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Conserved domains on  [gi|1952961141|ref|XP_038407508|]
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metal transporter CNNM3 isoform X1 [Canis lupus familiaris]

Protein Classification

CBS domain-containing protein( domain architecture ID 10140050)

CBS (cystathione beta synthase) domain-containing protein; the CBS domains may act as regulatory units

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 328-457 1.06e-38

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


:

Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 139.17  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 328 TVEDVLTPLEDCFMLDAGAvLDFGVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 407
Cdd:cd04590     1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952961141 408 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 457
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
 
Name Accession Description Interval E-value
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 328-457 1.06e-38

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 139.17  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 328 TVEDVLTPLEDCFMLDAGAvLDFGVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 407
Cdd:cd04590     1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952961141 408 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 457
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 290-470 2.11e-26

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 112.91  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 290 QLLELAARPGRLRE-------RVLELarggGDpysdlskgvlrcRTVEDVLTPLEDCFMLDAGAVLDfGVLASIMQSGHT 362
Cdd:COG1253   186 ALVEESEESGVIEEeeremieNVFEF----GD------------RTVREVMTPRTDVVALDLDDTLE-EALELILESGHS 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 363 RIPVYEEERSNIVDMLYLKDL--AFVDPEDcTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVnnegeg 440
Cdd:COG1253   249 RIPVYEGDLDDIVGVVHVKDLlrALLEGEP-FDLRDLLR----PPLFVPETKPLDDLLEEFRRERVHMAIV--V------ 315

                         170       180       190
                  ....*....|....*....|....*....|
gi 1952961141 441 DPFYEVLGLVTLEDVIEEIIkSEILDESED 470
Cdd:COG1253   316 DEYGGTAGLVTLEDILEEIV-GEIRDEYDE 344
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
302-478 1.21e-12

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 69.07  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 302 RERVLELARGGG-----DPYS-DLSKGVLRC--RTVEDVLTPLEDCFMLDAGAVLDfGVLASIMQSGHTRIPVYEEERSN 373
Cdd:PRK15094   34 RDELLALIRDSEqndliDEDTrDMLEGVMDIadQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 374 IVDMLYLKDLAFVDPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 451
Cdd:PRK15094  113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                         170       180
                  ....*....|....*....|....*..
gi 1952961141 452 LEDVIEEIIkSEILDESEDYRDATVRK 478
Cdd:PRK15094  181 IEDILELIV-GEIEDEYDEEDDIDFRQ 206
 
Name Accession Description Interval E-value
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 328-457 1.06e-38

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 139.17  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 328 TVEDVLTPLEDCFMLDAGAvLDFGVLASIMQSGHTRIPVYEEERSNIVDMLYLKDLAFVDPEDCTPlsTITRFYNHPLHF 407
Cdd:cd04590     1 TVREVMTPRTDVVALDADA-TLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREK--LDLRALLRPPLF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952961141 408 VFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVTLEDVIE 457
Cdd:cd04590    78 VPETTPLDDLLEEFRKERSHMAIVV--------DEYGGTAGIVTLEDILE 119
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 290-470 2.11e-26

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 112.91  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 290 QLLELAARPGRLRE-------RVLELarggGDpysdlskgvlrcRTVEDVLTPLEDCFMLDAGAVLDfGVLASIMQSGHT 362
Cdd:COG1253   186 ALVEESEESGVIEEeeremieNVFEF----GD------------RTVREVMTPRTDVVALDLDDTLE-EALELILESGHS 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 363 RIPVYEEERSNIVDMLYLKDL--AFVDPEDcTPLSTITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVnnegeg 440
Cdd:COG1253   249 RIPVYEGDLDDIVGVVHVKDLlrALLEGEP-FDLRDLLR----PPLFVPETKPLDDLLEEFRRERVHMAIV--V------ 315

                         170       180       190
                  ....*....|....*....|....*....|
gi 1952961141 441 DPFYEVLGLVTLEDVIEEIIkSEILDESED 470
Cdd:COG1253   316 DEYGGTAGLVTLEDILEEIV-GEIRDEYDE 344
CorB COG4536
Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion ...
 318-480 2.17e-22

Mg2+ and Co2+ transporter CorB, contains DUF21, CBS pair, and CorC-HlyC domains [Inorganic ion transport and metabolism];


Pssm-ID: 443602 [Multi-domain]  Cd Length: 420  Bit Score: 100.54  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 318 DLSKgvlrcRTVEDVLTPLEDCFMLDAGAVLDFgVLASIMQSGHTRIPVYEEERSNIVDMLYLKD-LAFVDPEDCTP--L 394
Cdd:COG4536   200 DLED-----VTVEDIMVPRNEIEGIDLDDPWEE-ILKQLLTSPHTRLPVYRGDIDNIVGVLHVRDlLRALRKGDLSKedL 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 395 STITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIEEIIkSEILDESeDYRDA 474
Cdd:COG4536   274 RKIAR----EPYFIPETTPLSTQLQNFQKRKRRFALV--VDEYG------DVQGLVTLEDILEEIV-GEITDEH-DPDAE 339


                  ....*.
gi 1952961141 475 TVRKKP 480
Cdd:COG4536   340 EIRPQE 345
PRK15094 PRK15094
magnesium/cobalt transporter CorC;
302-478 1.21e-12

magnesium/cobalt transporter CorC;


Pssm-ID: 185050 [Multi-domain]  Cd Length: 292  Bit Score: 69.07  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 302 RERVLELARGGG-----DPYS-DLSKGVLRC--RTVEDVLTPLEDCFMLDAGAVLDfGVLASIMQSGHTRIPVYEEERSN 373
Cdd:PRK15094   34 RDELLALIRDSEqndliDEDTrDMLEGVMDIadQRVRDIMIPRSQMITLKRNQTLD-ECLDVIIESAHSRFPVISEDKDH 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 374 IVDMLYLKDLAFVDPEDCTPLS--TITRfynhPLHFVFNDTKLDAVLEEFKRGKSHLAIVQkvnnegegDPFYEVLGLVT 451
Cdd:PRK15094  113 IEGILMAKDLLPFMRSDAEAFSmdKVLR----QAVVVPESKRVDRMLKEFRSQRYHMAIVI--------DEFGGVSGLVT 180

                         170       180
                  ....*....|....*....|....*..
gi 1952961141 452 LEDVIEEIIkSEILDESEDYRDATVRK 478
Cdd:PRK15094  181 IEDILELIV-GEIEDEYDEEDDIDFRQ 206
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
242-459 6.05e-05

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 44.87  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 242 GSAGLVFLVGEVVPAAVSGRWALALAPRALLLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSK 321
Cdd:COG2524     1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 322 GVLRCRTVEDVLTPleDCFMLDAGAVLdfGVLASIM-QSGHTRIPVYEEERsnIVDMLYLKDLAFVDPEDCTPLS-TITR 399
Cdd:COG2524    81 GLVLKMKVKDIMTK--DVITVSPDTTL--EEALELMlEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDaPVSD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 400 FYNHPLHFVFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGEgdpfyeVLGLVTLEDVIEEI 459
Cdd:COG2524   155 IMTRDVVTVSEDDSLEEALRLMLEHGIGRLPV--VDDDGK------LVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
328-461 1.56e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.08  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 328 TVEDVLTPleDCFMLDAGA-VLDfgVLASIMQSGHTRIPVYEEERsNIVDMLYLKDLAF-VDPEDCTPLST-ITRFYNHP 404
Cdd:COG0517     2 KVKDIMTT--DVVTVSPDAtVRE--ALELMSEKRIGGLPVVDEDG-KLVGIVTDRDLRRaLAAEGKDLLDTpVSEVMTRP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952961141 405 LHFVFNDTKLDAVLEEFKRGK-SHLAIVqkvnnEGEGdpfyEVLGLVTLEDVIEEIIK 461
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKiRRLPVV-----DDDG----RLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 352-456 3.60e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 37.61  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 352 VLASIMQSGHTRIPVYEEErSNIVDMLYLKDLAFVDPEDCTPLSTITRFY-NHPLHFVFNDTKLDAVLEEFKRGK-SHLA 429
Cdd:cd02205    16 ALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPVAEVmTPDVITVSPDTDLEEALELMLEHGiRRLP 94

                          90       100
                  ....*....|....*....|....*..
gi 1952961141 430 IVqkvNNEGEgdpfyeVLGLVTLEDVI 456
Cdd:cd02205    95 VV---DDDGK------LVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
328-457 5.98e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.58  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961141 328 TVEDVLTpLEDCFMLDAGAVLDfGVLASIMQSGHTRIPVYEEERsNIVDMLYLKDLAFVDPEDctplsTITRFYNHPLHF 407
Cdd:COG4109    17 LVEDIMT-LEDVATLSEDDTVE-DALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGKDDDT-----PIEDVMTKNPIT 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952961141 408 VFNDTKLDAVLEEFKRGKSHLAIVqkVNNEGegdpfyEVLGLVTLEDVIE 457
Cdd:COG4109    89 VTPDTSLASAAHKMIWEGIELLPV--VDDDG------RLLGIISRQDVLK 130
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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