Y.4
Mizutani, Y.5
Kitagawa, T.6
-
21
-
-
0033604830
-
Quaternary structure sensitive tyrosine residues in human hemoglobin: UV resonance Raman studies of mutants at α140, α35, and β145 tyrosine
-
Nagai, M., H. Wajcman, A. Lahary, T. Nakatsukasa, S, Nagatomo, and T. Kitagawa. 1999. Quaternary structure sensitive tyrosine residues in human hemoglobin: UV resonance Raman studies of mutants at α140, α35, and β145 tyrosine. Biochemistry. 38:1243-1251.
-
(1999)
Biochemistry
, vol.38
, pp. 1243-1251
-
-
Nagai, M.1
Wajcman, H.2
Lahary, A.3
Nakatsukasa, T.4
Nagatomo, S.5
Kitagawa, T.6
-
22
-
-
0016861436
-
The effects of inositol hexaphosphate on the allosteric properties of two beta-99-substituted abnormal hemoglobins, hemoglobin Yakima and hemoglobin Kempsey
-
Nagai, M., M. Nishibu, Y. Sugita, Y. Yoneyama, R. T. Jones, and S. Gordon. 1975. The effects of inositol hexaphosphate on the allosteric properties of two beta-99-substituted abnormal hemoglobins, hemoglobin Yakima and hemoglobin Kempsey. J. Biol. Chem. 250:3169-3173.
-
(1975)
J. Biol. Chem.
, vol.250
, pp. 3169-3173
-
-
Nagai, M.1
Nishibu, M.2
Sugita, Y.3
Yoneyama, Y.4
Jones, R.T.5
Gordon, S.6
-
23
-
-
0000909290
-
Novel spinning cell system for UVRR measurements of powder and small-volume solution samples in back-scattering geometry: Application to solid tryptophan and mutant hemoglobin solution
-
Kaminaka, S., and T. Kitagawa. 1995. Novel spinning cell system for UVRR measurements of powder and small-volume solution samples in back-scattering geometry: application to solid tryptophan and mutant hemoglobin solution. Appl. Spectrosc. 49:685-687.
-
(1995)
Appl. Spectrosc.
, vol.49
, pp. 685-687
-
-
Kaminaka, S.1
Kitagawa, T.2
-
24
-
-
0001068250
-
Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase
-
Ogura, T., S. Takahashi, S. Hirota, K. Shinzawa-Itoh, S. Yoshikawa, E. Appelman, and T. Kitagawa. 1993. Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase. J. Am. Chem. Soc. 115:8527-8536.
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 8527-8536
-
-
Ogura, T.1
Takahashi, S.2
Hirota, S.3
Shinzawa-Itoh, K.4
Yoshikawa, S.5
Appelman, E.6
Kitagawa, T.7
-
25
-
-
0001591573
-
A novel idea for practical UV resonance Raman measurement with a double monochromator and its application to protein structural studies
-
Kaminaka, S., and T. Kitagawa. 1992. A novel idea for practical UV resonance Raman measurement with a double monochromator and its application to protein structural studies, Appl. Spectrosc. 4:1804-1808.
-
(1992)
Appl. Spectrosc.
, vol.4
, pp. 1804-1808
-
-
Kaminaka, S.1
Kitagawa, T.2
-
26
-
-
0035756040
-
Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy
-
Mizutani, Y., and T. Kitagawa. 2001. Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy. Chem. Rec. 1:258-275.
-
(2001)
Chem. Rec.
, vol.1
, pp. 258-275
-
-
Mizutani, Y.1
Kitagawa, T.2
-
27
-
-
0035829917
-
Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy
-
Mizutani, Y., and T. Kitagawa. 2001. Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy. J. Phys. Chem. B. 105:10992-10999.
-
(2001)
J. Phys. Chem. B
, vol.105
, pp. 10992-10999
-
-
Mizutani, Y.1
Kitagawa, T.2
-
28
-
-
0031272781
-
Developments of widely tunable light sources for picosecond time-resolved resonance Raman spectroscopy
-
Uesugi, Y., Y. Mizutani, and T. Kitagawa. 1997. Developments of widely tunable light sources for picosecond time-resolved resonance Raman spectroscopy. Rev. Sci. Instrum. 68:4001-4008.
-
(1997)
Rev. Sci. Instrum.
, vol.68
, pp. 4001-4008
-
-
Uesugi, Y.1
Mizutani, Y.2
Kitagawa, T.3
-
29
-
-
0027818118
-
Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes
-
Hu, S., I. K. Morris, J. P. Singh, K. M. Smith, and T. G. Spiro. 1993. Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes. J. Am. Chem. Soc. 115:12446-12458.
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 12446-12458
-
-
Hu, S.1
Morris, I.K.2
Singh, J.P.3
Smith, K.M.4
Spiro, T.G.5
-
30
-
-
0030467166
-
Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
-
Hu, S., K. M. Smith, and T. G. Spiro. 1996. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118:12638-12646.
-
(1996)
J. Am. Chem. Soc.
, vol.118
, pp. 12638-12646
-
-
Hu, S.1
Smith, K.M.2
Spiro, T.G.3
-
31
-
-
0027194971
-
Nonexponential protein relaxation: Dynamics of conformational change in myoglobin
-
Lim, M., T. A. Jackson, and P. A. Anfinrud. 1993. Nonexponential protein relaxation: dynamics of conformational change in myoglobin. Proc. Natl. Acad. Sci. USA. 90:5801-5804.
-
(1993)
Proc. Natl. Acad. Sci. USA
, vol.90
, pp. 5801-5804
-
-
Lim, M.1
Jackson, T.A.2
Anfinrud, P.A.3
-
32
-
-
0027190494
-
Nonexponential relaxation after ligand dissociation from myoglobin: A molecular dynamics simulation
-
Kuczera, K., J.-C. Lambry, J.-L. Martin, and M. Karplus. 1993. Nonexponential relaxation after ligand dissociation from myoglobin: a molecular dynamics simulation. Proc. Natl. Acad. Sci. USA. 90:5805-5807.
-
(1993)
Proc. Natl. Acad. Sci. USA
, vol.90
, pp. 5805-5807
-
-
Kuczera, K.1
Lambry, J.-C.2
Martin, J.-L.3
Karplus, M.4
-
34
-
-
0020462757
-
Transient Raman study of hemoglobin: Structural dependence of the iron-histidine linkage
-
Friedman, J. M., D. L. Rousseau, M. R. Ondrias, and R. A. Stepnoski. 1982. Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage. Science. 218:1244-1246.
-
(1982)
Science
, vol.218
, pp. 1244-1246
-
-
Friedman, J.M.1
Rousseau, D.L.2
Ondrias, M.R.3
Stepnoski, R.A.4
-
36
-
-
0019191241
-
Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxy-haemoglobin studied by resonance Raman scattering
-
Nagai, K., T. Kitagawa, and H. Morimoto. 1980. Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxy-haemoglobin studied by resonance Raman scattering. J. Mol. Biol. 136:271-289.
-
(1980)
J. Mol. Biol.
, vol.136
, pp. 271-289
-
-
Nagai, K.1
Kitagawa, T.2
Morimoto, H.3
-
37
-
-
0001291195
-
Raman and ultraviolet resonance raman spectra of proteins and related compounds
-
R. J. H. Clark and R. E. Hester, editors. John, Wiley & Sons, New York
-
Harada, I., and H. Takeuchi. 1986. Raman and ultraviolet resonance raman spectra of proteins and related compounds. In Spectroscopy of Biological Systems. R. J. H. Clark and R. E. Hester, editors. John, Wiley & Sons, New York. 113-175.
-
(1986)
Spectroscopy of Biological Systems
, pp. 113-175
-
-
Harada, I.1
Takeuchi, H.2
-
38
-
-
0033790875
-
Heme structure of hemoglobin M Iwate [α87(F8)His → Tyr]: A UV and visible resonance Raman study
-
Nagai, M., M. Aki, R. Li, Y. Jin, H. Sakai, S. Nagatomo, and T. Kitagawa. 2000. Heme structure of hemoglobin M Iwate [α87(F8)His → Tyr]: a UV and visible resonance Raman study. Biochemistry. 39:13093-13105.
-
(2000)
Biochemistry
, vol.39
, pp. 13093-13105
-
-
Nagai, M.1
Aki, M.2
Li, R.3
Jin, Y.4
Sakai, H.5
Nagatomo, S.6
Kitagawa, T.7
-
39
-
-
0033609452
-
UV resonance Raman studies of α-nitrosyl hemoglobin derivatives: Relation between the α1-β2 subunit interface interactions and the Fe-histidine bonding of α heme
-
Nagatomo, S., M. Nagai, A. Tsuneshige, T. Yonetani, and T. Kitagawa. 1999. UV resonance Raman studies of α-nitrosyl hemoglobin derivatives: relation between the α1-β2 subunit interface interactions and the Fe-histidine bonding of α heme. Biochemistry. 38:9659-9666.
-
(1999)
Biochemistry
, vol.38
, pp. 9659-9666
-
-
Nagatomo, S.1
Nagai, M.2
Tsuneshige, A.3
Yonetani, T.4
Kitagawa, T.5
-
40
-
-
0037031126
-
Differences in changes of the α1-β2 subunit contacts between ligand binding to the α and β subunits of hemoglobin A: UV resonance Raman analysis using Ni-Fe hybrid
-
Nagatomo, S., M. Nagai, N. Shibayama, and T. Kitagawa. 2002. Differences in changes of the α1-β2 subunit contacts between ligand binding to the α and β subunits of hemoglobin A: UV resonance Raman analysis using Ni-Fe hybrid. Biochemistry. 41:10010-10020.
-
(2002)
Biochemistry
, vol.41
, pp. 10010-10020
-
-
Nagatomo, S.1
Nagai, M.2
Shibayama, N.3
Kitagawa, T.4
-
42
-
-
0035849542
-
Protein conformation change of myoglobin upon ligand binding probed by ultraviolet resonance Raman spectroscopy
-
Haruta, N., M. Aki, S. Ozaki, Y. Watanabe, and T. Kitagawa. 2001. Protein conformation change of myoglobin upon ligand binding probed by ultraviolet resonance Raman spectroscopy. Biochemistry. 40:6956-6963.
-
(2001)
Biochemistry
, vol.40
, pp. 6956-6963
-
-
Haruta, N.1
Aki, M.2
Ozaki, S.3
Watanabe, Y.4
Kitagawa, T.5
-
43
-
-
0001314221
-
The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin
-
Adair, G. S. 1925. The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin. J. Biol. Chem. 63:529-545.
-
(1925)
J. Biol. Chem.
, vol.63
, pp. 529-545
-
-
Adair, G.S.1
-
44
-
-
0000977357
-
Allosteric linkage
-
Wyman, J. 1967. Allosteric linkage. J. Am. Chem. Soc. 89:2202-2218.
-
(1967)
J. Am. Chem. Soc.
, vol.89
, pp. 2202-2218
-
-
Wyman, J.1
|