Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes - Test2 - elhamkhani - TriplyDB

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

http://www.wikidata.org/entity/Q24561556

about

Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus.Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2 Methionine aminopeptidase-2 regulates human mesothelioma cell survival: role of Bcl-2 expression and telomerase activity The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis.Inhibition of the methionine aminopeptidase 2 enzyme for the treatment of obesity N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes Structural Analysis of Bengamide Derivatives as Inhibitors of Methionine Aminopeptidases Pyridinylpyrimidines selectively inhibit human methionine aminopeptidase-1 Pyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1 in Cells Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo.Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana Advances in Bacterial Methionine Aminopeptidase Inhibition The class I antigen-processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae Cobalt proteins.Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria.Identification and characterization of three differentially expressed genes, encoding S-adenosylhomocysteine hydrolase, methionine aminopeptidase, and a histone-like protein, in the toxic dinoflagellate Alexandrium fundyense.Amino acid residues involved in the functional integrity of Escherichia coli methionine aminopeptidase.Initiation of protein synthesis in mammalian cells with codons other than AUG and amino acids other than methionine.Posttranslational protein modification in Archaea.Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.Methionine aminopeptidase 2 is a new target for the metastasis-associated protein, S100A4.Impact of the N-terminal amino acid on targeted protein degradation.Discovery of novel antigiardiasis drug candidates.An array of bengamide E analogues modified at the terminal olefinic position: synthesis and antitumor properties.Antimicrosporidial activities of fumagillin, TNP-470, ovalicin, and ovalicin derivatives in vitro and in vivo.Targeted gene disruption of methionine aminopeptidase 2 results in an embryonic gastrulation defect and endothelial cell growth arrest Bacterial protease inhibitors.Bridging of a substrate between cyclodextrin and an enzyme's active site pocket triggers a unique mode of inhibition Methionine aminopeptidases from Mycobacterium tuberculosis as novel antimycobacterial targets A cell cycle-dependent protein serves as a template-specific translation initiation factor.A novel transporter involved in cobalt uptake Zinc is the metal cofactor of Borrelia burgdorferi peptide deformylase.N-terminal protein processing: a comparative proteogenomic analysis.Phosphorylation and dephosphorylation of human myristoyltransferase type 1.

P2860

Q24323068-71DA70E4-AE6C-452F-8D56-90B8720EB28D Q24521506-C998DF4A-B6F3-420F-83E1-15EA5416B4EA Q24597763-D6AC5C23-2EC0-4358-8FE1-5CFE912E364C Q24646329-FCE30843-0447-4E16-922E-4D822AD78BEC Q24684014-A096D693-5B67-4EFF-BFE6-E48714E2FE62 Q24685718-77AE69F0-E315-4587-9DD9-09A78DEFCC2A Q24816633-52AFB193-4034-4FA3-864B-1311569409DC Q26859210-B110D026-C191-4707-B4D4-50BA4A624F51 Q27011436-DCB644DE-A071-42DC-B71E-55A64F208D40 Q27649367-AD1EEDDB-AB6F-4256-B6D9-3D99D649AB57 Q27671657-16B867E2-9E41-4283-A710-892F60E44581 Q27676869-2BB388AA-B532-4216-AAEE-02CD765D808C Q27677949-14622670-6349-4D96-ABFC-4B7EF07ADD33 Q27936010-DB090710-804B-4A0D-83BD-5F362E3E0A98 Q27937078-060CC1A6-CD24-42F5-8075-93D5D613ED10 Q28139711-7C74BA58-CDCB-43A8-89D7-5EAB250A4091 Q28831446-6F438AC1-B659-45C2-83A0-0ED13D411E72 Q30442820-83E572D6-7FB6-488A-B19A-7638F3E66FC8 Q33372298-52099C10-3E56-4AB0-8F4B-CD2890898DD6 Q33548215-D34F55E3-4A1F-407F-8586-DD09B0B9F3DC Q33581798-13894828-66EF-41E7-AEDF-CE9B91B10329 Q33590012-1F89567F-A669-4918-8A85-3F3EB5A05D39 Q33635634-BF9D0DCF-16DD-4E60-9D2D-493A244FF938 Q33777524-AC9998B0-8260-4965-8B19-AC8EEC5B27CF Q33940312-5C5D0357-AEF3-4BEE-B043-88513C005D24 Q33950959-320A1EE2-B5DF-4972-A1C8-A036A5009617 Q34127108-52BBD645-02EA-4B71-A434-BE78DCBD4CFA Q34557941-301E6F9C-7359-432C-A91F-47EEE4791059 Q34597506-1AB6F865-7A06-4B7F-95DA-56E2186EE2BE Q34628149-F5B3BA08-F666-4AB0-ACF5-520FC5BD0580 Q34680610-214A3688-2BA0-4A27-9E61-0FEA167F0A46 Q34687606-83BBFA5D-8633-4ECE-B076-A83B78BFAF65 Q34732982-E40E781D-6642-4B68-AFAD-EB3434F4E833 Q34797798-3F34EBD4-EB83-4B8C-A829-A2CA2D953C9B Q35190496-00E0A6FD-D2DF-4416-ACBC-CDF51C0ADF84 Q35201132-6AF3CA60-8AD7-497C-9AE1-831E20531F44 Q35898630-7D662B79-9BE1-42E9-8D62-F569038761C9 Q36295165-AFB4C916-2BDC-44D6-A8EE-06BF637720AA Q36508107-61C90B7C-9E5A-471B-97F0-4317A15052FE Q36602621-477E13EE-7B6C-46A7-BBA5-B1FF2BFB227A

P2860

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

http://www.wikidata.org/entity/Q24561556

description

1995 nî lūn-bûn

@nan

1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի օգոստոսին 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

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@ast

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@en

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@nl

type

label

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@ast

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@en

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@nl

prefLabel

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@ast

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@en

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@nl

P1433

Q24561556-47304AC6-128D-4389-8CBA-4DB5A593F635

P1476

Q24561556-C2B67A2B-6A7B-4B08-9D3A-67B926AE3062

P2093

Q24561556-2FEADCB7-5863-4E3D-8CB0-3C0B7AD73EDA

Q24561556-4E048AB4-479A-45A0-8BC7-ED88360CB60B

Q24561556-6019FE55-C428-4FF3-A1C0-BB16F1504A7C

Q24561556-6FAB555A-9429-4486-9D31-2613968F535E

Q24561556-B388CB33-4060-451F-BE9F-3CBE568E3A56

Q24561556-B72E5378-7EE9-49D5-BF04-A0447F6294B4

Q24561556-BA83DA94-291D-42FB-B30B-CF0707B57ABC

P2860

Q24561556-09E84777-03C8-4F29-9C33-455CA96D79AF

Q24561556-17BF1A73-FDBF-4F82-B9A3-B47931AEBF35

Q24561556-1FA404AE-2A9E-4048-8110-B1AC7F31B8B3

Q24561556-28004F3C-C305-4E41-9F86-1078B6CE48B2

Q24561556-3600CF98-7081-444E-AC7B-EB251EAE5EC8

Q24561556-38C4BAE3-C386-470A-9DC6-902D28EDDF73

Q24561556-3DCFF4F6-B4CF-4B7F-B2A5-86AFE95B6081

Q24561556-3E191F51-F0E5-4324-BD1D-B7B8955505FC

Q24561556-4244ECC9-58C2-4E47-82CF-34F8F1C818E4

Q24561556-4975266C-BD5E-4EDF-ABAF-BFD1FC7FD3B1

P304

Q24561556-129392C4-23CC-4A7B-BDD4-7F78EB14D343

P31

Q24561556-59069F51-9844-490B-BAA5-BDCE77B62729

P356

Q24561556-3EE389A7-3B6D-42D2-8226-7E86E20EB1AA

P407

Q24561556-8C8B87EE-55C7-4949-8870-2EE4B6A31D9B

P433

Q24561556-BC090206-F539-4D81-9138-B58EC979397C

P478

Q24561556-B03DE239-7780-4EF3-A479-9838F9AF7472

P577

Q24561556-DE789207-482C-4E32-8B7B-61A16CEABF25

P5875

Q24561556-549A673C-DECE-4884-A597-48DA82B10EA5

P698

Q24561556-A151B0BE-BE9C-4287-89FB-EFEE643D9444

P921

Q24561556-af65c3a6-337e-4d2a-b071-7a266e3049c7

P932

Q24561556-F926FDEF-A0EC-472A-A429-595157F534DA

P356

PNAS.92.17.7714

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes

@en

P2093

A E Stewart

http://www.w3.org/2001/XMLSchema#string

B W Matthews

http://www.w3.org/2001/XMLSchema#string

L H Weaver

http://www.w3.org/2001/XMLSchema#string

L Hall

http://www.w3.org/2001/XMLSchema#string

R A Bradshaw

http://www.w3.org/2001/XMLSchema#string

R L Kendall

http://www.w3.org/2001/XMLSchema#string

S M Arfin

http://www.w3.org/2001/XMLSchema#string

P2860

Complete DNA sequence of yeast chromosome II

Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme

Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer

Purification and characterization of a methionine aminopeptidase from Saccharomyces cerevisiae.

A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.

Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease

Primary structure and gene localization of human prolidase

Methionine or not methionine at the beginning of a protein

Structural features in eukaryotic mRNAs that modulate the initiation of translation

Cotranslational amino-terminal processing of cytosolic proteins. Cell-free expression of site-directed mutants of human hemoglobin.

P304

7714-8

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.92.17.7714

http://www.w3.org/2001/XMLSchema#string

P407

P433

17

http://www.w3.org/2001/XMLSchema#string

P478

92

http://www.w3.org/2001/XMLSchema#string

P577

1995-08-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

15553638

http://www.w3.org/2001/XMLSchema#string

P698

7644482

http://www.w3.org/2001/XMLSchema#string

P921

Béésh Łibáhí

P932

41216

http://www.w3.org/2001/XMLSchema#string