Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies.
about
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesisMechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiencyMutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiencyMolybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotidesCell biology and molecular basis of denitrificationA widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolismOn the origin of biochemistry at an alkaline hydrothermal ventMocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coliMutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilizationCrystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coliX-ray crystal structure of the trimeric N-terminal domain of gephyrinInsight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structureMutational Analysis of Escherichia coli MoeA: Two Functional Activities Map to the Active Site Cleft † , ‡Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobAStructural Insights into Putative Molybdenum Cofactor Biosynthesis Protein C (MoaC2) from Mycobacterium tuberculosis H37RvMechanism of pyranopterin ring formation in molybdenum cofactor biosynthesisIdentification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesisThe Pseudomonas aeruginosa lipid A deacylase: selection for expression and loss within the cystic fibrosis airway.Metal insertion into the molybdenum cofactor: product-substrate channelling demonstrates the functional origin of domain fusion in gephyrinThe neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cellsThiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins.Cloning, sequencing and heterologous expression of pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici.The mononuclear molybdenum enzymes.Mutational analysis of the sbo-alb locus of Bacillus subtilis: identification of genes required for subtilosin production and immunity.Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis.Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis.The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli.The tetrahydropyranopterin structure of the sulfur-free and metal-free molybdenum cofactor precursor.Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humansSynthesis of adenylated molybdopterin: an essential step for molybdenum insertion.In vitro molybdenum ligation to molybdopterin using purified components.Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism.The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesisENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications.Pterin chemistry and its relationship to the molybdenum cofactor.Isolation of Salmonella enterica serovar Kentucky strain ST 198 and its H2S-negative variant from a patient: implications for diagnosis.Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology.Complex biotransformations catalyzed by radical S-adenosylmethionine enzymes.Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)A Pterin-Dependent Signaling Pathway Regulates a Dual-Function Diguanylate Cyclase-Phosphodiesterase Controlling Surface Attachment in Agrobacterium tumefaciens.
P2860
Q24295080-ED06A3F0-0CFD-4B7E-A7F5-B1E9DC5479D0Q24301344-E31896E1-FE2E-4DBA-93E5-F731AC79A07AQ24311476-DC3C1CFC-BDF1-4F1F-9F0E-3231F0508761Q24598565-186827A3-2B00-42D3-87A9-BE4F8DFE4EC1Q24643477-0AE4F963-0FE0-41CE-AA90-A12F14EAD511Q24646968-60B5DA09-8A9F-4DAB-8A09-E5289E3A149CQ24648668-E3C2C488-6831-4B4D-B0B4-CC895802FFF0Q24658306-0C006AD2-3497-4D9C-91CF-CA7E391D957AQ24675408-E706F4FB-211E-4B09-9B3A-6AC762651773Q27620990-43777437-68A1-45F7-B5EC-608790CC61AAQ27631420-B5440C87-5478-4A56-9ED2-FE798B74D9A3Q27640918-91139071-002C-4AA0-9E69-4BC38C5E0E78Q27641025-29EB2ADE-5265-420E-959D-0BA694181C58Q27641091-31B547F0-F83A-48D7-B31D-34539A39710CQ27677039-F1E81474-262D-43E9-BFA8-D638230CD0EFQ28261545-35AE8CF5-636F-4E2F-9BA7-7799264AA06CQ28289818-066DBB4B-D962-4A8B-B527-B973E5F84377Q28492613-CDD15C9F-B961-4D3D-8B00-125DDEF9C645Q28582745-44B3712E-DB4F-4D6D-8495-133A4FEDAAFBQ28647110-55BF9108-8915-452B-963B-3B72662F8213Q30689971-42E12CB5-ACEE-43CC-9E75-F050CF420918Q33179012-394BE361-5850-439B-B043-0513B05384B3Q33840734-55B5A1AB-75F8-4ECB-99ED-982C44637E21Q33994182-339C4AA0-59FE-4EB2-A402-B5A1DA24DA12Q34118129-BC7BDA58-78F4-4D3E-8D56-243692F586D6Q34175574-D14A2CEB-0A9E-4722-AC2D-5CC72FEC8E9EQ34209577-4871D3C9-D3D4-4D0F-949E-0D8D6BF128D9Q34294783-E031B84A-74B2-41AC-A155-473A926193DAQ34342036-9A995267-6CB9-4F0A-83C5-32533A1AB4BCQ34361929-BC9877C4-A5C7-4F74-A05B-64FDAA2C7838Q34381641-58A4B54D-2B17-4EE6-8227-D5F4622DF169Q34516717-CA2F9EB5-D958-4D50-AAA8-250767B5DE72Q34529457-419175ED-FD66-4A2C-960B-70A3972045CEQ34989854-D2D7202C-8A34-4902-B1BA-508557CA4C35Q34994479-AB60D04A-B5DD-48F9-9540-033236A264BCQ35036123-FBA9B7A6-B6E2-43D8-A831-EA1E2B914B02Q35063758-72B3DFDE-A364-4D6A-963A-DA754038D1A8Q35182807-4D3A89B5-95FC-479D-B2F0-EB107726E579Q35329323-5BEA8588-7CAC-43C9-8153-9DD25AA722AAQ35809377-0129C95D-43F4-43F7-B107-CD557801F964
P2860
Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Investigation of the early ste ...... e of in vivo labeling studies.
@ast
Investigation of the early ste ...... e of in vivo labeling studies.
@en
Investigation of the early ste ...... e of in vivo labeling studies.
@nl
type
label
Investigation of the early ste ...... e of in vivo labeling studies.
@ast
Investigation of the early ste ...... e of in vivo labeling studies.
@en
Investigation of the early ste ...... e of in vivo labeling studies.
@nl
prefLabel
Investigation of the early ste ...... e of in vivo labeling studies.
@ast
Investigation of the early ste ...... e of in vivo labeling studies.
@en
Investigation of the early ste ...... e of in vivo labeling studies.
@nl
P2860
P356
P1476
Investigation of the early ste ...... e of in vivo labeling studies.
@en
P2093
Rajagopalan KV
Wuebbens MM
P2860
P304
P356
10.1074/JBC.270.3.1082
P407
P577
1995-01-01T00:00:00Z